entry created 2012-04-18 dataset Swiss-Prot modified 2022-12-14 version 58 accession Q6SW81 accession D2K3L8 name NEC2_HCMVM protein recommendedName fullName evidence 2 Nuclear-egress-protein-2 gene name evidence 2 type primary NEC2 name type ordered-locus UL50 organism name type scientific Human-cytomegalovirus-(strain-Merlin) name type common HHV-5 name type synonym Human-herpesvirus-5 dbReference id 295027 type NCBI-Taxonomy lineage taxon Viruses taxon Duplodnaviria taxon Heunggongvirae taxon Peploviricota taxon Herviviricetes taxon Herpesvirales taxon Herpesviridae taxon Betaherpesvirinae taxon Cytomegalovirus organismHost name type scientific Homo-sapiens name type common Human dbReference id 9606 type NCBI-Taxonomy reference key 1 citation date 2004 first 1301 last 1312 name J.-Gen.-Virol. type journal-article volume 85 title Genetic-content-of-wild-type-human-cytomegalovirus. authorList person name Dolan-A. person name Cunningham-C. person name Hector-R.D. person name Hassan-Walker-A.F. person name Lee-L. person name Addison-C. person name Dargan-D.J. person name McGeoch-D.J. person name Gatherer-D. person name Emery-V.C. person name Griffiths-P.D. person name Sinzger-C. person name McSharry-B.P. person name Wilkinson-G.W.G. person name Davison-A.J. dbReference id 15105547 type PubMed dbReference id 10.1099/vir.0.79888-0 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] reference evidence 5 key 2 citation date 2015 first 27452 last 27458 name J.-Biol.-Chem. type journal-article volume 290 title Crystal-Structure-of-the-Human-Cytomegalovirus-pUL50-pUL53-Core-Nuclear-Egress-Complex-Provides-Insight-into-a-Unique-Assembly-Scaffold-for-Virus-Host-Protein-Interactions. authorList person name Walzer-S.A. person name Egerer-Sieber-C. person name Sticht-H. person name Sevvana-M. person name Hohl-K. person name Milbradt-J. person name Muller-Y.A. person name Marschall-M. dbReference id 26432641 type PubMed dbReference id 10.1074/jbc.c115.686527 type DOI scope X-RAY-CRYSTALLOGRAPHY-(2.44-ANGSTROMS)-OF-1-175 scope INTERACTION-WITH-NEC1 comment type function text evidence 2 Plays-an-essential-role-in-virion-nuclear-egress,-the-first-step-of-virion-release-from-infected-cell.-Within-the-host-nucleus,-NEC1-interacts-with-the-newly-formed-capsid-through-the-vertexes-and-directs-it-to-the-inner-nuclear-membrane-by-associating-with-NEC2.-Induces-the-budding-of-the-capsid-at-the-inner-nuclear-membrane-as-well-as-its-envelopment-into-the-perinuclear-space.-There,-the-NEC1/NEC2-complex-promotes-the-fusion-of-the-enveloped-capsid-with-the-outer-nuclear-membrane-and-the-subsequent-release-of-the-viral-capsid-into-the-cytoplasm-where-it-will-reach-the-secondary-budding-sites-in-the-host-Golgi-or-trans-Golgi-network. comment type subunit text evidence 2-4 Forms-a-heterohexameric-complex-with-NEC1. comment type subcellular-location subcellularLocation location evidence 2 Host-nucleus-inner-membrane topology evidence 2 Single-pass-membrane-protein text evidence 2 Localizes-also-at-the-transient-membrane-of-perinuclear-virions. comment type PTM text evidence 1-2 Phosphorylated-(By-similarity).-Phosphorylation-by-viral-kinase-UL97-at-Ser-216-plays-an-important-role-for-correct-viral-nuclear-egress-complex-(NEC)-localization-(By-similarity). comment type similarity text evidence 2 Belongs-to-the-herpesviridae-NEC2-protein-family. dbReference id AY446894 type EMBL property type protein-sequence-ID value AAR31616.1 property type molecule-type value Genomic_DNA dbReference id YP_081509.1 type RefSeq property type nucleotide-sequence-ID value NC_006273.2 dbReference id 5D5N type PDB property type method value X-ray property type resolution value 2.44-A property type chains value A=1-175 dbReference id 5D5N type PDBsum dbReference id Q6SW81 type SMR dbReference id 3077439 type DNASU dbReference id 3077439 type GeneID dbReference id vg:3077439 type KEGG dbReference id R-HSA-9609690 type Reactome property type pathway-name value HCMV-Early-Events dbReference id R-HSA-9610379 type Reactome property type pathway-name value HCMV-Late-Events dbReference id UP000000938 type Proteomes property type component value Genome dbReference id GO:0044201 type GO property type term value C:host-cell-nuclear-inner-membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0016020 type GO property type term value C:membrane property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0019033 type GO property type term value C:viral-tegument property type evidence value ECO:0000304 property type project value Reactome dbReference id GO:0046765 type GO property type term value P:viral-budding-from-nuclear-membrane property type evidence value ECO:0000314 property type project value UniProtKB dbReference id MF_04024 type HAMAP property type entry-name value HSV_NEC2 property type match-status value 1 dbReference id IPR007626 type InterPro property type entry-name value Herpesvirus_viron_egress-type dbReference id PF04541 type Pfam property type entry-name value Herpes_U34 property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0002 3D-structure keyword id KW-1043 Host-membrane keyword id KW-1048 Host-nucleus keyword id KW-0426 Late-protein keyword id KW-0472 Membrane keyword id KW-0597 Phosphoprotein keyword id KW-1185 Reference-proteome keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix feature description Nuclear-egress-protein-2 id PRO_0000416719 type chain location begin position 1 end position 398 feature description Perinuclear-space evidence 2 type topological-domain location begin position 1 end position 359 feature description Helical evidence 2 type transmembrane-region location begin position 360 end position 382 feature description Nuclear evidence 2 type topological-domain location begin position 383 end position 398 feature description Disordered evidence 3 type region-of-interest location begin position 202 end position 246 feature description Disordered evidence 3 type region-of-interest location begin position 306 end position 334 feature description Pro-residues evidence 3 type compositionally-biased-region location begin position 213 end position 227 feature description Phosphoserine evidence 1 type modified-residue location position position 216 feature evidence 6 type helix location begin position 5 end position 19 feature evidence 6 type helix location begin position 23 end position 25 feature evidence 6 type strand location begin position 26 end position 28 feature evidence 6 type helix location begin position 31 end position 36 feature evidence 6 type strand location begin position 42 end position 47 feature evidence 6 type helix location begin position 55 end position 66 feature evidence 6 type strand location begin position 71 end position 76 feature evidence 6 type strand location begin position 81 end position 88 feature evidence 6 type strand location begin position 102 end position 106 feature evidence 6 type strand location begin position 111 end position 114 feature evidence 6 type helix location begin position 116 end position 122 feature evidence 6 type strand location begin position 126 end position 128 feature evidence 6 type strand location begin position 130 end position 137 feature evidence 6 type strand location begin position 139 end position 142 feature evidence 6 type strand location begin position 144 end position 152 feature evidence 6 type helix location begin position 156 end position 169 evidence key 1 type ECO:0000250 source dbReference id P16791 type UniProtKB evidence key 2 type ECO:0000255 source dbReference id MF_04024 type HAMAP-Rule evidence key 3 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 4 type ECO:0000269 source dbReference id 26432641 type PubMed evidence key 5 type ECO:0007744 source dbReference id 5D5N type PDB evidence key 6 type ECO:0007829 source dbReference id 5D5N type PDB sequence checksum 367FF459968AD468 length 398 mass 43052 modified 2004-07-05 version 1 MEMNKVLHQDLVQATRRILKLGPSELRVTDAGLICKNPNYSVCDAMLKTDTVYCVEYLLSYWESRTDHVPCFIFKNTGCAVSLCCFVRAPVKLVSPARHVGEFNVLKVNESLIVTLKDIEEIKPSAYGVLTKCVVRKSNSASVFNIELIAFGPENEGEYENLLRELYAKKAASTSLAVRNHVTVSSHSGSGPSLWRARMSAALTRTAGKRSPRTASPPPPPPRHPSCSPTMVAAGGAAAGPRPPPPPMAAGSWRLCRCEACMGRCGCASEGDADEEEEELLALAGEGKAAAAAAGQDIGGSARRPLEEHVSRRRGVSTHHRHPPSPPCTPSLERTGYRWAPSSWWRARSGPSRPQSGPWLPARFATLGPLVLALLLVLALLWRGHGQSSSPTRSAHRD 
entry created 2012-05-16 dataset Swiss-Prot modified 2023-02-22 version 91 accession Q97Y84 name CAS1B_SACS2 protein recommendedName fullName evidence 1 CRISPR-associated-endonuclease-Cas1-2 ecNumber evidence 1 3.1.-.- gene name evidence 1 type primary cas1-2 name type ordered-locus SSO1450 organism name type scientific Saccharolobus-solfataricus-(strain-ATCC-35092-/-DSM-1617-/-JCM-11322-/-P2) name type common Sulfolobus-solfataricus dbReference id 273057 type NCBI-Taxonomy lineage taxon Archaea taxon Crenarchaeota taxon Thermoprotei taxon Sulfolobales taxon Sulfolobaceae taxon Saccharolobus reference key 1 citation date 2001 first 7835 last 7840 name Proc.-Natl.-Acad.-Sci.-U.S.A. type journal-article volume 98 title The-complete-genome-of-the-crenarchaeon-Sulfolobus-solfataricus-P2. authorList person name She-Q. person name Singh-R.K. person name Confalonieri-F. person name Zivanovic-Y. person name Allard-G. person name Awayez-M.J. person name Chan-Weiher-C.C.-Y. person name Clausen-I.G. person name Curtis-B.A. person name De-Moors-A. person name Erauso-G. person name Fletcher-C. person name Gordon-P.M.K. person name Heikamp-de-Jong-I. person name Jeffries-A.C. person name Kozera-C.J. person name Medina-N. person name Peng-X. person name Thi-Ngoc-H.P. person name Redder-P. person name Schenk-M.E. person name Theriault-C. person name Tolstrup-N. person name Charlebois-R.L. person name Doolittle-W.F. person name Duguet-M. person name Gaasterland-T. person name Garrett-R.A. person name Ragan-M.A. person name Sensen-C.W. person name Van-der-Oost-J. dbReference id 11427726 type PubMed dbReference id 10.1073/pnas.141222098 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain ATCC-35092-/-DSM-1617-/-JCM-11322-/-P2 reference key 2 citation date 2009 first 1928 last 1932 name FEBS-Lett. type journal-article volume 583 title SSO1450--a-CAS1-protein-from-Sulfolobus-solfataricus-P2-with-high-affinity-for-RNA-and-DNA. authorList person name Han-D. person name Lehmann-K. person name Krauss-G. dbReference id 19427858 type PubMed dbReference id 10.1016/j.febslet.2009.04.047 type DOI scope FUNCTION scope SUBUNIT scope DNA-BINDING scope RNA-BINDING source strain ATCC-35092-/-DSM-1617-/-JCM-11322-/-P2 reference key 3 citation date 2015 first 0 last 0 name Elife type journal-article volume 4 title Intrinsic-sequence-specificity-of-the-Cas1-integrase-directs-new-spacer-acquisition. authorList person name Rollie-C. person name Schneider-S. person name Brinkmann-A.S. person name Bolt-E.L. person name White-M.F. dbReference id 26284603 type PubMed dbReference id 10.7554/elife.08716 type DOI scope FUNCTION scope MUTAGENESIS-OF-GLU-142 source strain ATCC-35092-/-DSM-1617-/-JCM-11322-/-P2 comment type function text evidence 1 CRISPR-(clustered-regularly-interspaced-short-palindromic-repeat),-is-an-adaptive-immune-system-that-provides-protection-against-mobile-genetic-elements-(viruses,-transposable-elements-and-conjugative-plasmids).-CRISPR-clusters-contain-spacers,-sequences-complementary-to-antecedent-mobile-elements,-and-target-invading-nucleic-acids.-CRISPR-clusters-are-transcribed-and-processed-into-CRISPR-RNA-(crRNA).-Acts-as-a-dsDNA-endonuclease.-Involved-in-the-integration-of-spacer-DNA-into-the-CRISPR-cassette. comment type function text evidence 2-3 In-vitro-catalyzes-a-concerted-transesterification-reaction-on-branched-DNA,-as-would-be-expected-during-integration-of-protospacers-into-the-CRISPR-leader-sequence;-Cas2-is-not-required-in-vitro.-This-reaction-requires-a-3'-OH-group-at-the-branch-point-(PubMed:26284603).-Binds-ss--and-dsDNA-and-ss--and-dsRNA-with-approximately-equal-affinity.-May-be-able-to-anneal-complementary-DNA-strands-(PubMed:19427858). comment type cofactor cofactor evidence 1 name Mg(2+) dbReference id CHEBI:18420 type ChEBI cofactor evidence 1 name Mn(2+) dbReference id CHEBI:29035 type ChEBI comment type subunit text evidence 1-2 Homodimer,-forms-a-heterotetramer-with-a-Cas2-homodimer-(By-similarity).-Forms-oligomers,-probably-binds-nucleic-acids-as-a-homodimer-(PubMed:19427858). comment type similarity text evidence 1 Belongs-to-the-CRISPR-associated-endonuclease-Cas1-family. dbReference evidence 1 id 3.1.-.- type EC dbReference id AE006641 type EMBL property type protein-sequence-ID value AAK41681.1 property type molecule-type value Genomic_DNA dbReference id B90303 type PIR property type entry-name value B90303 dbReference id Q97Y84 type AlphaFoldDB dbReference id Q97Y84 type SMR dbReference id 273057.SSO1450 type STRING dbReference id AAK41681 type EnsemblBacteria property type protein-sequence-ID value AAK41681 property type gene-ID value SSO1450 dbReference id sso:SSO1450 type KEGG dbReference id fig|273057.12.peg.1480 type PATRIC dbReference id arCOG01452 type eggNOG property type taxonomic-scope value Archaea dbReference id CLU_052779_0_0_2 type HOGENOM dbReference id Q97Y84 type InParanoid dbReference id FIRLECY type OMA dbReference id Q97Y84 type PhylomeDB dbReference id UP000001974 type Proteomes property type component value Chromosome dbReference id GO:0003677 type GO property type term value F:DNA-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0004519 type GO property type term value F:endonuclease-activity property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0046872 type GO property type term value F:metal-ion-binding property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0003723 type GO property type term value F:RNA-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0051607 type GO property type term value P:defense-response-to-virus property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0043571 type GO property type term value P:maintenance-of-CRISPR-repeat-elements property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id cd09634 type CDD property type entry-name value Cas1_I-II-III property type match-status value 1 dbReference id 1.20.120.920 type Gene3D property type entry-name value CRISPR-associated-endonuclease-Cas1,-C-terminal-domain property type match-status value 1 dbReference id 3.100.10.20 type Gene3D property type entry-name value CRISPR-associated-endonuclease-Cas1,-N-terminal-domain property type match-status value 1 dbReference id MF_01470 type HAMAP property type entry-name value Cas1 property type match-status value 1 dbReference id IPR002729 type InterPro property type entry-name value CRISPR-assoc_Cas1 dbReference id IPR042206 type InterPro property type entry-name value CRISPR-assoc_Cas1_C dbReference id IPR042211 type InterPro property type entry-name value CRISPR-assoc_Cas1_N dbReference id PTHR34353 type PANTHER property type entry-name value CRISPR-ASSOCIATED-ENDONUCLEASE-CAS1-1 property type match-status value 1 dbReference id PTHR34353:SF2 type PANTHER property type entry-name value CRISPR-ASSOCIATED-ENDONUCLEASE-CAS1-1 property type match-status value 1 dbReference id PF01867 type Pfam property type entry-name value Cas_Cas1 property type match-status value 2 dbReference id TIGR00287 type TIGRFAMs property type entry-name value cas1 property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0051 Antiviral-defense keyword id KW-0238 DNA-binding keyword id KW-0255 Endonuclease keyword id KW-0378 Hydrolase keyword id KW-0460 Magnesium keyword id KW-0464 Manganese keyword id KW-0479 Metal-binding keyword id KW-0540 Nuclease keyword id KW-1185 Reference-proteome keyword id KW-0694 RNA-binding feature description CRISPR-associated-endonuclease-Cas1-2 id PRO_0000417111 type chain location begin position 1 end position 307 feature evidence 1-4 type binding-site location position position 142 ligand name Mn(2+) dbReference id CHEBI:29035 type ChEBI feature evidence 1 type binding-site location position position 206 ligand name Mn(2+) dbReference id CHEBI:29035 type ChEBI feature evidence 1 type binding-site location position position 221 ligand name Mn(2+) dbReference id CHEBI:29035 type ChEBI feature description No-longer-catalyzes-a-transesterification-reaction-on-branched-DNA. evidence 3 type mutagenesis-site original E variation A location position position 142 evidence key 1 type ECO:0000255 source dbReference id MF_01470 type HAMAP-Rule evidence key 2 type ECO:0000269 source dbReference id 19427858 type PubMed evidence key 3 type ECO:0000269 source dbReference id 26284603 type PubMed evidence key 4 type ECO:0000305 source dbReference id 26284603 type PubMed sequence checksum A179E60F2BBB6410 length 307 mass 34895 modified 2001-10-01 version 1 MISVRTLVISEYGAYVYVKKNMLVIKKGDKKVEISPSEVDEILITVSCSISTSALSLALTHGISVMFLNSRETPWGILLPSIVTETVKTKKAQYEAIVVRKDNRYGEEIISSKIYNQSVHLKYWARVTGTKNDYKELLDKDEPAAARVYWQNISQLLPKDIGFDGRDVDGTDQFNMALNYSYAILYNTIFKYLVIAGLDPYLGFIHKDRPGNESLVYDFSEMFKPYIDFLLVRALRSGFRLKVKGGLIEENSRGDLAKLIRKGMEENVKEESDHNPKTLIQAIRAHAVKLASSIREGKEYRGFKLVM 
entry created 2012-09-05 dataset Swiss-Prot modified 2023-02-22 version 73 accession Q2YHJ2 name PA2B_TRIBO protein recommendedName fullName Basic-phospholipase-A2-Tbo-G6D49 shortName svPLA2 ecNumber 3.1.1.4 alternativeName fullName Phosphatidylcholine-2-acylhydrolase organism name type scientific Trimeresurus-borneensis name type common Borneo-pit-viper dbReference id 109778 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Chordata taxon Craniata taxon Vertebrata taxon Euteleostomi taxon Lepidosauria taxon Squamata taxon Bifurcata taxon Unidentata taxon Episquamata taxon Toxicofera taxon Serpentes taxon Colubroidea taxon Viperidae taxon Crotalinae taxon Trimeresurus reference key 1 citation date 2005 first 3015 last 3025 name FEBS-J. type journal-article volume 272 title Unusual-venom-phospholipases-A2-of-two-primitive-tree-vipers-Trimeresurus-puniceus-and-Trimeresurus-borneensis. authorList person name Wang-Y.-M. person name Peng-H.-F. person name Tsai-I.-H. dbReference id 15955061 type PubMed dbReference id 10.1111/j.1742-4658.2005.04715.x type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] scope PROTEIN-SEQUENCE-OF-17-39 scope FUNCTION scope SUBUNIT scope MASS-SPECTROMETRY source tissue Venom tissue Venom-gland comment type function text evidence 4 Snake-venom-phospholipase-A2-(PLA2)-that-impairs-hemostasis.-It-weakly-inhibits-ADP-induced-platelet-aggregation-when-tested-on-platelet-rich-plasma-from-human-and-rabbit-blood-(15-25%-of-inhibition-at-5-10-ug-of-enzyme),-and-dose-dependently-inhibits-blood-coagulation,-possibly-by-inhibiting-thrombin-activation.-Exhibits-strong-hydrolytic-activities-toward-L-dipalmitoyl-phosphatidylcholine.-PLA2-catalyzes-the-calcium-dependent-hydrolysis-of-the-2-acyl-groups-in-3-sn-phosphoglycerides. comment type catalytic-activity reaction evidence 2-3 text a-1,2-diacyl-sn-glycero-3-phosphocholine-+-H2O-=-a-1-acyl-sn-glycero-3-phosphocholine-+-a-fatty-acid-+-H(+) dbReference id RHEA:15801 type Rhea dbReference id CHEBI:15377 type ChEBI dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:28868 type ChEBI dbReference id CHEBI:57643 type ChEBI dbReference id CHEBI:58168 type ChEBI dbReference id 3.1.1.4 type EC comment type cofactor cofactor evidence 1 name Ca(2+) dbReference id CHEBI:29108 type ChEBI text evidence 1 Binds-1-Ca(2+)-ion. comment type subunit text evidence 4 Monomer. comment type subcellular-location subcellularLocation location Secreted comment type tissue-specificity text Expressed-by-the-venom-gland. comment evidence 4 mass 13959.6 method Electrospray type mass-spectrometry comment type similarity text evidence 5 Belongs-to-the-phospholipase-A2-family.-Group-II-subfamily.-D49-sub-subfamily. dbReference id 3.1.1.4 type EC dbReference id AY355179 type EMBL property type protein-sequence-ID value AAR14173.1 property type molecule-type value mRNA dbReference id Q2YHJ2 type AlphaFoldDB dbReference id Q2YHJ2 type SMR dbReference id GO:0005576 type GO property type term value C:extracellular-region property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0005509 type GO property type term value F:calcium-ion-binding property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0004623 type GO property type term value F:phospholipase-A2-activity property type evidence value ECO:0007669 property type project value UniProtKB-EC dbReference id GO:0090729 type GO property type term value F:toxin-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0050482 type GO property type term value P:arachidonic-acid-secretion property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0016042 type GO property type term value P:lipid-catabolic-process property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0006644 type GO property type term value P:phospholipid-metabolic-process property type evidence value ECO:0007669 property type project value InterPro dbReference id cd00125 type CDD property type entry-name value PLA2c property type match-status value 1 dbReference id 1.20.90.10 type Gene3D property type entry-name value Phospholipase-A2-domain property type match-status value 1 dbReference id IPR001211 type InterPro property type entry-name value PLipase_A2 dbReference id IPR033112 type InterPro property type entry-name value PLipase_A2_Asp_AS dbReference id IPR016090 type InterPro property type entry-name value PLipase_A2_dom dbReference id IPR036444 type InterPro property type entry-name value PLipase_A2_dom_sf dbReference id IPR033113 type InterPro property type entry-name value PLipase_A2_His_AS dbReference id PTHR11716 type PANTHER property type entry-name value PHOSPHOLIPASE-A2-FAMILY-MEMBER property type match-status value 1 dbReference id PTHR11716:SF9 type PANTHER property type entry-name value PHOSPHOLIPASE-A2,-MEMBRANE-ASSOCIATED property type match-status value 1 dbReference id PF00068 type Pfam property type entry-name value Phospholip_A2_1 property type match-status value 1 dbReference id PR00389 type PRINTS property type entry-name value PHPHLIPASEA2 dbReference id SM00085 type SMART property type entry-name value PA2c property type match-status value 1 dbReference id SSF48619 type SUPFAM property type entry-name value Phospholipase-A2,-PLA2 property type match-status value 1 dbReference id PS00119 type PROSITE property type entry-name value PA2_ASP property type match-status value 1 dbReference id PS00118 type PROSITE property type entry-name value PA2_HIS property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-1203 Blood-coagulation-cascade-inhibiting-toxin keyword id KW-0106 Calcium keyword id KW-0903 Direct-protein-sequencing keyword id KW-1015 Disulfide-bond keyword id KW-1199 Hemostasis-impairing-toxin keyword id KW-0378 Hydrolase keyword id KW-0442 Lipid-degradation keyword id KW-0443 Lipid-metabolism keyword id KW-0479 Metal-binding keyword id KW-1201 Platelet-aggregation-inhibiting-toxin keyword id KW-0964 Secreted keyword id KW-0732 Signal keyword id KW-0800 Toxin feature evidence 4 type signal-peptide location begin position 1 end position 16 feature description Basic-phospholipase-A2-Tbo-G6D49 id PRO_0000419055 type chain location begin position 17 end position 138 feature evidence 1 type active-site location position position 63 feature evidence 1 type active-site location position position 105 feature evidence 1 type binding-site location position position 43 ligand name Ca(2+) dbReference id CHEBI:29108 type ChEBI feature evidence 1 type binding-site location position position 45 ligand name Ca(2+) dbReference id CHEBI:29108 type ChEBI feature evidence 1 type binding-site location position position 47 ligand name Ca(2+) dbReference id CHEBI:29108 type ChEBI feature evidence 1 type binding-site location position position 64 ligand name Ca(2+) dbReference id CHEBI:29108 type ChEBI feature evidence 1 type disulfide-bond location begin position 42 end position 131 feature evidence 1 type disulfide-bond location begin position 44 end position 60 feature evidence 1 type disulfide-bond location begin position 59 end position 111 feature evidence 1 type disulfide-bond location begin position 65 end position 138 feature evidence 1 type disulfide-bond location begin position 66 end position 104 feature evidence 1 type disulfide-bond location begin position 73 end position 97 feature evidence 1 type disulfide-bond location begin position 91 end position 102 evidence key 1 type ECO:0000250 evidence key 2 type ECO:0000255 source dbReference id PRU10035 type PROSITE-ProRule evidence key 3 type ECO:0000255 source dbReference id PRU10036 type PROSITE-ProRule evidence key 4 type ECO:0000269 source dbReference id 15955061 type PubMed evidence key 5 type ECO:0000305 sequence checksum 6F2F90E4748828F5 length 138 mass 15742 modified 2005-12-20 precursor true version 1 MRTLWIMAVLLVGVEGSLLEFGRMIKEETGKNPLFSYISYGCYCGWGGQGQPKDATDRCCFVHDCCYGKLWSCSPKTDIYFYYRKNGAIVCARGTWCEKQICECDKAAAICFRENLGTYKDEYQSYGKSRCTEKSLKC 
entry created 2013-03-06 dataset Swiss-Prot modified 2023-02-22 version 34 accession F8WRK9 name CEEP_RHOMR protein recommendedName fullName evidence 1 Cellobiose-2-epimerase shortName evidence 1 CE ecNumber evidence 1 5.1.3.11 gene name type primary ce organism name type scientific Rhodothermus-marinus name type common Rhodothermus-obamensis dbReference id 29549 type NCBI-Taxonomy lineage taxon Bacteria taxon Bacteroidota taxon Bacteroidetes-Order-II.-Incertae-sedis taxon Rhodothermaceae taxon Rhodothermus reference key 1 citation date 2011 first 2162 last 2168 name Biosci.-Biotechnol.-Biochem. type journal-article volume 75 title Biochemical-characterization-of-a-thermophilic-cellobiose-2-epimerase-from-a-thermohalophilic-bacterium,-Rhodothermus-marinus-JCM9785. authorList person name Ojima-T. person name Saburi-W. person name Sato-H. person name Yamamoto-T. person name Mori-H. person name Matsui-H. dbReference id 22056431 type PubMed dbReference id 10.1271/bbb.110456 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope PROTEIN-SEQUENCE-OF-4-12 scope FUNCTION scope CATALYTIC-ACTIVITY scope BIOPHYSICOCHEMICAL-PROPERTIES source strain OKD7-/-DSM-12399-/-JCM-9785 comment type function text evidence 1-2 Catalyzes-the-reversible-epimerization-of-cellobiose-to-4-O-beta-D-glucopyranosyl-D-mannose-(Glc-Man).-Can-also-use-lactose,-epilactose,-mannobiose-and-cellotriose.-Highly-specific-for-oligosaccharides-linked-by-the-beta-1,4-glycosidic-linkage.-Shows-preference-for-lactose. comment type catalytic-activity reaction evidence 1-2 text D-cellobiose-=-beta-D-glucosyl-(1->4)-D-mannopyranose dbReference id RHEA:23384 type Rhea dbReference id CHEBI:17057 type ChEBI dbReference id CHEBI:47931 type ChEBI dbReference id 5.1.3.11 type EC comment type biophysicochemical-properties kinetics KM evidence 2 27.2-mM-for-cellobiose KM evidence 2 28.8-mM-for-lactose text kcat-is-80.8-sec(-1)-for-cellobiose.-kcat-is-111-sec(-1)-for-lactose. phDependence text evidence 2 Optimum-pH-is-6.3. temperatureDependence text evidence 2 Optimum-temperature-is-80-degrees-Celsius. comment type similarity text evidence 1 Belongs-to-the-cellobiose-2-epimerase-family. dbReference evidence 1 id 5.1.3.11 type EC dbReference id AB638764 type EMBL property type protein-sequence-ID value BAK61777.1 property type molecule-type value Genomic_DNA dbReference id 3WKF type PDB property type method value X-ray property type resolution value 1.74-A property type chains value A=1-412 dbReference id 3WKG type PDB property type method value X-ray property type resolution value 1.47-A property type chains value A=1-412 dbReference id 3WKH type PDB property type method value X-ray property type resolution value 1.64-A property type chains value A=1-412 dbReference id 3WKI type PDB property type method value X-ray property type resolution value 2.19-A property type chains value A=1-412 dbReference id 3WKF type PDBsum dbReference id 3WKG type PDBsum dbReference id 3WKH type PDBsum dbReference id 3WKI type PDBsum dbReference id F8WRK9 type AlphaFoldDB dbReference id F8WRK9 type SMR dbReference id 5.1.3.11 type BRENDA property type organism-ID value 5425 dbReference id GO:0047736 type GO property type term value F:cellobiose-epimerase-activity property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0005975 type GO property type term value P:carbohydrate-metabolic-process property type evidence value ECO:0007669 property type project value InterPro dbReference id 1.50.10.10 type Gene3D property type match-status value 1 dbReference id MF_00929 type HAMAP property type entry-name value Cellobiose_2_epim property type match-status value 1 dbReference id IPR008928 type InterPro property type entry-name value 6-hairpin_glycosidase_sf dbReference id IPR012341 type InterPro property type entry-name value 6hp_glycosidase-like_sf dbReference id IPR010819 type InterPro property type entry-name value AGE/CE dbReference id IPR028584 type InterPro property type entry-name value Cellobiose_2_epim dbReference id PTHR15108:SF0 type PANTHER property type entry-name value N-ACYLGLUCOSAMINE-2-EPIMERASE property type match-status value 1 dbReference id PTHR15108 type PANTHER property type entry-name value N-ACYLGLUCOSAMINE-2-EPIMERASE property type match-status value 1 dbReference id PF07221 type Pfam property type entry-name value GlcNAc_2-epim property type match-status value 1 dbReference id SSF48208 type SUPFAM property type entry-name value Six-hairpin-glycosidases property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0002 3D-structure keyword id KW-0903 Direct-protein-sequencing keyword id KW-0413 Isomerase feature description Cellobiose-2-epimerase id PRO_0000421447 type chain location begin position 1 end position 412 feature evidence 3 type helix location begin position 9 end position 25 feature evidence 3 type helix location begin position 27 end position 34 feature evidence 3 type turn location begin position 38 end position 40 feature evidence 3 type strand location begin position 41 end position 43 feature evidence 3 type helix location begin position 61 end position 78 feature evidence 3 type helix location begin position 81 end position 97 feature evidence 3 type turn location begin position 101 end position 103 feature evidence 3 type strand location begin position 108 end position 110 feature evidence 3 type strand location begin position 116 end position 118 feature evidence 3 type helix location begin position 123 end position 140 feature evidence 3 type helix location begin position 143 end position 159 feature evidence 3 type turn location begin position 163 end position 165 feature evidence 3 type strand location begin position 166 end position 168 feature evidence 3 type strand location begin position 192 end position 194 feature evidence 3 type helix location begin position 195 end position 211 feature evidence 3 type helix location begin position 215 end position 231 feature evidence 3 type turn location begin position 235 end position 237 feature evidence 3 type strand location begin position 238 end position 240 feature evidence 3 type helix location begin position 257 end position 274 feature evidence 3 type turn location begin position 277 end position 279 feature evidence 3 type helix location begin position 280 end position 297 feature evidence 3 type helix location begin position 321 end position 338 feature evidence 3 type helix location begin position 342 end position 356 feature evidence 3 type turn location begin position 361 end position 363 feature evidence 3 type strand location begin position 364 end position 366 feature evidence 3 type strand location begin position 368 end position 370 feature evidence 3 type strand location begin position 381 end position 383 feature evidence 3 type helix location begin position 389 end position 406 evidence key 1 type ECO:0000255 source dbReference id MF_00929 type HAMAP-Rule evidence key 2 type ECO:0000269 source dbReference id 22056431 type PubMed evidence key 3 type ECO:0007829 source dbReference id 3WKG type PDB sequence checksum 0EEE153737F40DBD length 412 mass 47387 modified 2011-10-19 version 1 MSTETIPDVRRLRALQAEVHEELTENILKFWATRTHDPVHGGFVGRVGPDGRPHPEAPRGAILNARILWTFAAAYRQLGTPLYREMAERAYRYFVRHFVDAEHGGVYWMVAADGRPLDTRKHVYAQSFAIYALSEWHRATGGEAALALARSIYDLIETHCADRVHGGYVEACDRAWRPLEDARLSAKDAPEPRSMNTHLHVLEAYANLYRVWPETELAARLQALIELFLRAIYHPATGHLILFFDERWRPRSRAVSFGHDIEASWLLLEAVDVLGQATLRPRVQQASLHLARATLAEGRAPDGSLYYEIGEQGHLDTDRHWWPQAEALVGFLNAYQESGEVLFYEAAEDVWRYIRERQRDTRGGEWFARVRDDGAPYPDDKVDFWKGPYHNGRACLEAIQRLRHLLEHVRSR 
entry created 2013-10-16 dataset Swiss-Prot modified 2023-02-22 version 43 accession B8B4K9 name NAF1D_ORYSI protein recommendedName fullName Nucleosome-assembly-protein-1-like-4 gene name type ORF OsI_23686 organism name type scientific Oryza-sativa-subsp.-indica name type common Rice dbReference id 39946 type NCBI-Taxonomy lineage taxon Eukaryota taxon Viridiplantae taxon Streptophyta taxon Embryophyta taxon Tracheophyta taxon Spermatophyta taxon Magnoliopsida taxon Liliopsida taxon Poales taxon Poaceae taxon BOP-clade taxon Oryzoideae taxon Oryzeae taxon Oryzinae taxon Oryza taxon Oryza-sativa reference key 1 citation date 2005 first 266 last 281 name PLoS-Biol. type journal-article volume 3 title The-genomes-of-Oryza-sativa:-a-history-of-duplications. authorList person name Yu-J. person name Wang-J. person name Lin-W. person name Li-S. person name Li-H. person name Zhou-J. person name Ni-P. person name Dong-W. person name Hu-S. person name Zeng-C. person name Zhang-J. person name Zhang-Y. person name Li-R. person name Xu-Z. person name Li-S. person name Li-X. person name Zheng-H. person name Cong-L. person name Lin-L. person name Yin-J. person name Geng-J. person name Li-G. person name Shi-J. person name Liu-J. person name Lv-H. person name Li-J. person name Wang-J. person name Deng-Y. person name Ran-L. person name Shi-X. person name Wang-X. person name Wu-Q. person name Li-C. person name Ren-X. person name Wang-J. person name Wang-X. person name Li-D. person name Liu-D. person name Zhang-X. person name Ji-Z. person name Zhao-W. person name Sun-Y. person name Zhang-Z. person name Bao-J. person name Han-Y. person name Dong-L. person name Ji-J. person name Chen-P. person name Wu-S. person name Liu-J. person name Xiao-Y. person name Bu-D. person name Tan-J. person name Yang-L. person name Ye-C. person name Zhang-J. person name Xu-J. person name Zhou-Y. person name Yu-Y. person name Zhang-B. person name Zhuang-S. person name Wei-H. person name Liu-B. person name Lei-M. person name Yu-H. person name Li-Y. person name Xu-H. person name Wei-S. person name He-X. person name Fang-L. person name Zhang-Z. person name Zhang-Y. person name Huang-X. person name Su-Z. person name Tong-W. person name Li-J. person name Tong-Z. person name Li-S. person name Ye-J. person name Wang-L. person name Fang-L. person name Lei-T. person name Chen-C.-S. person name Chen-H.-C. person name Xu-Z. person name Li-H. person name Huang-H. person name Zhang-F. person name Xu-H. person name Li-N. person name Zhao-C. person name Li-S. person name Dong-L. person name Huang-Y. person name Li-L. person name Xi-Y. person name Qi-Q. person name Li-W. person name Zhang-B. person name Hu-W. person name Zhang-Y. person name Tian-X. person name Jiao-Y. person name Liang-X. person name Jin-J. person name Gao-L. person name Zheng-W. person name Hao-B. person name Liu-S.-M. person name Wang-W. person name Yuan-L. person name Cao-M. person name McDermott-J. person name Samudrala-R. person name Wang-J. person name Wong-G.K.-S. person name Yang-H. dbReference id 15685292 type PubMed dbReference id 10.1371/journal.pbio.0030038 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain cv.-93-11 comment type function text evidence 1 May-modulate-chromatin-structure-by-regulation-of-nucleosome-assembly/disassembly. comment type subcellular-location subcellularLocation location evidence 1 Nucleus subcellularLocation location evidence 1 Cytoplasm comment type domain text The-acidic-domain-is-probably-involved-in-the-interaction-with-histones. comment type similarity text evidence 4 Belongs-to-the-nucleosome-assembly-protein-(NAP)-family. comment evidence 4 type sequence-caution conflict type erroneous-gene-model-prediction sequence id EEC80965 resource EMBL-CDS version 1 comment evidence 4 type sequence-caution conflict type frameshift sequence id EEC80965 resource EMBL-CDS version 1 dbReference id CM000131 type EMBL property type protein-sequence-ID value EEC80965.1 property type status value ALT_SEQ property type molecule-type value Genomic_DNA dbReference id B8B4K9 type AlphaFoldDB dbReference id B8B4K9 type SMR dbReference id 39946.B8B4K9 type STRING dbReference id CLU_038841_4_2_1 type HOGENOM dbReference id UP000007015 type Proteomes property type component value Chromosome-6 dbReference id GO:0005737 type GO property type term value C:cytoplasm property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0005634 type GO property type term value C:nucleus property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0042393 type GO property type term value F:histone-binding property type evidence value ECO:0007669 property type project value UniProt dbReference id GO:0000724 type GO property type term value P:double-strand-break-repair-via-homologous-recombination property type evidence value ECO:0007669 property type project value UniProt dbReference id GO:0006334 type GO property type term value P:nucleosome-assembly property type evidence value ECO:0007669 property type project value InterPro dbReference id 1.20.5.1500 type Gene3D property type match-status value 1 dbReference id 3.30.1120.90 type Gene3D property type entry-name value Nucleosome-assembly-protein property type match-status value 1 dbReference id IPR037231 type InterPro property type entry-name value NAP-like_sf dbReference id IPR002164 type InterPro property type entry-name value NAP_family dbReference id PTHR11875:SF7 type PANTHER property type entry-name value AT14585P-RELATED property type match-status value 1 dbReference id PTHR11875 type PANTHER property type entry-name value TESTIS-SPECIFIC-Y-ENCODED-PROTEIN property type match-status value 1 dbReference id PF00956 type Pfam property type entry-name value NAP property type match-status value 1 dbReference id SSF143113 type SUPFAM property type entry-name value NAP-like property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0143 Chaperone keyword id KW-0175 Coiled-coil keyword id KW-0963 Cytoplasm keyword id KW-0539 Nucleus keyword id KW-1185 Reference-proteome feature description Nucleosome-assembly-protein-1-like-4 id PRO_0000423693 type chain location begin position 1 end position 312 feature description Disordered evidence 3 type region-of-interest location begin position 288 end position 312 feature evidence 2 type coiled-coil-region location begin position 24 end position 78 feature description Nuclear-export-signal evidence 2 type short-sequence-motif location begin position 45 end position 60 feature description Acidic-residues evidence 3 type compositionally-biased-region location begin position 290 end position 312 evidence key 1 type ECO:0000250 evidence key 2 type ECO:0000255 evidence key 3 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 4 type ECO:0000305 sequence checksum 579D2BFAB67896F4 length 312 mass 36323 modified 2013-10-16 version 2 MNEEVEDGEVKPLELSSEDKAILVETLKNKLQALAEQHVDVLESLAPSVRKRVDVLMEIQSQHDELEVKFFEEKAALEAKYQKLYGPLYSKRSKIVSGVLEVEGETEEREEKGVPDFWLNAMKNNEILAEEIHESDEEALKYLKDIKWCRIDDPKGFKFEFFFYTNPFFKNQVLTKTYHMIDEDDEPILEKAIGTEIEWHPGYCLTQEVLTKESSESTKPITKTEECESFFNFFSPPQVPDDDAKIDENTAEELQNQMERDYDIASTLRDKIIPHAVSWFTREAVQDEDYGASWVDDEEEDDNDDEYSDEEA 
entry created 2014-04-16 dataset Swiss-Prot modified 2023-02-22 version 44 accession P9WMY5 accession L0T409 accession O06423 accession Q7BTG3 accession Q8VKJ0 name MGTA_MYCTU protein recommendedName fullName GDP-mannose-dependent-alpha-mannosyltransferase ecNumber 2.4.1.- alternativeName fullName Guanosine-diphosphomannose-dependent-alpha-mannosyltransferase gene name type primary mgtA name type synonym pimB name type ordered-locus Rv0557 organism name type scientific Mycobacterium-tuberculosis-(strain-ATCC-25618-/-H37Rv) dbReference id 83332 type NCBI-Taxonomy lineage taxon Bacteria taxon Actinobacteria taxon Corynebacteriales taxon Mycobacteriaceae taxon Mycobacterium taxon Mycobacterium-tuberculosis-complex reference key 1 citation date 1999 first 31625 last 31631 name J.-Biol.-Chem. type journal-article volume 274 title The-pimB-gene-of-Mycobacterium-tuberculosis-encodes-a-mannosyltransferase-involved-in-lipoarabinomannan-biosynthesis. authorList person name Schaeffer-M.L. person name Khoo-K.H. person name Besra-G.S. person name Chatterjee-D. person name Brennan-P.J. person name Belisle-J.T. person name Inamine-J.M. dbReference id 10531370 type PubMed dbReference id 10.1074/jbc.274.44.31625 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] source strain ATCC-25618-/-H37Rv reference key 2 citation date 1998 first 537 last 544 name Nature type journal-article volume 393 title Deciphering-the-biology-of-Mycobacterium-tuberculosis-from-the-complete-genome-sequence. authorList person name Cole-S.T. person name Brosch-R. person name Parkhill-J. person name Garnier-T. person name Churcher-C.M. person name Harris-D.E. person name Gordon-S.V. person name Eiglmeier-K. person name Gas-S. person name Barry-C.E.-III person name Tekaia-F. person name Badcock-K. person name Basham-D. person name Brown-D. person name Chillingworth-T. person name Connor-R. person name Davies-R.M. person name Devlin-K. person name Feltwell-T. person name Gentles-S. person name Hamlin-N. person name Holroyd-S. person name Hornsby-T. person name Jagels-K. person name Krogh-A. person name McLean-J. person name Moule-S. person name Murphy-L.D. person name Oliver-S. person name Osborne-J. person name Quail-M.A. person name Rajandream-M.A. person name Rogers-J. person name Rutter-S. person name Seeger-K. person name Skelton-S. person name Squares-S. person name Squares-R. person name Sulston-J.E. person name Taylor-K. person name Whitehead-S. person name Barrell-B.G. dbReference id 9634230 type PubMed dbReference id 10.1038/31159 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain ATCC-25618-/-H37Rv reference key 3 citation date 2008 first 109 last 109 name BMC-Syst.-Biol. type journal-article volume 2 title targetTB:-a-target-identification-pipeline-for-Mycobacterium-tuberculosis-through-an-interactome,-reactome-and-genome-scale-structural-analysis. authorList person name Raman-K. person name Yeturu-K. person name Chandra-N. dbReference id 19099550 type PubMed dbReference id 10.1186/1752-0509-2-109 type DOI scope IDENTIFICATION-AS-A-DRUG-TARGET-[LARGE-SCALE-ANALYSIS] reference key 4 citation date 2009 first 4465 last 4472 name J.-Bacteriol. type journal-article volume 191 title Characterization-of-the-Corynebacterium-glutamicum-deltapimB'-deltamgtA-double-deletion-mutant-and-the-role-of-Mycobacterium-tuberculosis-orthologues-Rv2188c-and-Rv0557-in-glycolipid-biosynthesis. authorList person name Mishra-A.K. person name Batt-S. person name Krumbach-K. person name Eggeling-L. person name Besra-G.S. dbReference id 19395496 type PubMed dbReference id 10.1128/jb.01729-08 type DOI scope FUNCTION-IN-MANGLCAGROAC2-BIOSYNTHESIS scope NOMENCLATURE comment type function text evidence 1 Catalyzes-the-addition-of-a-mannose-residue-from-GDP-D-mannose-to-GlcAGroAc2-to-generate-1,2-di-O-C16/C18:1-(alpha-D-mannopyranosyl)-(1-4)-(alpha-D-glucopyranosyluronic-acid)-(1-3)-glycerol(ManGlcAGroAc2). comment type pathway text Phospholipid-metabolism;-phosphatidylinositol-metabolism. comment type miscellaneous text Was-identified-as-a-high-confidence-drug-target. comment type similarity text evidence 2 Belongs-to-the-glycosyltransferase-group-1-family.-Glycosyltransferase-4-subfamily. dbReference id 2.4.1.- type EC dbReference id AF061562 type EMBL property type protein-sequence-ID value AAC63250.1 property type molecule-type value Genomic_DNA dbReference id AL123456 type EMBL property type protein-sequence-ID value CCP43295.1 property type molecule-type value Genomic_DNA dbReference id H70548 type PIR property type entry-name value H70548 dbReference id NP_215071.1 type RefSeq property type nucleotide-sequence-ID value NC_000962.3 dbReference id WP_003900963.1 type RefSeq property type nucleotide-sequence-ID value NC_000962.3 dbReference id P9WMY5 type AlphaFoldDB dbReference id P9WMY5 type SMR dbReference id 83332.Rv0557 type STRING dbReference id GT4 type CAZy property type family-name value Glycosyltransferase-Family-4 dbReference id P9WMY5 type PaxDb dbReference id 887609 type DNASU dbReference id 887609 type GeneID dbReference id mtu:Rv0557 type KEGG dbReference id fig|83332.111.peg.614 type PATRIC dbReference id Rv0557 type TubercuList dbReference id COG0438 type eggNOG property type taxonomic-scope value Bacteria dbReference id ERVDLWQ type OMA dbReference id 9802525at2 type OrthoDB dbReference id P9WMY5 type PhylomeDB dbReference id MetaCyc:G185E-6398-MON type BioCyc dbReference id 2.4.1.346 type BRENDA property type organism-ID value 3445 dbReference id 2.4.1.B74 type BRENDA property type organism-ID value 3445 dbReference id UPA00949 type UniPathway dbReference id UP000001584 type Proteomes property type component value Chromosome dbReference id GO:0016757 type GO property type term value F:glycosyltransferase-activity property type evidence value ECO:0000318 property type project value GO_Central dbReference id GO:0016758 type GO property type term value F:hexosyltransferase-activity property type evidence value ECO:0000318 property type project value GO_Central dbReference id GO:0000030 type GO property type term value F:mannosyltransferase-activity property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0009247 type GO property type term value P:glycolipid-biosynthetic-process property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0046488 type GO property type term value P:phosphatidylinositol-metabolic-process property type evidence value ECO:0007669 property type project value UniProtKB-UniPathway dbReference id GO:0008654 type GO property type term value P:phospholipid-biosynthetic-process property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id cd03814 type CDD property type entry-name value GT4-like property type match-status value 1 dbReference id 3.40.50.2000 type Gene3D property type entry-name value Glycogen-Phosphorylase-B property type match-status value 2 dbReference id IPR001296 type InterPro property type entry-name value Glyco_trans_1 dbReference id IPR028098 type InterPro property type entry-name value Glyco_trans_4-like_N dbReference id PTHR45947 type PANTHER property type entry-name value SULFOQUINOVOSYL-TRANSFERASE-SQD2 property type match-status value 1 dbReference id PTHR45947:SF3 type PANTHER property type entry-name value SULFOQUINOVOSYL-TRANSFERASE-SQD2 property type match-status value 1 dbReference id PF13439 type Pfam property type entry-name value Glyco_transf_4 property type match-status value 1 dbReference id PF00534 type Pfam property type entry-name value Glycos_transf_1 property type match-status value 1 dbReference id SSF53756 type SUPFAM property type entry-name value UDP-Glycosyltransferase/glycogen-phosphorylase property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0328 Glycosyltransferase keyword id KW-0444 Lipid-biosynthesis keyword id KW-0443 Lipid-metabolism keyword id KW-0594 Phospholipid-biosynthesis keyword id KW-1208 Phospholipid-metabolism keyword id KW-1185 Reference-proteome keyword id KW-0808 Transferase keyword id KW-0843 Virulence feature description GDP-mannose-dependent-alpha-mannosyltransferase id PRO_0000393729 type chain location begin position 1 end position 378 evidence key 1 type ECO:0000269 source dbReference id 19395496 type PubMed evidence key 2 type ECO:0000305 sequence checksum E1E5524A88A52D65 length 378 mass 41238 modified 2014-04-16 version 1 MCGVRVAIVAESFLPQVNGVSNSVVKVLEHLRRTGHEALVIAPDTPPGEDRAERLHDGVRVHRVPSRMFPKVTTLPLGVPTFRMLRALRGFDPDVVHLASPALLGYGGLHAARRLGVPTVAVYQTDVPGFASSYGIPMTARAAWAWFRHLHRLADRTLAPSTATMESLIAQGIPRVHRWARGVDVQRFAPSARNEVLRRRWSPDGKPIVGFVGRLAPEKHVDRLTGLAASGAVRLVIVGDGIDRARLQSAMPTAVFTGARYGKELAEAYASMDVFVHSGEHETFCQVVQEALASGLPVIAPDAGGPRDLITPHRTGLLLPVGEFEHRLPDAVAHLVHERQRYALAARRSVLGRSWPVVCDELLGHYEAVRGRRTTQAA 
entry created 2014-07-09 dataset Swiss-Prot modified 2023-02-22 version 25 accession B8V7S0 name CPP1_ACRMI protein recommendedName fullName evidence 5 CUB-and-peptidase-domain-containing-protein-1 organism name type scientific Acropora-millepora name type common Staghorn-coral name type synonym Heteropora-millepora dbReference id 45264 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Cnidaria taxon Anthozoa taxon Hexacorallia taxon Scleractinia taxon Astrocoeniina taxon Acroporidae taxon Acropora reference evidence 6 key 1 citation date 2012 first 2440 last 2454 name Mol.-Ecol. type journal-article volume 21 title Whole-transcriptome-analysis-of-the-coral-Acropora-millepora-reveals-complex-responses-to-CO(2)-driven-acidification-during-the-initiation-of-calcification. authorList person name Moya-A. person name Huisman-L. person name Ball-E.E. person name Hayward-D.C. person name Grasso-L.C. person name Chua-C.M. person name Woo-H.N. person name Gattuso-J.P. person name Foret-S. person name Miller-D.J. dbReference id 22490231 type PubMed dbReference id 10.1111/j.1365-294x.2012.05554.x type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] reference evidence 6 key 2 citation date 2013 first 2099 last 2112 name Mol.-Biol.-Evol. type journal-article volume 30 title The-skeletal-proteome-of-the-coral-Acropora-millepora:-the-evolution-of-calcification-by-co-option-and-domain-shuffling. authorList person name Ramos-Silva-P. person name Kaandorp-J. person name Huisman-L. person name Marie-B. person name Zanella-Cleon-I. person name Guichard-N. person name Miller-D.J. person name Marin-F. dbReference id 23765379 type PubMed dbReference id 10.1093/molbev/mst109 type DOI scope PROTEIN-SEQUENCE-OF-112-122;-158-168;-209-222-AND-335-348 scope TISSUE-SPECIFICITY scope IDENTIFICATION-BY-MASS-SPECTROMETRY comment type subcellular-location subcellularLocation location evidence 7 Secreted comment type tissue-specificity text evidence 4 Component-of-the-acid-insoluble-organic-matrix-of-the-aragonitic-skeleton-(at-protein-level). comment type similarity text evidence 3 Belongs-to-the-peptidase-S1-family. dbReference id JR970990 type EMBL property type status value NOT_ANNOTATED_CDS property type molecule-type value mRNA dbReference id B8V7S0 type AlphaFoldDB dbReference id B8V7S0 type SMR dbReference id GO:0005576 type GO property type term value C:extracellular-region property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0004252 type GO property type term value F:serine-type-endopeptidase-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0006508 type GO property type term value P:proteolysis property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id cd00041 type CDD property type entry-name value CUB property type match-status value 1 dbReference id cd00190 type CDD property type entry-name value Tryp_SPc property type match-status value 1 dbReference id 2.60.120.290 type Gene3D property type entry-name value Spermadhesin,-CUB-domain property type match-status value 1 dbReference id 2.40.10.10 type Gene3D property type entry-name value Trypsin-like-serine-proteases property type match-status value 1 dbReference id IPR000859 type InterPro property type entry-name value CUB_dom dbReference id IPR009003 type InterPro property type entry-name value Peptidase_S1_PA dbReference id IPR043504 type InterPro property type entry-name value Peptidase_S1_PA_chymotrypsin dbReference id IPR001314 type InterPro property type entry-name value Peptidase_S1A dbReference id IPR035914 type InterPro property type entry-name value Sperma_CUB_dom_sf dbReference id IPR001254 type InterPro property type entry-name value Trypsin_dom dbReference id IPR018114 type InterPro property type entry-name value TRYPSIN_HIS dbReference id IPR033116 type InterPro property type entry-name value TRYPSIN_SER dbReference id PTHR24252:SF8 type PANTHER property type entry-name value ACROSIN property type match-status value 1 dbReference id PTHR24252 type PANTHER property type entry-name value ACROSIN-RELATED property type match-status value 1 dbReference id PF00431 type Pfam property type entry-name value CUB property type match-status value 1 dbReference id PF00089 type Pfam property type entry-name value Trypsin property type match-status value 1 dbReference id PR00722 type PRINTS property type entry-name value CHYMOTRYPSIN dbReference id SM00042 type SMART property type entry-name value CUB property type match-status value 1 dbReference id SM00020 type SMART property type entry-name value Tryp_SPc property type match-status value 1 dbReference id SSF49854 type SUPFAM property type entry-name value Spermadhesin,-CUB-domain property type match-status value 2 dbReference id SSF50494 type SUPFAM property type entry-name value Trypsin-like-serine-proteases property type match-status value 1 dbReference id PS01180 type PROSITE property type entry-name value CUB property type match-status value 1 dbReference id PS50240 type PROSITE property type entry-name value TRYPSIN_DOM property type match-status value 1 dbReference id PS00134 type PROSITE property type entry-name value TRYPSIN_HIS property type match-status value 1 dbReference id PS00135 type PROSITE property type entry-name value TRYPSIN_SER property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0903 Direct-protein-sequencing keyword id KW-1015 Disulfide-bond keyword id KW-0378 Hydrolase keyword id KW-0645 Protease keyword id KW-0964 Secreted keyword id KW-0720 Serine-protease keyword id KW-0732 Signal feature evidence 1 type signal-peptide location begin position 1 status less-than end position 16 feature description CUB-and-peptidase-domain-containing-protein-1 evidence 1 id PRO_0000429495 type chain location begin position 17 end position 435 status greater-than feature description Peptidase-S1 evidence 3 type domain location begin position 25 end position 261 feature description CUB evidence 2 type domain location begin position 256 end position 378 feature description Charge-relay-system evidence 1 type active-site location position position 65 feature description Charge-relay-system evidence 1 type active-site location position position 116 feature description Charge-relay-system evidence 1 type active-site location position position 212 feature evidence 1 type disulfide-bond location begin position 50 end position 66 feature evidence 1 type disulfide-bond location begin position 151 end position 218 feature evidence 1 type disulfide-bond location begin position 182 end position 197 feature evidence 1 type disulfide-bond location begin position 208 end position 237 feature evidence 1 type disulfide-bond location begin position 322 end position 341 feature evidence 6 type non-terminal-residue location position position 1 feature evidence 6 type non-terminal-residue location position position 435 evidence key 1 type ECO:0000255 evidence key 2 type ECO:0000255 source dbReference id PRU00059 type PROSITE-ProRule evidence key 3 type ECO:0000255 source dbReference id PRU00274 type PROSITE-ProRule evidence key 4 type ECO:0000269 source dbReference id 23765379 type PubMed evidence key 5 type ECO:0000303 source dbReference id 23765379 type PubMed evidence key 6 type ECO:0000305 evidence key 7 type ECO:0000305 source dbReference id 23765379 type PubMed sequence checksum 586F5AFD73605F6A fragment single length 435 mass 47906 modified 2014-07-09 precursor true version 1 SGFHLSFSFFRRAVCGIRPTLSGFIVGGTVAPINSWPWQAKLRIAGNFLCGGSLIQPEWVLTAAHCVEGESPSIIKVTLGAHYLSTAQVVGTEQYFDVVQIIQHENYKMPKRFSNDVALLKLSRPAALRNGVGLVCLSDDQFQRPFNGTSCWTTGWGRLSWPGPVAKELMQVDLPLVSPQNCLSSYPNGYDPNTMICAGRSQGGTGACRGDSGGPLVCEFKGKWYLEGVTSWGQLPCDLPNKPTVYADVRKLKSWITGKISRSPALKVATNCSSVLNNTLKSPGYPDSYPINMFCVYRVPIPCDTELVIHFNSFHLENHVFCWYDRLRITDGSNRVIGTYCGQQTGRSVLVNDTVAVLTFKTDRSLNSSGFHLSFSFFPRGNATLLPFTTPTQTTTQRPTTTPTPGCGVVQNNTLRSPGYPSNYPRNTHCVYRVF 
entry created 2014-10-01 dataset Swiss-Prot modified 2023-02-22 version 47 accession A0CDD4 name CFA20_PARTE protein recommendedName fullName Cilia--and-flagella-associated-protein-20 shortName Bug22p gene name type primary CFAP20 name type synonym Bug22 name type synonym Bug22a name type synonym Bug22b name type synonym Bug22c name type synonym Bug22d name type ORF GSPATT00007012001 name type ORF GSPATT00012810001 name type ORF GSPATT00013199001 name type ORF GSPATT00016658001 organism name type scientific Paramecium-tetraurelia dbReference id 5888 type NCBI-Taxonomy lineage taxon Eukaryota taxon Sar taxon Alveolata taxon Ciliophora taxon Intramacronucleata taxon Oligohymenophorea taxon Peniculida taxon Parameciidae taxon Paramecium reference key 1 citation date 2006 first 171 last 178 name Nature type journal-article volume 444 title Global-trends-of-whole-genome-duplications-revealed-by-the-ciliate-Paramecium-tetraurelia. authorList person name Aury-J.-M. person name Jaillon-O. person name Duret-L. person name Noel-B. person name Jubin-C. person name Porcel-B.M. person name Segurens-B. person name Daubin-V. person name Anthouard-V. person name Aiach-N. person name Arnaiz-O. person name Billaut-A. person name Beisson-J. person name Blanc-I. person name Bouhouche-K. person name Camara-F. person name Duharcourt-S. person name Guigo-R. person name Gogendeau-D. person name Katinka-M. person name Keller-A.-M. person name Kissmehl-R. person name Klotz-C. person name Koll-F. person name Le-Mouel-A. person name Lepere-G. person name Malinsky-S. person name Nowacki-M. person name Nowak-J.K. person name Plattner-H. person name Poulain-J. person name Ruiz-F. person name Serrano-V. person name Zagulski-M. person name Dessen-P. person name Betermier-M. person name Weissenbach-J. person name Scarpelli-C. person name Schaechter-V. person name Sperling-L. person name Meyer-E. person name Cohen-J. person name Wincker-P. dbReference id 17086204 type PubMed dbReference id 10.1038/nature05230 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain Stock-d4-2 reference key 2 citation date 2010 first 645 last 655 name Eukaryot.-Cell type journal-article volume 9 title Bug22p,-a-conserved-centrosomal/ciliary-protein-also-present-in-higher-plants,-is-required-for-an-effective-ciliary-stroke-in-Paramecium. authorList person name Laligne-C. person name Klotz-C. person name de-Loubresse-N.G. person name Lemullois-M. person name Hori-M. person name Laurent-F.X. person name Papon-J.F. person name Louis-B. person name Cohen-J. person name Koll-F. dbReference id 20118210 type PubMed dbReference id 10.1128/ec.00368-09 type DOI scope FUNCTION scope SUBCELLULAR-LOCATION comment type function text evidence 1 Cilium--and-flagellum-specific-protein-required-for-axonemal-structure-organization-and-motility.-May-also-play-a-role-in-cortical-organization-of-basal-body. comment type subcellular-location subcellularLocation location evidence 1 Cytoplasm location evidence 1 Cytoskeleton location evidence 1 Cilium-basal-body subcellularLocation location evidence 1 Cell-projection location evidence 1 Cilium text Localizes-preferentially-in-the-terminal-plate-of-the-basal-body-and-the-transition-zone-of-the-cilium-as-well-as-in-the-vicinity-of-the-outer-doublets-of-axoneme-and-between-the-axoneme-and-the-cell-membrane. comment type similarity text evidence 2 Belongs-to-the-CFAP20-family. dbReference id CT868063 type EMBL property type protein-sequence-ID value CAK68801.1 property type molecule-type value Genomic_DNA dbReference id CT868263 type EMBL property type protein-sequence-ID value CAK77302.1 property type molecule-type value Genomic_DNA dbReference id CT868285 type EMBL property type protein-sequence-ID value CAK77734.1 property type molecule-type value Genomic_DNA dbReference id CT868418 type EMBL property type protein-sequence-ID value CAK81845.1 property type molecule-type value Genomic_DNA dbReference id XP_001436198.1 type RefSeq property type nucleotide-sequence-ID value XM_001436161.1 dbReference id XP_001444699.1 type RefSeq property type nucleotide-sequence-ID value XM_001444662.1 dbReference id XP_001445131.1 type RefSeq property type nucleotide-sequence-ID value XM_001445094.1 dbReference id XP_001449242.1 type RefSeq property type nucleotide-sequence-ID value XM_001449205.1 dbReference id A0CDD4 type AlphaFoldDB dbReference id A0CDD4 type SMR dbReference id 5888.CAK68801 type STRING dbReference id CAK68801 type EnsemblProtists property type protein-sequence-ID value CAK68801 property type gene-ID value GSPATT00007012001 dbReference id CAK77302 type EnsemblProtists property type protein-sequence-ID value CAK77302 property type gene-ID value GSPATT00012810001 dbReference id CAK77734 type EnsemblProtists property type protein-sequence-ID value CAK77734 property type gene-ID value GSPATT00013199001 dbReference id CAK81845 type EnsemblProtists property type protein-sequence-ID value CAK81845 property type gene-ID value GSPATT00016658001 dbReference id 5021983 type GeneID dbReference id 5030483 type GeneID dbReference id 5030916 type GeneID dbReference id 5035027 type GeneID dbReference id ptm:GSPATT00007012001 type KEGG dbReference id ptm:GSPATT00012810001 type KEGG dbReference id ptm:GSPATT00013199001 type KEGG dbReference id ptm:GSPATT00016658001 type KEGG dbReference id KOG3213 type eggNOG property type taxonomic-scope value Eukaryota dbReference id CLU_060610_1_1_1 type HOGENOM dbReference id A0CDD4 type InParanoid dbReference id TTYISCP type OMA dbReference id UP000000600 type Proteomes property type component value Partially-assembled-WGS-sequence dbReference id GO:0036064 type GO property type term value C:ciliary-basal-body property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0005929 type GO property type term value C:cilium property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0005737 type GO property type term value C:cytoplasm property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0005874 type GO property type term value C:microtubule property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0031514 type GO property type term value C:motile-cilium property type evidence value ECO:0000318 property type project value GO_Central dbReference id GO:0060271 type GO property type term value P:cilium-assembly property type evidence value ECO:0000315 property type project value UniProtKB dbReference id GO:2000147 type GO property type term value P:positive-regulation-of-cell-motility property type evidence value ECO:0000315 property type project value UniProtKB dbReference id GO:0060296 type GO property type term value P:regulation-of-cilium-beat-frequency-involved-in-ciliary-motility property type evidence value ECO:0000315 property type project value UniProtKB dbReference id IPR040441 type InterPro property type entry-name value CFA20/CFAP20DC dbReference id IPR007714 type InterPro property type entry-name value CFA20_dom dbReference id PTHR12458:SF8 type PANTHER property type entry-name value CILIA--AND-FLAGELLA-ASSOCIATED-PROTEIN-20 property type match-status value 1 dbReference id PTHR12458 type PANTHER property type entry-name value ORF-PROTEIN property type match-status value 1 dbReference id PF05018 type Pfam property type entry-name value CFA20_dom property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0966 Cell-projection keyword id KW-0969 Cilium keyword id KW-0963 Cytoplasm keyword id KW-0206 Cytoskeleton keyword id KW-0493 Microtubule keyword id KW-1185 Reference-proteome feature description Cilia--and-flagella-associated-protein-20 id PRO_0000430500 type chain location begin position 1 end position 191 evidence key 1 type ECO:0000269 source dbReference id 20118210 type PubMed evidence key 2 type ECO:0000305 sequence checksum 580B6B9BE96BD546 length 191 mass 22486 modified 2006-11-28 version 1 MFKNSFQSGFLSILYSIGSKPLQIWDKQIKNGHIKRITDQDIQSSVLEIMGTNVSTNFITAPADPKETLGIKLPFLVMIIKNLKKYFTFEVQVLDDKNVRRRFRASNYQSTTRVKPFICTMPMRLDEGWNQIQFNLSDFTRRAYGTNYIETLRVQIHANCRIRRIYFSDRLYSEEELPPEFKLFLPIQKQG 
entry created 2015-01-07 dataset Swiss-Prot modified 2023-02-22 version 24 accession P0DKH9 name AREP1_ARATH protein recommendedName fullName evidence 3 Auxin-responsive-endogenous-peptide-1 gene name evidence 3 type primary AREP1 name type ordered-locus At1g01335 name evidence 4 type ORF F6F3 organism name type scientific Arabidopsis-thaliana name type common Mouse-ear-cress dbReference id 3702 type NCBI-Taxonomy lineage taxon Eukaryota taxon Viridiplantae taxon Streptophyta taxon Embryophyta taxon Tracheophyta taxon Spermatophyta taxon Magnoliopsida taxon eudicotyledons taxon Gunneridae taxon Pentapetalae taxon rosids taxon malvids taxon Brassicales taxon Brassicaceae taxon Camelineae taxon Arabidopsis reference key 1 citation date 2014 first 635 last 647 name J.-Integr.-Plant-Biol. type journal-article volume 56 title An-auxin-responsive-endogenous-peptide-regulates-root-development-in-Arabidopsis. authorList person name Yang-F. person name Song-Y. person name Yang-H. person name Liu-Z. person name Zhu-G. person name Yang-Y. dbReference id 24479837 type PubMed dbReference id 10.1111/jipb.12178 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] scope IDENTIFICATION scope FUNCTION scope INDUCTION-BY-AUXIN scope SUBCELLULAR-LOCATION scope DEVELOPMENTAL-STAGE scope TISSUE-SPECIFICITY source strain cv.-Columbia reference key 2 citation date 2000 first 816 last 820 name Nature type journal-article volume 408 title Sequence-and-analysis-of-chromosome-1-of-the-plant-Arabidopsis-thaliana. authorList person name Theologis-A. person name Ecker-J.R. person name Palm-C.J. person name Federspiel-N.A. person name Kaul-S. person name White-O. person name Alonso-J. person name Altafi-H. person name Araujo-R. person name Bowman-C.L. person name Brooks-S.Y. person name Buehler-E. person name Chan-A. person name Chao-Q. person name Chen-H. person name Cheuk-R.F. person name Chin-C.W. person name Chung-M.K. person name Conn-L. person name Conway-A.B. person name Conway-A.R. person name Creasy-T.H. person name Dewar-K. person name Dunn-P. person name Etgu-P. person name Feldblyum-T.V. person name Feng-J.-D. person name Fong-B. person name Fujii-C.Y. person name Gill-J.E. person name Goldsmith-A.D. person name Haas-B. person name Hansen-N.F. person name Hughes-B. person name Huizar-L. person name Hunter-J.L. person name Jenkins-J. person name Johnson-Hopson-C. person name Khan-S. person name Khaykin-E. person name Kim-C.J. person name Koo-H.L. person name Kremenetskaia-I. person name Kurtz-D.B. person name Kwan-A. person name Lam-B. person name Langin-Hooper-S. person name Lee-A. person name Lee-J.M. person name Lenz-C.A. person name Li-J.H. person name Li-Y.-P. person name Lin-X. person name Liu-S.X. person name Liu-Z.A. person name Luros-J.S. person name Maiti-R. person name Marziali-A. person name Militscher-J. person name Miranda-M. person name Nguyen-M. person name Nierman-W.C. person name Osborne-B.I. person name Pai-G. person name Peterson-J. person name Pham-P.K. person name Rizzo-M. person name Rooney-T. person name Rowley-D. person name Sakano-H. person name Salzberg-S.L. person name Schwartz-J.R. person name Shinn-P. person name Southwick-A.M. person name Sun-H. person name Tallon-L.J. person name Tambunga-G. person name Toriumi-M.J. person name Town-C.D. person name Utterback-T. person name Van-Aken-S. person name Vaysberg-M. person name Vysotskaia-V.S. person name Walker-M. person name Wu-D. person name Yu-G. person name Fraser-C.M. person name Venter-J.C. person name Davis-R.W. dbReference id 11130712 type PubMed dbReference id 10.1038/35048500 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain cv.-Columbia reference key 3 citation date 2017 first 789 last 804 name Plant-J. type journal-article volume 89 title Araport11:-a-complete-reannotation-of-the-Arabidopsis-thaliana-reference-genome. authorList person name Cheng-C.Y. person name Krishnakumar-V. person name Chan-A.P. person name Thibaud-Nissen-F. person name Schobel-S. person name Town-C.D. dbReference id 27862469 type PubMed dbReference id 10.1111/tpj.13415 type DOI scope GENOME-REANNOTATION source strain cv.-Columbia comment type function text evidence 2 Negative-regulator-of-the-auxin-response. comment type subcellular-location subcellularLocation location evidence 2 Cytoplasm subcellularLocation location evidence 2 Nucleus subcellularLocation location evidence 1 Membrane topology evidence 1 Single-pass-membrane-protein text evidence 2 Not-localized-under-normal-conditions,-but-found-in-the-cytoplasm-and-in-the-nucleus-when-auxin-is-added. comment type tissue-specificity text evidence 2 Expressed-in-cotyledons,-hypocotyls,-roots,-newly-developing-leaves-and-shoot-apical-meristem.-Not-detected-in-flowers,-siliques-or-mature-leaves. comment type developmental-stage text evidence 2 Expressed-during-the-primary-developmental-stages. comment type induction text evidence 2 Up-regulated-by-auxin. comment type miscellaneous text evidence 2 Knock-down-mutants-have-no-visible-phenotype-in-the-absence-of-exogenous-auxin,-but-are-more-sensitive-to-auxin-induced-inhibition-of-root-elongation-and-initiation-of-lateral-roots. dbReference id AC023628 type EMBL property type status value NOT_ANNOTATED_CDS property type molecule-type value Genomic_DNA dbReference id CP002684 type EMBL property type protein-sequence-ID value ANM60886.1 property type molecule-type value Genomic_DNA dbReference id NP_001323136.1 type RefSeq property type nucleotide-sequence-ID value NM_001331266.1 dbReference id P0DKH9 type AlphaFoldDB dbReference id AT1G01335.1 type EnsemblPlants property type protein-sequence-ID value AT1G01335.1 property type gene-ID value AT1G01335 dbReference id 28716020 type GeneID dbReference id AT1G01335.1 type Gramene property type protein-sequence-ID value AT1G01335.1 property type gene-ID value AT1G01335 dbReference id ath:AT1G01335 type KEGG dbReference id AT1G01335 type Araport dbReference id 5562675at2759 type OrthoDB dbReference id PR:P0DKH9 type PRO dbReference id UP000006548 type Proteomes property type component value Chromosome-1 dbReference id GO:0005737 type GO property type term value C:cytoplasm property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0016020 type GO property type term value C:membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0005634 type GO property type term value C:nucleus property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0009734 type GO property type term value P:auxin-activated-signaling-pathway property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0010930 type GO property type term value P:negative-regulation-of-auxin-mediated-signaling-pathway property type evidence value ECO:0000315 property type project value UniProtKB dbReference id GO:0048364 type GO property type term value P:root-development property type evidence value ECO:0000315 property type project value UniProtKB proteinExistence type evidence-at-transcript-level keyword id KW-0927 Auxin-signaling-pathway keyword id KW-0963 Cytoplasm keyword id KW-0472 Membrane keyword id KW-0539 Nucleus keyword id KW-1185 Reference-proteome keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix feature description Auxin-responsive-endogenous-peptide-1 id PRO_0000431425 type chain location begin position 1 end position 40 feature description Helical evidence 1 type transmembrane-region location begin position 7 end position 29 evidence key 1 type ECO:0000255 evidence key 2 type ECO:0000269 source dbReference id 24479837 type PubMed evidence key 3 type ECO:0000303 source dbReference id 24479837 type PubMed evidence key 4 type ECO:0000312 source dbReference id AC023628 type EMBL sequence checksum F9C5C75E99E2CE63 length 40 mass 4747 modified 2015-01-07 version 1 MGLSDCLIYRLVVRCFLDYSICAPFYFYHKFMLSASEPVF 
entry created 2015-03-04 dataset Swiss-Prot modified 2023-02-22 version 20 accession P0DMS4 name APOA1_LEPWE protein recommendedName fullName Apolipoprotein-A-I shortName Apo-AI shortName ApoA-I alternativeName fullName Apolipoprotein-A1 component recommendedName fullName Proapolipoprotein-A-I shortName ProapoA-I component recommendedName fullName Truncated-apolipoprotein-A-I gene name type primary APOA1 organism name type scientific Leptonychotes-weddellii name type common Weddell-seal name type synonym Otaria-weddellii dbReference id 9713 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Chordata taxon Craniata taxon Vertebrata taxon Euteleostomi taxon Mammalia taxon Eutheria taxon Laurasiatheria taxon Carnivora taxon Caniformia taxon Phocidae taxon Leptonychotes reference key 1 citation date 2013-04 db EMBL/GenBank/DDBJ-databases type submission authorList person name Di-Palma-F. person name Alfoldi-J. person name Johnson-J. person name Berlin-A. person name Gnerre-S. person name Jaffe-D. person name MacCallum-I. person name Young-S. person name Walker-B.J. person name Lindblad-Toh-K. scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] reference key 2 citation date 2014-12 type unpublished-observations authorList person name Puppione-D.L. scope IDENTIFICATION comment type function text evidence 3 Participates-in-the-reverse-transport-of-cholesterol-from-tissues-to-the-liver-for-excretion-by-promoting-cholesterol-efflux-from-tissues-and-by-acting-as-a-cofactor-for-the-lecithin-cholesterol-acyltransferase-(LCAT).-As-part-of-the-SPAP-complex,-activates-spermatozoa-motility. comment type subunit text evidence 2-3-5 Homodimer-(By-similarity).-Interacts-with-APOA1BP-and-CLU.-Component-of-a-sperm-activating-protein-complex-(SPAP),-consisting-of-APOA1,-an-immunoglobulin-heavy-chain,-an-immunoglobulin-light-chain-and-albumin.-Interacts-with-NDRG1.-Interacts-with-SCGB3A2-(By-similarity).-Interacts-with-NAXE-and-YJEFN3-(By-similarity). comment type subcellular-location subcellularLocation location evidence 3 Secreted comment type PTM text evidence 4 Glycosylated. comment type PTM text evidence 4 Palmitoylated. comment type PTM text evidence 1 Phosphorylation-sites-are-present-in-the-extracellular-medium. comment type similarity text evidence 7 Belongs-to-the-apolipoprotein-A1/A4/E-family. dbReference id APMU01110376 type EMBL property type status value NOT_ANNOTATED_CDS property type molecule-type value Genomic_DNA dbReference id XP_006743516.1 type RefSeq property type nucleotide-sequence-ID value XM_006743453.1 dbReference id P0DMS4 type AlphaFoldDB dbReference id P0DMS4 type SMR dbReference id 9713.XP_006743516.1 type STRING dbReference id 102732504 type GeneID dbReference id 335 type CTD dbReference id 5310876at2759 type OrthoDB dbReference id UP000245341 type Proteomes property type component value Unplaced dbReference id GO:0034364 type GO property type term value C:high-density-lipoprotein-particle property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0008289 type GO property type term value F:lipid-binding property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0042803 type GO property type term value F:protein-homodimerization-activity property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:0008203 type GO property type term value P:cholesterol-metabolic-process property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0006869 type GO property type term value P:lipid-transport property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0042157 type GO property type term value P:lipoprotein-metabolic-process property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0010875 type GO property type term value P:positive-regulation-of-cholesterol-efflux property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:0050766 type GO property type term value P:positive-regulation-of-phagocytosis property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:1902995 type GO property type term value P:positive-regulation-of-phospholipid-efflux property type evidence value ECO:0000250 property type project value UniProtKB dbReference id GO:0050821 type GO property type term value P:protein-stabilization property type evidence value ECO:0000250 property type project value UniProtKB dbReference id 1.20.5.20 type Gene3D property type match-status value 1 dbReference id 6.10.140.380 type Gene3D property type match-status value 1 dbReference id 1.20.120.20 type Gene3D property type entry-name value Apolipoprotein property type match-status value 1 dbReference id IPR000074 type InterPro property type entry-name value ApoA_E dbReference id PTHR18976 type PANTHER property type entry-name value APOLIPOPROTEIN property type match-status value 1 dbReference id PTHR18976:SF11 type PANTHER property type entry-name value APOLIPOPROTEIN-A-I property type match-status value 1 dbReference id PF01442 type Pfam property type entry-name value Apolipoprotein property type match-status value 1 dbReference id SSF58113 type SUPFAM property type entry-name value Apolipoprotein-A-I property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0153 Cholesterol-metabolism keyword id KW-0325 Glycoprotein keyword id KW-0345 HDL keyword id KW-0443 Lipid-metabolism keyword id KW-0445 Lipid-transport keyword id KW-0449 Lipoprotein keyword id KW-0558 Oxidation keyword id KW-0564 Palmitate keyword id KW-0597 Phosphoprotein keyword id KW-1185 Reference-proteome keyword id KW-0677 Repeat keyword id KW-0964 Secreted keyword id KW-0732 Signal keyword id KW-0753 Steroid-metabolism keyword id KW-1207 Sterol-metabolism keyword id KW-0813 Transport feature evidence 6 type signal-peptide location begin position 1 end position 18 feature description Proapolipoprotein-A-I id PRO_0000432004 type chain location begin position 19 end position 266 feature description Apolipoprotein-A-I id PRO_0000432005 type chain location begin position 25 end position 266 feature description Truncated-apolipoprotein-A-I evidence 3 id PRO_0000432006 type chain location begin position 25 end position 265 feature description 1 type repeat location begin position 67 end position 88 feature description 2 type repeat location begin position 89 end position 110 feature description 3;-half-length type repeat location begin position 111 end position 121 feature description 4 type repeat location begin position 122 end position 143 feature description 5 type repeat location begin position 144 end position 165 feature description 6 type repeat location begin position 166 end position 187 feature description 7 type repeat location begin position 188 end position 209 feature description 8 type repeat location begin position 210 end position 231 feature description 9;-half-length type repeat location begin position 232 end position 242 feature description 10 type repeat location begin position 243 end position 266 feature description 10-X-approximate-tandem-repeats type region-of-interest location begin position 67 end position 266 feature description Methionine-sulfoxide evidence 3 type modified-residue location position position 109 evidence key 1 type ECO:0000250 evidence key 2 type ECO:0000250 source dbReference id G5BQH5 type UniProtKB evidence key 3 type ECO:0000250 source dbReference id P02647 type UniProtKB evidence key 4 type ECO:0000250 source dbReference id P02648 type UniProtKB evidence key 5 type ECO:0000250 source dbReference id P04639 type UniProtKB evidence key 6 type ECO:0000255 evidence key 7 type ECO:0000305 sequence checksum 9ECDD0778737CF3B length 266 mass 30311 modified 2015-03-04 precursor true version 1 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