entry created 2001-09-26 dataset Swiss-Prot modified 2023-02-22 version 174 accession Q94981 accession Q0KHQ9 name ARI1_DROME protein recommendedName fullName evidence 9 E3-ubiquitin-protein-ligase-ariadne-1 ecNumber evidence 5-6 2.3.2.31 alternativeName fullName evidence 7 Protein-ariadne-1 alternativeName fullName evidence 10 RING-type-E3-ubiquitin-transferase-ariadne-1 gene name evidence 7-11 type primary ari-1 name type synonym ari name evidence 8 type synonym ari-1a name evidence 11 type ORF CG5659 organism name type scientific Drosophila-melanogaster name type common Fruit-fly dbReference id 7227 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Ecdysozoa taxon Arthropoda taxon Hexapoda taxon Insecta taxon Pterygota taxon Neoptera taxon Endopterygota taxon Diptera taxon Brachycera taxon Muscomorpha taxon Ephydroidea taxon Drosophilidae taxon Drosophila taxon Sophophora reference key 1 citation date 2000 first 1231 last 1244 name Genetics type journal-article volume 155 title Ariadne-1:-a-vital-Drosophila-gene-is-required-in-development-and-defines-a-new-conserved-family-of-ring-finger-proteins. authorList person name Aguilera-M. person name Oliveros-M. person name Martinez-Padron-M. person name Barbas-J.A. person name Ferrus-A. dbReference id 10880484 type PubMed dbReference id 10.1093/genetics/155.3.1231 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA-/-MRNA] scope FUNCTION scope SUBUNIT scope INTERACTION-WITH-UBC10 scope SUBCELLULAR-LOCATION scope TISSUE-SPECIFICITY scope DEVELOPMENTAL-STAGE scope MUTAGENESIS-OF-CYS-150-AND-CYS-309 source strain Oregon-R reference key 2 citation date 2000 first 2185 last 2195 name Science type journal-article volume 287 title The-genome-sequence-of-Drosophila-melanogaster. authorList person name Adams-M.D. person name Celniker-S.E. person name Holt-R.A. person name Evans-C.A. person name Gocayne-J.D. person name Amanatides-P.G. person name Scherer-S.E. person name Li-P.W. person name Hoskins-R.A. person name Galle-R.F. person name George-R.A. person name Lewis-S.E. person name Richards-S. person name Ashburner-M. person name Henderson-S.N. person name Sutton-G.G. person name Wortman-J.R. person name Yandell-M.D. person name Zhang-Q. person name Chen-L.X. person name Brandon-R.C. person name Rogers-Y.-H.C. person name Blazej-R.G. person name Champe-M. person name Pfeiffer-B.D. person name Wan-K.H. person name Doyle-C. person name Baxter-E.G. person name Helt-G. person name Nelson-C.R. person name Miklos-G.L.G. person name Abril-J.F. person name Agbayani-A. person name An-H.-J. person name Andrews-Pfannkoch-C. person name Baldwin-D. person name Ballew-R.M. person name Basu-A. person name Baxendale-J. person name Bayraktaroglu-L. person name Beasley-E.M. person name Beeson-K.Y. person name Benos-P.V. person name Berman-B.P. person name Bhandari-D. person name Bolshakov-S. person name Borkova-D. person name Botchan-M.R. person name Bouck-J. person name Brokstein-P. person name Brottier-P. person name Burtis-K.C. person name Busam-D.A. person name Butler-H. person name Cadieu-E. person name Center-A. person name Chandra-I. person name Cherry-J.M. person name Cawley-S. person name Dahlke-C. person name Davenport-L.B. person name Davies-P. person name de-Pablos-B. person name Delcher-A. person name Deng-Z. person name Mays-A.D. person name Dew-I. person name Dietz-S.M. person name Dodson-K. person name Doup-L.E. person name Downes-M. person name Dugan-Rocha-S. person name Dunkov-B.C. person name Dunn-P. person name Durbin-K.J. person name Evangelista-C.C. person name Ferraz-C. person name Ferriera-S. person name Fleischmann-W. person name Fosler-C. person name Gabrielian-A.E. person name Garg-N.S. person name Gelbart-W.M. person name Glasser-K. person name Glodek-A. person name Gong-F. person name Gorrell-J.H. person name Gu-Z. person name Guan-P. person name Harris-M. person name Harris-N.L. person name Harvey-D.A. person name Heiman-T.J. person name Hernandez-J.R. person name Houck-J. person name Hostin-D. person name Houston-K.A. person name Howland-T.J. person name Wei-M.-H. person name Ibegwam-C. person name Jalali-M. person name Kalush-F. person name Karpen-G.H. person name Ke-Z. person name Kennison-J.A. person name Ketchum-K.A. person name Kimmel-B.E. person name Kodira-C.D. person name Kraft-C.L. person name Kravitz-S. person name Kulp-D. person name Lai-Z. person name Lasko-P. person name Lei-Y. person name Levitsky-A.A. person name Li-J.H. person name Li-Z. person name Liang-Y. person name Lin-X. person name Liu-X. person name Mattei-B. person name McIntosh-T.C. person name McLeod-M.P. person name McPherson-D. person name Merkulov-G. person name Milshina-N.V. person name Mobarry-C. person name Morris-J. person name Moshrefi-A. person name Mount-S.M. person name Moy-M. person name Murphy-B. person name Murphy-L. person name Muzny-D.M. person name Nelson-D.L. person name Nelson-D.R. person name Nelson-K.A. person name Nixon-K. person name Nusskern-D.R. person name Pacleb-J.M. person name Palazzolo-M. person name Pittman-G.S. person name Pan-S. person name Pollard-J. person name Puri-V. person name Reese-M.G. person name Reinert-K. person name Remington-K. person name Saunders-R.D.C. person name Scheeler-F. person name Shen-H. person name Shue-B.C. person name Siden-Kiamos-I. person name Simpson-M. person name Skupski-M.P. person name Smith-T.J. person name Spier-E. person name Spradling-A.C. person name Stapleton-M. person name Strong-R. person name Sun-E. person name Svirskas-R. person name Tector-C. person name Turner-R. person name Venter-E. person name Wang-A.H. person name Wang-X. person name Wang-Z.-Y. person name Wassarman-D.A. person name Weinstock-G.M. person name Weissenbach-J. person name Williams-S.M. person name Woodage-T. person name Worley-K.C. person name Wu-D. person name Yang-S. person name Yao-Q.A. person name Ye-J. person name Yeh-R.-F. person name Zaveri-J.S. person name Zhan-M. person name Zhang-G. person name Zhao-Q. person name Zheng-L. person name Zheng-X.H. person name Zhong-F.N. person name Zhong-W. person name Zhou-X. person name Zhu-S.C. person name Zhu-X. person name Smith-H.O. person name Gibbs-R.A. person name Myers-E.W. person name Rubin-G.M. person name Venter-J.C. dbReference id 10731132 type PubMed dbReference id 10.1126/science.287.5461.2185 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain Berkeley reference key 3 citation date 2002 first RESEARCH0083.1 last RESEARCH0083.22 name Genome-Biol. type journal-article volume 3 title Annotation-of-the-Drosophila-melanogaster-euchromatic-genome:-a-systematic-review. authorList person name Misra-S. person name Crosby-M.A. person name Mungall-C.J. person name Matthews-B.B. person name Campbell-K.S. person name Hradecky-P. person name Huang-Y. person name Kaminker-J.S. person name Millburn-G.H. person name Prochnik-S.E. person name Smith-C.D. person name Tupy-J.L. person name Whitfield-E.J. person name Bayraktaroglu-L. person name Berman-B.P. person name Bettencourt-B.R. person name Celniker-S.E. person name de-Grey-A.D.N.J. person name Drysdale-R.A. person name Harris-N.L. person name Richter-J. person name Russo-S. person name Schroeder-A.J. person name Shu-S.Q. person name Stapleton-M. person name Yamada-C. person name Ashburner-M. person name Gelbart-W.M. person name Rubin-G.M. person name Lewis-S.E. dbReference id 12537572 type PubMed dbReference id 10.1186/gb-2002-3-12-research0083 type DOI scope GENOME-REANNOTATION source strain Berkeley reference key 4 citation date 2011 first 871 last 883 name Genetics type journal-article volume 189 title Isoform-specific-regulation-of-a-steroid-hormone-nuclear-receptor-by-an-E3-ubiquitin-ligase-in-Drosophila-melanogaster. authorList person name Gradilla-A.C. person name Mansilla-A. person name Ferrus-A. dbReference id 21900267 type PubMed dbReference id 10.1534/genetics.111.132191 type DOI scope FUNCTION scope CATALYTIC-ACTIVITY scope INTERACTION-WITH-ECR-(ISOFORM-ECR-A) scope SUBCELLULAR-LOCATION reference key 5 citation date 2018 first 226 last 244 name Dev.-Cell type journal-article volume 45 title Ari-1-Regulates-Myonuclear-Organization-Together-with-Parkin-and-Is-Associated-with-Aortic-Aneurysms. authorList consortium name University-of-Washington-Center-for-Mendelian-Genomics person name Tan-K.L. person name Haelterman-N.A. person name Kwartler-C.S. person name Regalado-E.S. person name Lee-P.T. person name Nagarkar-Jaiswal-S. person name Guo-D.C. person name Duraine-L. person name Wangler-M.F. person name Bamshad-M.J. person name Nickerson-D.A. person name Lin-G. person name Milewicz-D.M. person name Bellen-H.J. dbReference id 29689197 type PubMed dbReference id 10.1016/j.devcel.2018.03.020 type DOI scope FUNCTION scope CATALYTIC-ACTIVITY scope SUBUNIT scope INTERACTION-WITH-UBC10;-KOI;-PARK-AND-ARI-2 scope TISSUE-SPECIFICITY scope DOMAIN scope AUTOPHOSPHORYLATION scope DISRUPTION-PHENOTYPE scope MUTAGENESIS-OF-CYS-136;-VAL-187;-CYS-223;-CYS-304;-SER-332;-PHE-377;-GLU-378-AND-GLU-450 comment type function text evidence 4-5-6 Atypical-E3-ubiquitin-protein-ligase,-which-catalyzes-ubiquitination-of-target-proteins-together-with-ubiquitin-conjugating-enzyme-E2-Ubc10-(PubMed:10880484,-PubMed:21900267,-PubMed:29689197).-Controls-the-subcellular-localization-and-morphology-of-muscle-nuclei-(myonuclei)-by-regulating-the-protein-levels-and-distribution-of-the-LINC-(LInker-of-Nucleoskeleton-and-Cytoskeleton)-complex-(PubMed:29689197).-Functions-by-mediating-the-monoubiquitination-of-the-LINC-complex-subunit-koi-leading-to-its-subsequent-proteasomal-degradation-(PubMed:29689197).-Appears-to-function,-at-least-partially-redundantly,-with-the-RBR-E3-ligase-family-member-park-in-nuclear-localization-and-morphology-(PubMed:29689197).-Likely-to-function-in-metamorphosis-by-regulating-the-proteins-levels-of-EcR-isoform-A-(ECR-A)-and-its-heterodimeric-partner-usp,-via-the-ubiquitination-and-subsequent-degradation-of-ECR-A-(PubMed:21900267). comment type catalytic-activity reaction evidence 5-6 text [E2-ubiquitin-conjugating-enzyme]-S-ubiquitinyl-L-cysteine-+-[acceptor-protein]-L-lysine-=-[E2-ubiquitin-conjugating-enzyme]-L-cysteine-+-[acceptor-protein]-N(6)-ubiquitinyl-L-lysine. dbReference id 2.3.2.31 type EC comment type subunit text evidence 4-5-6 Can-form-homodimers-(PubMed:10880484,-PubMed:29689197).-Interacts-(via-RING-type-1-zinc-finger)-with-Ubc10-(PubMed:10880484,-PubMed:29689197).-Interacts-with-the-LINC-complex-member-koi-(PubMed:29689197).-Interacts-with-park-(PubMed:29689197).-Interacts-with-ari-2-(PubMed:29689197).-Specifically-interacts-with-isoform-ECR-A-of-EcR-(PubMed:21900267). comment type subcellular-location subcellularLocation location evidence 4 Cytoplasm subcellularLocation location evidence 5 Nucleus text evidence 4 Mainly-cytoplasmic. comment type tissue-specificity text evidence 4-6 Widely-expressed,-with-prominent-levels-in-the-nervous-system-and-female-gonads. comment type developmental-stage text evidence 4 Expressed-in-all-tissues-throughout-development,-with-maximum-levels-reached-during-metamorphosis-and-maintained-in-the-adult. comment type domain text evidence 6 Members-of-the-RBR-family-are-atypical-E3-ligases.-They-interact-with-E2-conjugating-enzymes-such-as-Ubc10-and-function-like-HECT-type-E3-enzymes:-they-bind-E2s-via-the-first-RING-type-zinc-finger,-but-require-an-obligate-trans-thiolation-step-during-the-ubiquitin-transfer,-requiring-a-conserved-active-site-Cys-residue-in-the-second-RING-type-zinc-finger.-The-active-site-probably-forms-a-thioester-intermediate-with-ubiquitin-taken-from-the-active-site-cysteine-of-the-E2-before-ultimately-transferring-it-to-a-Lys-residue-on-the-substrate. comment type PTM text evidence 6 Autophosphorylated. comment type disruption-phenotype text evidence 6 Pharate-pupae-lethal.-Larval-muscles-exhibit-an-increase-in-nuclear-clustering. comment type similarity text evidence 10 Belongs-to-the-RBR-family.-Ariadne-subfamily. dbReference evidence 5-6 id 2.3.2.31 type EC dbReference id X98309 type EMBL property type protein-sequence-ID value CAA66953.1 property type molecule-type value Genomic_DNA dbReference id X98310 type EMBL property type protein-sequence-ID value CAA66954.1 property type molecule-type value mRNA dbReference id AE014298 type EMBL property type protein-sequence-ID value AAN09462.1 property type molecule-type value Genomic_DNA dbReference id NP_001245736.1 type RefSeq property type nucleotide-sequence-ID value NM_001258807.3 dbReference id NP_001259671.1 type RefSeq property type nucleotide-sequence-ID value NM_001272742.2 dbReference id NP_001259672.1 type RefSeq property type nucleotide-sequence-ID value NM_001272743.1 dbReference id NP_523399.1 type RefSeq property type nucleotide-sequence-ID value NM_078675.4 dbReference id NP_728145.1 type RefSeq property type nucleotide-sequence-ID value NM_167610.4 dbReference id NP_996500.1 type RefSeq property type nucleotide-sequence-ID value NM_206777.2 dbReference id Q94981 type AlphaFoldDB dbReference id Q94981 type SMR dbReference id 59116 type BioGRID property type interactions value 13 dbReference id DIP-17812N type DIP dbReference id Q94981 type IntAct property type interactions value 1 dbReference id 7227.FBpp0297199 type STRING dbReference id Q94981 type PaxDb dbReference id FBtr0089506 type EnsemblMetazoa property type protein-sequence-ID value FBpp0088499 property type gene-ID value FBgn0017418 dbReference id FBtr0089507 type EnsemblMetazoa property type protein-sequence-ID value FBpp0088500 property type gene-ID value FBgn0017418 dbReference id FBtr0089508 type EnsemblMetazoa property type protein-sequence-ID value FBpp0089023 property type gene-ID value FBgn0017418 dbReference id FBtr0306057 type EnsemblMetazoa property type protein-sequence-ID value FBpp0297199 property type gene-ID value FBgn0017418 dbReference id FBtr0332850 type EnsemblMetazoa property type protein-sequence-ID value FBpp0305073 property type gene-ID value FBgn0017418 dbReference id FBtr0332851 type EnsemblMetazoa property type protein-sequence-ID value FBpp0305074 property type gene-ID value FBgn0017418 dbReference id 32796 type GeneID dbReference id dme:Dmel_CG5659 type KEGG dbReference id CG5659-RA type UCSC property type organism-name value d.-melanogaster dbReference id FB:FBgn0017418 type AGR dbReference id 32796 type CTD dbReference id FBgn0017418 type FlyBase property type gene-designation value ari-1 dbReference id VectorBase:FBgn0017418 type VEuPathDB dbReference id KOG1815 type eggNOG property type taxonomic-scope value Eukaryota dbReference id ENSGT00940000155744 type GeneTree dbReference id CLU_009823_4_2_1 type HOGENOM dbReference id Q94981 type InParanoid dbReference id CAAHACD type OMA dbReference id 3084186at2759 type OrthoDB dbReference id Q94981 type PhylomeDB dbReference id R-DME-1169408 type Reactome property type pathway-name value ISG15-antiviral-mechanism dbReference id Q94981 type SignaLink dbReference id 32796 type BioGRID-ORCS property type hits value 1-hit-in-1-CRISPR-screen dbReference id 32796 type GenomeRNAi dbReference id PR:Q94981 type PRO dbReference id UP000000803 type Proteomes property type component value Chromosome-X dbReference id FBgn0017418 type Bgee property type expression-patterns value Expressed-in-cleaving-embryo-and-23-other-tissues dbReference id Q94981 type ExpressionAtlas property type expression-patterns value baseline-and-differential dbReference id Q94981 type Genevisible property type organism-ID value DM dbReference id GO:0005737 type GO property type term value C:cytoplasm property type evidence value ECO:0000318 property type project value GO_Central dbReference id GO:0005829 type GO property type term value C:cytosol property type evidence value ECO:0000314 property type project value FlyBase dbReference id GO:0005634 type GO property type term value C:nucleus property type evidence value ECO:0000314 property type project value FlyBase dbReference id GO:0000151 type GO property type term value C:ubiquitin-ligase-complex property type evidence value ECO:0000318 property type project value GO_Central dbReference id GO:0031624 type GO property type term value F:ubiquitin-conjugating-enzyme-binding property type evidence value ECO:0000353 property type project value FlyBase dbReference id GO:0061630 type GO property type term value F:ubiquitin-protein-ligase-activity property type evidence value ECO:0000314 property type project value FlyBase dbReference id GO:0008270 type GO property type term value F:zinc-ion-binding property type evidence value ECO:0000255 property type project value FlyBase dbReference id GO:0007029 type GO property type term value P:endoplasmic-reticulum-organization property type evidence value ECO:0000315 property type project value FlyBase dbReference id GO:0048477 type GO property type term value P:oogenesis property type evidence value ECO:0000315 property type project value FlyBase dbReference id GO:0050769 type GO property type term value P:positive-regulation-of-neurogenesis property type evidence value ECO:0000315 property type project value FlyBase dbReference id GO:1901800 type GO property type term value P:positive-regulation-of-proteasomal-protein-catabolic-process property type evidence value ECO:0000315 property type project value FlyBase dbReference id GO:0032436 type GO property type term value P:positive-regulation-of-proteasomal-ubiquitin-dependent-protein-catabolic-process property type evidence value ECO:0000318 property type project value GO_Central dbReference id GO:0006513 type GO property type term value P:protein-monoubiquitination property type evidence value ECO:0000314 property type project value FlyBase dbReference id GO:0000209 type GO property type term value P:protein-polyubiquitination property type evidence value ECO:0000318 property type project value GO_Central dbReference id GO:0016567 type GO property type term value P:protein-ubiquitination property type evidence value ECO:0000314 property type project value FlyBase dbReference id GO:0006511 type GO property type term value P:ubiquitin-dependent-protein-catabolic-process property type evidence value ECO:0000315 property type project value FlyBase dbReference id cd16626 type CDD property type entry-name value RING-HC_RBR_HHARI property type match-status value 1 dbReference id 1.20.120.1750 type Gene3D property type match-status value 1 dbReference id 3.30.40.10 type Gene3D property type entry-name value Zinc/RING-finger-domain,-C3HC4-(zinc-finger) property type match-status value 1 dbReference id IPR045840 type InterPro property type entry-name value Ariadne dbReference id IPR031127 type InterPro property type entry-name value E3_UB_ligase_RBR dbReference id IPR002867 type InterPro property type entry-name value IBR_dom dbReference id IPR044066 type InterPro property type entry-name value TRIAD_supradom dbReference id IPR018957 type InterPro property type entry-name value Znf_C3HC4_RING-type dbReference id IPR001841 type InterPro property type entry-name value Znf_RING dbReference id IPR013083 type InterPro property type entry-name value Znf_RING/FYVE/PHD dbReference id PTHR11685:SF212 type PANTHER property type entry-name value E3-UBIQUITIN-PROTEIN-LIGASE-ARIH1 property type match-status value 1 dbReference id PTHR11685 type PANTHER property type entry-name value RBR-FAMILY-RING-FINGER-AND-IBR-DOMAIN-CONTAINING property type match-status value 1 dbReference id PF19422 type Pfam property type entry-name value Ariadne property type match-status value 1 dbReference id PF01485 type Pfam property type entry-name value IBR property type match-status value 2 dbReference id PF00097 type Pfam property type entry-name value zf-C3HC4 property type match-status value 1 dbReference id SM00647 type SMART property type entry-name value IBR property type match-status value 2 dbReference id SSF57850 type SUPFAM property type entry-name value RING/U-box property type match-status value 3 dbReference id PS51873 type PROSITE property type entry-name value TRIAD property type match-status value 1 dbReference id PS50089 type PROSITE property type entry-name value ZF_RING_2 property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0175 Coiled-coil keyword id KW-0963 Cytoplasm keyword id KW-0479 Metal-binding keyword id KW-0539 Nucleus keyword id KW-0597 Phosphoprotein keyword id KW-1185 Reference-proteome keyword id KW-0677 Repeat keyword id KW-0808 Transferase keyword id KW-0833 Ubl-conjugation-pathway keyword id KW-0862 Zinc keyword id KW-0863 Zinc-finger feature description E3-ubiquitin-protein-ligase-ariadne-1 id PRO_0000055754 type chain location begin position 1 end position 503 feature description RING-type-1 evidence 2 type zinc-finger-region location begin position 133 end position 183 feature description IBR-type evidence 2 type zinc-finger-region location begin position 203 end position 264 feature description RING-type-2;-atypical evidence 2 type zinc-finger-region location begin position 291 end position 322 feature description Disordered evidence 3 type region-of-interest location begin position 1 end position 40 feature description TRIAD-supradomain evidence 2 type region-of-interest location begin position 129 end position 340 feature description Important-for-interaction-with-Ubc10 evidence 4 type region-of-interest location begin position 133 end position 201 feature evidence 1 type coiled-coil-region location begin position 341 end position 361 feature evidence 2 type active-site location position position 304 feature evidence 2 type binding-site location position position 133 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 1 feature evidence 2 type binding-site location position position 136 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 1 feature evidence 2 type binding-site location position position 150 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 2 feature evidence 2 type binding-site location position position 152 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 2 feature evidence 2 type binding-site location position position 155 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 1 feature evidence 2 type binding-site location position position 158 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 1 feature evidence 2 type binding-site location position position 178 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 2 feature evidence 2 type binding-site location position position 183 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 2 feature evidence 2 type binding-site location position position 223 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 3 feature evidence 2 type binding-site location position position 228 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 3 feature evidence 2 type binding-site location position position 244 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 3 feature evidence 2 type binding-site location position position 246 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 3 feature evidence 2 type binding-site location position position 251 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 4 feature evidence 2 type binding-site location position position 254 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 4 feature evidence 2 type binding-site location position position 259 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 4 feature evidence 2 type binding-site location position position 264 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 4 feature evidence 2 type binding-site location position position 291 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 5 feature evidence 2 type binding-site location position position 294 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 5 feature evidence 2 type binding-site location position position 309 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 5 feature evidence 2 type binding-site location position position 314 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 5 feature evidence 2 type binding-site location position position 319 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 6 feature evidence 2 type binding-site location position position 322 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 6 feature evidence 2 type binding-site location position position 329 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 6 feature evidence 2 type binding-site location position position 336 ligand name Zn(2+) dbReference id CHEBI:29105 type ChEBI label 6 feature description In-ari-1a;-Loss-of-catalytic-activity.-Late-pupal-lethal-and-adult-escapers-have-a-reduced-lifespan-and-thinner-bristles.-Nuclei-in-larval-muscles-(myonuclei)-are-displaced-from-the-cell-membrane,-exhibit-clustering-and-morphological-defects,-likely-due-to-the-mislocalization-of-the-LINC-complex.-Reduced-degradation-of-the-LINC-complex-member-koi. evidence 6 type mutagenesis-site original C variation Y location position position 136 feature description In-ari1-2;-lethal-phenotype-and-loss-of-interaction-with-Ubc10. evidence 4 type mutagenesis-site original C variation Y location position position 150 feature description In-ari-1b;-Loss-of-catalytic-activity.-Late-pupal-lethal-and-adult-escapers-have-a-reduced-lifespan-and-thinner-bristles.-Nuclei-in-larval-muscles-(myonuclei)-are-displaced-from-the-cell-membrane,-exhibit-clustering-and-morphological-defects,-likely-due-to-the-mislocalization-of-the-LINC-complex;-when-associated-with-P-332. evidence 6 type mutagenesis-site original V variation E location position position 187 feature description In-ari-1d;-late-pupal-lethal-and-adult-escapers-have-a-reduced-lifespan-and-thinner-bristles.-Nuclei-in-larval-muscles-(myonuclei)-are-displaced-from-the-cell-membrane,-exhibit-clustering-and-morphological-defects. evidence 6 type mutagenesis-site original C variation S location position position 223 feature description Loss-of-catalytic-activity-and-impaired-autoinhibition;-when-associated-with-A-377;-A-378-and-A-450. evidence 6 type mutagenesis-site original C variation S location position position 304 feature description In-ari1-3;-lethal-phenotype-and-no-loss-of-interaction-with-Ubc10. evidence 4 type mutagenesis-site original C variation Y location position position 309 feature description In-ari-1b;-Loss-of-catalytic-activity.-Late-pupal-lethal-and-adult-escapers-have-a-reduced-lifespan-and-thinner-bristles.-Nuclei-in-larval-muscles-(myonuclei)-are-displaced-from-the-cell-membrane,-exhibit-clustering-and-morphological-defects,-likely-due-to-the-mislocalization-of-the-LINC-complex;-when-associated-with-E-187. evidence 6 type mutagenesis-site original S variation P location position position 332 feature description Impairs-autoinhibition;-when-associated-with-A-378-and-A-450.-Loss-of-activity-and-impaired-autoinhibition;-when-associated-with-A-378;-A-450-and-S-304. evidence 6 type mutagenesis-site original F variation A location position position 377 feature description Impairs-autoinhibition;-when-associated-with-A-377-and-A-450.-Loss-of-activity-and-impaired-autoinhibition;-when-associated-with-A-377;-A-450-and-S-304. evidence 6 type mutagenesis-site original E variation A location position position 378 feature description Impairs-autoinhibition;-when-associated-with-A-377-and-A-378.-Loss-of-activity-and-impaired-autoinhibition;-when-associated-with-A-377;-A-378-and-S-304. evidence 6 type mutagenesis-site original E variation A location position position 450 evidence key 1 type ECO:0000255 evidence key 2 type ECO:0000255 source dbReference id PRU01221 type PROSITE-ProRule evidence key 3 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 4 type ECO:0000269 source dbReference id 10880484 type PubMed evidence key 5 type ECO:0000269 source dbReference id 21900267 type PubMed evidence key 6 type ECO:0000269 source dbReference id 29689197 type PubMed evidence key 7 type ECO:0000303 source dbReference id 10880484 type PubMed evidence key 8 type ECO:0000303 source dbReference id 21900267 type PubMed evidence key 9 type ECO:0000303 source dbReference id 29689197 type PubMed evidence key 10 type ECO:0000305 evidence key 11 type ECO:0000312 source dbReference id FBgn0017418 type FlyBase sequence checksum 0AECCE256CF5EC00 length 503 mass 58932 modified 1997-07-01 version 2 MDSDNDNDFCDNVDSGNVSSGDDGDDDFGMEVDLPSSADRQMDQDDYQYKVLTTDEIVQHQREIIDEANLLLKLPTPTTRILLNHFKWDKEKLLEKYFDDNTDEFFKCAHVINPFNATEAIKQKTSRSQCEECEICFSQLPPDSMAGLECGHRFCMPCWHEYLSTKIVAEGLGQTISCAAHGCDILVDDVTVANLVTDARVRVKYQQLITNSFVECNQLLRWCPSVDCTYAVKVPYAEPRRVHCKCGHVFCFACGENWHDPVKCRWLKKWIKKCDDDSETSNWIAANTKECPRCSVTIEKDGGCNHMVCKNQNCKNEFCWVCLGSWEPHGSSWYNCNRYDEDEAKTARDAQEKLRSSLARYLHYYNRYMNHMQSMKFENKLYASVKQKMEEMQQHNMSWIEVQFLKKAVDILCQCRQTLMYTYVFAYYLKKNNQSMIFEDNQKDLESATEMLSEYLERDITSENLADIKQKVQDKYRYCEKRCSVLLKHVHEGYDKEWWEYTE 
entry created 2003-07-03 dataset Swiss-Prot modified 2022-12-14 version 115 accession Q8DIN8 name PSBL_THEVB protein recommendedName fullName evidence 1 Photosystem-II-reaction-center-protein-L shortName evidence 1 PSII-L gene name evidence 1 type primary psbL name type ordered-locus tsr1543 organism name type scientific Thermosynechococcus-vestitus-(strain-NIES-2133-/-IAM-M-273-/-BP-1) dbReference id 197221 type NCBI-Taxonomy lineage taxon Bacteria taxon Cyanobacteria taxon Pseudanabaenales taxon Thermosynechococcaceae taxon Thermosynechococcus reference key 1 citation date 2002 first 123 last 130 name DNA-Res. type journal-article volume 9 title Complete-genome-structure-of-the-thermophilic-cyanobacterium-Thermosynechococcus-elongatus-BP-1. authorList person name Nakamura-Y. person name Kaneko-T. person name Sato-S. person name Ikeuchi-M. person name Katoh-H. person name Sasamoto-S. person name Watanabe-A. person name Iriguchi-M. person name Kawashima-K. person name Kimura-T. person name Kishida-Y. person name Kiyokawa-C. person name Kohara-M. person name Matsumoto-M. person name Matsuno-A. person name Nakazaki-N. person name Shimpo-S. person name Sugimoto-M. person name Takeuchi-C. person name Yamada-M. person name Tabata-S. dbReference id 12240834 type PubMed dbReference id 10.1093/dnares/9.4.123 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain NIES-2133-/-IAM-M-273-/-BP-1 reference key 2 citation date 2007 first 1269 last 1275 name Biochim.-Biophys.-Acta type journal-article volume 1767 title Ycf12-is-a-core-subunit-in-the-photosystem-II-complex. authorList person name Kashino-Y. person name Takahashi-T. person name Inoue-Kashino-N. person name Ban-A. person name Ikeda-Y. person name Satoh-K. person name Sugiura-M. dbReference id 17935689 type PubMed dbReference id 10.1016/j.bbabio.2007.08.008 type DOI scope PROTEIN-SEQUENCE-OF-1-15 scope COFACTOR scope SUBCELLULAR-LOCATION reference key 3 citation date 2007 first 1758 last 1763 name 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5 citation date 2005 first 1040 last 1044 name Nature type journal-article volume 438 title Towards-complete-cofactor-arrangement-in-the-3.0-A-resolution-structure-of-photosystem-II. authorList person name Loll-B. person name Kern-J. person name Saenger-W. person name Zouni-A. person name Biesiadka-J. dbReference id 16355230 type PubMed dbReference id 10.1038/nature04224 type DOI scope X-RAY-CRYSTALLOGRAPHY-(3.00-ANGSTROMS)-IN-PHOTOSYSTEM-II scope FUNCTION scope COFACTOR scope SUBUNIT scope SUBCELLULAR-LOCATION source strain NIES-2133-/-IAM-M-273-/-BP-1 reference key 6 citation date 2009 first 334 last 342 name Nat.-Struct.-Mol.-Biol. type journal-article volume 16 title Cyanobacterial-photosystem-II-at-2.9-A-resolution-and-the-role-of-quinones,-lipids,-channels-and-chloride. authorList person name Guskov-A. person name Kern-J. person name Gabdulkhakov-A. person name Broser-M. person name Zouni-A. person name Saenger-W. dbReference id 19219048 type PubMed dbReference id 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name Sauter-N.K. person name Yachandra-V.K. person name Bergmann-U. person name Yano-J. dbReference id 23413188 type PubMed dbReference id 10.1126/science.1234273 type DOI scope X-RAY-CRYSTALLOGRAPHY-(5.70-ANGSTROMS)-IN-PHOTOSYSTEM-II scope COFACTOR scope SUBUNIT scope SUBCELLULAR-LOCATION source strain NIES-2133-/-IAM-M-273-/-BP-1 reference key 11 citation date 2014 first 261 last 265 name Nature type journal-article volume 513 title Serial-time-resolved-crystallography-of-photosystem-II-using-a-femtosecond-X-ray-laser. authorList person name Kupitz-C. person name Basu-S. person name Grotjohann-I. person name Fromme-R. person name Zatsepin-N.A. person name Rendek-K.N. person name Hunter-M.S. person name Shoeman-R.L. person name White-T.A. person name Wang-D. person name James-D. person name Yang-J.H. person name Cobb-D.E. person name Reeder-B. person name Sierra-R.G. person name Liu-H. person name Barty-A. person name Aquila-A.L. person name Deponte-D. person name Kirian-R.A. person 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scope X-RAY-CRYSTALLOGRAPHY-(5.00-ANGSTROMS)-IN-PHOTOSYSTEM-II scope COFACTOR scope SUBUNIT scope SUBCELLULAR-LOCATION source strain NIES-2133-/-IAM-M-273-/-BP-1 reference key 12 citation date 2014 first 4371 last 4371 name Nat.-Commun. type journal-article volume 5 title Taking-snapshots-of-photosynthetic-water-oxidation-using-femtosecond-X-ray-diffraction-and-spectroscopy. authorList person name Kern-J. person name Tran-R. person name Alonso-Mori-R. person name Koroidov-S. person name Echols-N. person name Hattne-J. person name Ibrahim-M. person name Gul-S. person name Laksmono-H. person name Sierra-R.G. person name Gildea-R.J. person name Han-G. person name Hellmich-J. person name Lassalle-Kaiser-B. person name Chatterjee-R. person name Brewster-A.S. person name Stan-C.A. person name Gloeckner-C. person name Lampe-A. person name DiFiore-D. person name Milathianaki-D. person name Fry-A.R. person name Seibert-M.M. person name Koglin-J.E. person name Gallo-E. person name Uhlig-J. person name Sokaras-D. person name Weng-T.C. person name Zwart-P.H. person name Skinner-D.E. person name Bogan-M.J. person name Messerschmidt-M. person name Glatzel-P. person name Williams-G.J. person name Boutet-S. person name Adams-P.D. person name Zouni-A. person name Messinger-J. person name Sauter-N.K. person name Bergmann-U. person name Yano-J. person name Yachandra-V.K. dbReference id 25006873 type PubMed dbReference id 10.1038/ncomms5371 type DOI scope X-RAY-CRYSTALLOGRAPHY-(4.50-ANGSTROMS)-IN-PHOTOSYSTEM-II scope FUNCTION scope COFACTOR scope SUBUNIT scope SUBCELLULAR-LOCATION source strain NIES-2133-/-IAM-M-273-/-BP-1 comment type function text evidence 1-7-8-11 One-of-the-components-of-the-core-complex-of-photosystem-II-(PSII).-PSII-is-a-light-driven-water:plastoquinone-oxidoreductase-that-uses-light-energy-to-abstract-electrons-from-H(2)O,-generating-O(2)-and-a-proton-gradient-subsequently-used-for-ATP-formation.-It-consists-of-a-core-antenna-complex-that-captures-photons,-and-an-electron-transfer-chain-that-converts-photonic-excitation-into-a-charge-separation.-This-subunit-is-found-at-the-monomer-monomer-interface-and-is-required-for-correct-PSII-assembly-and/or-dimerization.-This-subunit-may-make-specific-contacts-with-lipid(s)-(PubMed:16355230). comment type cofactor text evidence 2-3-4-5-6-7-8-9-10-11-12 PSII-binds-multiple-chlorophylls,-carotenoids-and-specific-lipids. comment type subunit text evidence 1-2-3-6-7-8-9-10-11-12 Cyanobacterial-PSII-is-composed-of-1-copy-each-of-membrane-proteins-PsbA,-PsbB,-PsbC,-PsbD,-PsbE,-PsbF,-PsbH,-PsbI,-PsbJ,-PsbK,-PsbL,-PsbM,-PsbT,-PsbX,-PsbY,-PsbZ,-Ycf12,-at-least-3-peripheral-proteins-PsbO,-PsbU,-PsbV-and-a-large-number-of-cofactors.-It-forms-dimeric-complexes. comment type subcellular-location subcellularLocation location evidence 1-2-3-4-5-6-7-8-9-10-11-12 Cellular-thylakoid-membrane topology evidence 1-2-3-4-5-6-7-8-9-10-11-12 Single-pass-membrane-protein comment error 4.0 evidence 6 mass 4301.0 method MALDI type mass-spectrometry comment evidence 7 mass 4299.0 method MALDI type mass-spectrometry comment type similarity text evidence 1 Belongs-to-the-PsbL-family. dbReference id BA000039 type EMBL property type protein-sequence-ID value BAC09095.1 property type molecule-type value Genomic_DNA dbReference id NP_682333.1 type RefSeq property type nucleotide-sequence-ID value NC_004113.1 dbReference id WP_011057383.1 type RefSeq property type nucleotide-sequence-ID 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dbReference id 7RF6 type PDB property type method value X-ray property type resolution value 2.01-A property type chains value L/l=1-37 dbReference id 7RF7 type PDB property type method value X-ray property type resolution value 2.09-A property type chains value L/l=1-37 dbReference id 7RF8 type PDB property type method value X-ray property type resolution value 2.09-A property type chains value L/l=1-37 dbReference id 1S5L type PDBsum dbReference id 2AXT type PDBsum dbReference id 3KZI type PDBsum dbReference id 4FBY type PDBsum dbReference id 4IXQ type PDBsum dbReference id 4IXR type PDBsum dbReference id 4PBU type PDBsum dbReference id 4PJ0 type PDBsum dbReference id 4RVY type PDBsum dbReference id 4TNH type PDBsum dbReference id 4TNI type PDBsum dbReference id 4TNJ type PDBsum dbReference id 4TNK type PDBsum dbReference id 4V62 type PDBsum dbReference id 4V82 type PDBsum dbReference id 5E79 type PDBsum dbReference id 5E7C type PDBsum dbReference id 5H2F type PDBsum dbReference id 5KAF type PDBsum dbReference id 5KAI type PDBsum dbReference id 5MX2 type PDBsum dbReference id 5TIS type PDBsum dbReference id 5ZZN type PDBsum dbReference id 6DHE type PDBsum dbReference id 6DHF type PDBsum dbReference id 6DHG type PDBsum dbReference id 6DHH type PDBsum dbReference id 6DHO type PDBsum dbReference id 6DHP type PDBsum dbReference id 6W1O type PDBsum dbReference id 6W1P type PDBsum dbReference id 6W1Q type PDBsum dbReference id 6W1R type PDBsum dbReference id 6W1T type PDBsum dbReference id 6W1U type PDBsum dbReference id 6W1V type PDBsum dbReference id 7NHO type PDBsum dbReference id 7NHP type PDBsum dbReference id 7NHQ type PDBsum dbReference id 7RF1 type PDBsum dbReference id 7RF2 type PDBsum dbReference id 7RF3 type PDBsum dbReference id 7RF4 type PDBsum dbReference id 7RF5 type PDBsum dbReference id 7RF6 type PDBsum dbReference id 7RF7 type PDBsum dbReference id 7RF8 type PDBsum dbReference id Q8DIN8 type AlphaFoldDB dbReference id Q8DIN8 type SMR dbReference id DIP-48497N type DIP dbReference id Q8DIN8 type IntAct property type interactions value 1 dbReference id 197221.22295268 type STRING dbReference id BAC09095 type EnsemblBacteria property type protein-sequence-ID value BAC09095 property type gene-ID value BAC09095 dbReference id tel:tsr1543 type KEGG dbReference id fig|197221.4.peg.1619 type PATRIC dbReference id ENOG5033AKP type eggNOG property type taxonomic-scope value Bacteria dbReference id Q8DIN8 type EvolutionaryTrace dbReference id UP000000440 type Proteomes property type component value Chromosome dbReference id GO:0009539 type GO property type term value C:photosystem-II-reaction-center property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0031676 type GO property type term value C:plasma-membrane-derived-thylakoid-membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0015979 type GO property type term value P:photosynthesis property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id MF_01317 type HAMAP property type entry-name value PSII_PsbL property type match-status value 1 dbReference id IPR003372 type InterPro property type entry-name value PSII_PsbL dbReference id IPR037266 type InterPro property type entry-name value PSII_PsbL_sf dbReference id PF02419 type Pfam property type entry-name value PsbL property type match-status value 1 dbReference id SSF161017 type SUPFAM property type entry-name value Photosystem-II-reaction-center-protein-L,-PsbL 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-0472 Membrane keyword id KW-0602 Photosynthesis keyword id KW-0604 Photosystem-II keyword id KW-0674 Reaction-center keyword id KW-1185 Reference-proteome keyword id KW-0793 Thylakoid keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix feature description Photosystem-II-reaction-center-protein-L id PRO_0000219790 type chain location begin position 1 end position 37 feature description Cytoplasmic evidence 6 type topological-domain location begin position 1 end position 17 feature description Helical evidence 6 type transmembrane-region location begin position 18 end position 32 feature description Lumenal evidence 6 type topological-domain location begin position 33 end position 37 feature evidence 13 type helix location begin position 14 end position 36 evidence key 1 type ECO:0000255 source dbReference id MF_01317 type HAMAP-Rule evidence key 2 type ECO:0000269 source dbReference id 14764885 type PubMed evidence key 3 type ECO:0000269 source dbReference id 16355230 type PubMed evidence key 4 type ECO:0000269 source dbReference id 17935689 type PubMed evidence key 5 type ECO:0000269 source dbReference id 17967798 type PubMed evidence key 6 type ECO:0000269 source dbReference id 19219048 type PubMed evidence key 7 type ECO:0000269 source dbReference id 20558739 type PubMed evidence key 8 type ECO:0000269 source dbReference id 21367867 type PubMed evidence key 9 type ECO:0000269 source dbReference id 22665786 type PubMed evidence key 10 type ECO:0000269 source dbReference id 23413188 type PubMed evidence key 11 type ECO:0000269 source dbReference id 25006873 type PubMed evidence key 12 type ECO:0000269 source dbReference id 25043005 type PubMed evidence key 13 type ECO:0007829 source dbReference id 5ZZN type PDB sequence checksum 8EB1690C62528BC5 length 37 mass 4297 modified 2003-03-01 version 1 MEPNPNRQPVELNRTSLYLGLLLILVLALLFSSYFFN 
