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Database: UniProt
Entry: A0A455C3Q4_PHYMC
LinkDB: A0A455C3Q4_PHYMC
Original site: A0A455C3Q4_PHYMC 
ID   A0A455C3Q4_PHYMC        Unreviewed;       474 AA.
AC   A0A455C3Q4;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000256|ARBA:ARBA00029536, ECO:0000256|PIRNR:PIRNR037880};
DE            EC=2.3.2.31 {ECO:0000256|PIRNR:PIRNR037880};
GN   Name=PRKN {ECO:0000313|RefSeq:XP_028350571.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028350571.1};
RN   [1] {ECO:0000313|RefSeq:XP_028350571.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028350571.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex,
CC       catalyzing the covalent attachment of ubiquitin moieties onto substrate
CC       proteins. {ECO:0000256|PIRNR:PIRNR037880}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|PIRNR:PIRNR037880};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|PIRNR:PIRNR037880}.
CC   -!- SUBUNIT: Forms an E3 ubiquitin ligase complex.
CC       {ECO:0000256|PIRNR:PIRNR037880}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|PIRNR:PIRNR037880}.
CC   -!- SIMILARITY: Belongs to the RBR family. Parkin subfamily.
CC       {ECO:0000256|ARBA:ARBA00029442, ECO:0000256|PIRNR:PIRNR037880}.
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DR   RefSeq; XP_028350571.1; XM_028494770.1.
DR   AlphaFoldDB; A0A455C3Q4; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000248484; Chromosome 10.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-UniRule.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR   CDD; cd20340; BRcat_RBR_parkin; 1.
DR   CDD; cd16627; RING-HC_RBR_parkin; 1.
DR   CDD; cd21382; RING0_parkin; 1.
DR   CDD; cd01798; Ubl_parkin; 1.
DR   Gene3D; 2.20.25.20; -; 1.
DR   InterPro; IPR047534; BRcat_RBR_parkin.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR003977; Parkin.
DR   InterPro; IPR041565; Parkin_Znf-RING.
DR   InterPro; IPR047535; RING-HC_RBR_parkin.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR015496; Ubiquilin.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR041170; Znf-RING_14.
DR   PANTHER; PTHR10677; UBIQUILIN; 1.
DR   PANTHER; PTHR10677:SF40; UBIQUITIN-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   Pfam; PF17976; zf-RING_12; 1.
DR   Pfam; PF17978; zf-RING_14; 1.
DR   PIRSF; PIRSF037880; Parkin; 1.
DR   PRINTS; PR01475; PARKIN.
DR   SMART; SM00647; IBR; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   3: Inferred from homology;
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006, ECO:0000256|PIRNR:PIRNR037880};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR037880};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|PIRNR:PIRNR037880};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|PIRNR:PIRNR037880};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR037880};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037880};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          21..92
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          253..474
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          97..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  52157 MW;  BF4B2570F7AFDE60 CRC64;
     MMQYNSLIST LLRLNLRRNC FFVFVRFNSS HGFPVEVDSD TSIFQLKEVV AKRQGVPADQ
     LRVIFAGKEL RNDLTVRSCD LDQQSIIHIV LRPQRKVPER KAAGGESPQD TAGGSEREPE
     SLTRVDLSSS VLPSDSAGLA VILKDDNENG GPPAERPGRP TYNSFYVYCK GPCQGVQPGK
     LRVRCSTCQQ ATLTLAQGPS RWEDVLIPNQ MSGECQSPNC PGTRAEFFFK CGAHPTSDEE
     TSVALNLITT NSRDITCITC MDIRSPVLVF QCSYRHVICL DCFHLYCVTR LNDRQFVHDP
     QLGYSLPCVA GCPNSLIKEL HHFRILGEEQ YNRYQQYGAE ECVLQMGGVL CPSPGCGAGL
     LPEPSQRKVT CEGGSGLGCG FVFCRDCKEL YHEGECSALF EASGTVTQTS PIGHTQLKAS
     HKGPKGHGPS DSAFHTQSRG EKRTQNNQYI LYGLVYRVSG FLISTRATLG HGEG
//
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