ID   A1IGZ9_HUMAN            Unreviewed;       465 AA.
AC   A1IGZ9;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000256|ARBA:ARBA00029536, ECO:0000256|PIRNR:PIRNR037880};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251, ECO:0000256|PIRNR:PIRNR037880};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAF43729.1};
RN   [1] {ECO:0000313|EMBL:BAF43729.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Cai Y., Zou H., Chen B., Wen M., Xie S.;
RT   "Homo sapiens Parkin 2, mRNA. complete cds.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001798,
CC         ECO:0000256|PIRNR:PIRNR037880};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR037880}.
CC   -!- SUBUNIT: Forms an E3 ubiquitin ligase complex.
CC       {ECO:0000256|PIRNR:PIRNR037880}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173, 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   EMBL; AB245403; BAF43729.1; -; mRNA.
DR   AlphaFoldDB; A1IGZ9; -.
DR   SMR; A1IGZ9; -.
DR   PeptideAtlas; A1IGZ9; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; cd20357; Rcat_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; 1.20.120.1750; -; 1.
DR   Gene3D; 2.20.25.20; -; 1.
DR   InterPro; IPR047534; BRcat_RBR_parkin.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR003977; Parkin.
DR   InterPro; IPR041565; Parkin_Znf-RING.
DR   InterPro; IPR047536; Rcat_RBR_parkin.
DR   InterPro; IPR047535; RING-HC_RBR_parkin.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR041170; Znf-RING_14.
DR   PANTHER; PTHR11685:SF471; E3 UBIQUITIN-PROTEIN LIGASE PARKIN; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 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; 2.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843,
KW   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          1..72
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          234..465
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          77..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037880-1"
SQ   SEQUENCE   465 AA;  51678 MW;  7D37347356F22EFA CRC64;
     MIVFVRFNSS HGFPVEVDSD TSIFQLKEVV AKRQGVPADQ LRVIFAGKEL RNDWTVQNCD
     LDQQSIVHIV QRPWRKGQEM NATGGDDPRN AAGGCEREPQ SLTRVDLSSS VLPGDSVGLA
     VILHTDSRKD SPPAGSPAGR SIYNSFYVYC KGPCQRVQPG KLRVQCSTCR QATLTLTQGP
     SCWDDVLIPN RMSGECQSPH CPGTSAEFFF KCGAHPTSDK ETPVALHLIA TNSRNITCIT
     CTNVRSPVLV FQCNSRHVIC LDCFHLYCVT RLNDRQFVHD PQLGYSLPCV AGCPNSLIKE
     LHHFRILGEE QYNRYQQYGA EECVLQMGGV LCPRPGCGVG LLPEPDQRKV TCEGGNGLGC
     GFAFCRECKE AYHEGECSAV FEASGTTTQA YRVDERAAEQ ARWEAASKET IKKTTKPCPR
     CHVPVEKNGG CMHMKCPQPQ CRLEWCWNCG CEWNRVCMGD HWFDV
//