ID Q19K47_PIG Unreviewed; 410 AA.
AC Q19K47;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000256|PIRNR:PIRNR037880};
DE EC=2.3.2.31 {ECO:0000256|PIRNR:PIRNR037880};
GN Name=PARK2 {ECO:0000313|EMBL:ABF69685.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ABF69685.1};
RN [1] {ECO:0000313|EMBL:ABF69685.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16844087; DOI=10.1016/j.bbrc.2006.06.167;
RA Bjerre D., Madsen L.B., Bendixen C., Larsen K.;
RT "Porcine Parkin: molecular cloning of PARK2 cDNA, expression analysis, and
RT identification of a splicing variant.";
RL Biochem. Biophys. Res. Commun. 347:803-813(2006).
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|PIRNR:PIRNR037880}.
CC -!- SIMILARITY: Belongs to the RBR family. Parkin subfamily.
CC {ECO:0000256|PIRNR:PIRNR037880}.
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DR EMBL; DQ525852; ABF69685.1; -; mRNA.
DR AlphaFoldDB; Q19K47; -.
DR SMR; Q19K47; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; PARK2; pig.
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; 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; 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; 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; 2.
DR PRINTS; PR01475; PARKIN.
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|PIRNR:PIRNR037880};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR037880};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR037880};
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 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 229..410
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT ACT_SITE 376
FT /evidence="ECO:0000256|PIRSR:PIRSR037880-1"
SQ SEQUENCE 410 AA; 45748 MW; 39C4050B5D39E719 CRC64;
MIVFVRFNSS HGFPVEVDSD TSIFQLKEVV AKRQGVPADQ LRVIFAGKEL RNDLTVQRCD
LDQQSIVHVV LRPQRNGQER GVAAGHRPGR AGREPASLTR VDLSGSVLPG DAVGLAVILQ
DDSADGAAPA GRPDRPTNKS FYVYCKGPCQ RVQPGKLRVR CSTCQQATLT LTQGPSCWDD
VLIPNRMSGE CQSPNCPGTT AEFFFKCGAH PTSDKETSVA LNLITTNSRD ITCITCTDIR
SPVLVFQCNC RHVICLDCFH LYCVTRLNDR QFVHDPQLGY SLPCVAGCPN SLIKELHHFR
ILGEEQLVFC RDCKESYHEG ECSALFEASA AVAQAYRVDQ KAAEQARWEE ASKETIRKTT
KPCPRCHVPV EKNGGCMHMK CPQPQCQLEW CWNCGWEWNR DCMGDHWFDV
//