ID A0A3P8TDR3_AMPPE Unreviewed; 438 AA.
AC A0A3P8TDR3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000022816.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000022816.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000022816.1}
RP IDENTIFICATION.
RG Ensembl;
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|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 AlphaFoldDB; A0A3P8TDR3; -.
DR Ensembl; ENSAPET00000023422.1; ENSAPEP00000022816.1; ENSAPEG00000016250.1.
DR GeneTree; ENSGT00390000011034; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265080; Chromosome 20.
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 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:SF469; E3 UBIQUITIN-PROTEIN LIGASE PARKIN; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
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 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080};
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..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 211..438
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 74..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /evidence="ECO:0000256|PIRSR:PIRSR037880-1"
SQ SEQUENCE 438 AA; 48244 MW; 7F3D8894F3EFAA75 CRC64;
MIVFVRYNLG PGVAVELQEE SSVAELKELV GSQQGVRHEQ LRVLFAGTEL QNSSTLQSCD
LPEQSTVHVI LPPAGSSSQL QQNHLTRPDL GSSHLPPSSP SSPGPAEVLE GRQEAAGVRT
CSTFYVYCKS CRSVQPGKLR VRCQSCRQTT MMLSRGPSCW DDVLLQGRIH GICQSEGCHG
NETEFYMKCA THPTPDDDLS VALDLIMTNT RDMPCIACTD VMDVVVVFPC LERHVICLDC
FRGYCEARLS ERRFVHHPVI GYSLPCAAGC EDSLIREVHH FRVLGDEQYG RYQRYGAEEC
LLAIGGLMCP SPGCGAGLLP PDGSRRVECD RPLGCGFIFC RDCREGYHQG PCQAAPAPPT
GEASQGFLVG GEAALRGRWD RESLLLIQET TKRCPQCSVP VERNGGCMHM ACPRCQTEWC
WLCGVPWNRD CMGNHWFG
//
