ID A0A1A9WHJ3_9MUSC Unreviewed; 481 AA.
AC A0A1A9WHJ3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 Glossina brevipalpis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37001 {ECO:0000313|EnsemblMetazoa:GBRI020028-PA, ECO:0000313|Proteomes:UP000091820};
RN [1] {ECO:0000313|Proteomes:UP000091820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000091820};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GBRI020028-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GBRI020028-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; A0A1A9WHJ3; -.
DR STRING; 37001.A0A1A9WHJ3; -.
DR EnsemblMetazoa; GBRI020028-RA; GBRI020028-PA; GBRI020028.
DR VEuPathDB; VectorBase:GBRI020028; -.
DR OrthoDB; 3084186at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000091820; Unassembled WGS sequence.
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:SF469; 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; 2.
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 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 30..105
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 254..481
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT ACT_SITE 448
FT /evidence="ECO:0000256|PIRSR:PIRSR037880-1"
SQ SEQUENCE 481 AA; 54266 MW; 9AE63BA959938535 CRC64;
MSFLLNVLKN LFSKMLELLS FGRKSITSSL NIYVKTNTGR TLSVNLEPKW DIKNVKEIVA
PQLGLQPDEV KIIFAGKELS DATTIEECDL GQQSILHAIR ARPAKQRKSV HSMVTEEEVT
SEEVPSKPLC ETLLDVQFQN EEKIQELETV CERKRVHFFV HCSQCNKLCK GKLRVRCSLC
KGGAFTVHRD PECWDDVLKC RRIRGHCESY DIACVDNNAG DPPFAEFYFK CAEHVSGGEK
DFAAPLNLVK LNTKDIPCLA CTDISEIVLV FPCASKHVTC VECFLHYCRS RLLERQFMPH
PDIGYTLQCP AGCENSFIEE IHHFKLLTRE EYDRYQHFAT EEYVLQAGGV LCPQPGCGMG
LLVDPGCMKV TCQNGCGYVF CRNCLQGYHL GDCLQDIVNG GDSPSCEYSV DPNRAAEARW
DEASNVTIKV LTKPCPKCRT PTERDGGCMH MVCTRSGCGF EWCWICQTEW TRDCMGAHWF
G
//
