ID A0A3B3Z2J1_9TELE Unreviewed; 174 AA.
AC A0A3B3Z2J1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000033744.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000033744.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004363}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004363}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the RNF152 family.
CC {ECO:0000256|ARBA:ARBA00007082}.
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DR AlphaFoldDB; A0A3B3Z2J1; -.
DR STRING; 48701.ENSPMEP00000033744; -.
DR Ensembl; ENSPMET00000028850.1; ENSPMEP00000033744.1; ENSPMEG00000022457.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045744; RNF152_C.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR25464:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF152; 1.
DR PANTHER; PTHR25464; TRIPARTITE MOTIF-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR Pfam; PF19325; RNF152_C; 2.
DR Pfam; PF14634; zf-RING_5; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 137..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..55
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 174 AA; 19114 MW; DF8BD527922510CD CRC64;
METLSQDSIL ECQICFNYYS PRRRPKLLDC RHTCCSVCLT QMRSTQKEIR CPWCRGVTKL
PPGLSVSQLP DDPDIITVIA IPHASEHTPV FIRLPSNGCY MLPLPVTKER ALGLPGDLGC
RERRVPGPVG GGKGSTWSGV CTVILVACVL LFLLGIVLHN MSCISKRFTV ISCG
//
