RN183_BOVIN
ID RN183_BOVIN Reviewed; 188 AA.
AC Q3SWY0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=E3 ubiquitin-protein ligase RNF183;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q96D59};
GN Name=RNF183;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a E3 ubiquitin ligase catalyzing the covalent
CC attachment of ubiquitin moieties onto substrate proteins. Triggers
CC apoptosis in response to prolonged ER stress by mediating the
CC polyubiquitination and subsequent proteasomal degradation of BCL2L1.
CC May collaborate with FATE1 to restrain BIK protein levels thus
CC regulating apoptotic signaling. {ECO:0000250|UniProtKB:Q96D59}.
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:0000250|UniProtKB:Q96D59};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with FATE1. Interacts with SEC16A. Interacts with
CC BCL2L1. {ECO:0000250|UniProtKB:Q8QZS5, ECO:0000250|UniProtKB:Q96D59}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type IV membrane protein {ECO:0000305}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:Q96D59}. Golgi apparatus, cis-Golgi
CC network membrane {ECO:0000250|UniProtKB:Q8QZS5}. Lysosome
CC {ECO:0000250|UniProtKB:Q8QZS5}.
CC -!- PTM: Autoubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q96D59}.
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DR EMBL; BC104611; AAI04612.1; -; mRNA.
DR RefSeq; NP_001030499.1; NM_001035422.1.
DR AlphaFoldDB; Q3SWY0; -.
DR STRING; 9913.ENSBTAP00000006005; -.
DR PaxDb; Q3SWY0; -.
DR PRIDE; Q3SWY0; -.
DR GeneID; 539200; -.
DR KEGG; bta:539200; -.
DR CTD; 138065; -.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_122905_0_0_1; -.
DR InParanoid; Q3SWY0; -.
DR OrthoDB; 1337075at2759; -.
DR TreeFam; TF337102; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0033106; C:cis-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Endoplasmic reticulum; Golgi apparatus; Lysosome; Membrane;
KW Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..188
FT /note="E3 ubiquitin-protein ligase RNF183"
FT /id="PRO_0000247357"
FT TOPO_DOM 1..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..188
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ZN_FING 11..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 188 AA; 21492 MW; 1BBB467A8E590509 CRC64;
MAEQQGREPE CPVCWNPFNN TFHTPKVLDC CHSFCVECLA HISLVTPTRR RLLCPLCRHP
TVLASGQPVT DLPTDTAVLT LLRLEPHHVI LEGHQLCLKD QPKSRYFLRQ PRVYTLDLGP
EPASQAGQPQ DVGPSTRPVP IRSRYSLREC FRNPHFRIFA YMMAVILCGT VLFIFSIFCT
RRFFWGVG
