RN185_CHICK
ID RN185_CHICK Reviewed; 194 AA.
AC Q5ZIR9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=E3 ubiquitin-protein ligase RNF185;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q96GF1};
DE AltName: Full=RING finger protein 185;
GN Name=RNF185; ORFNames=RCJMB04_23p11;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that regulates selective
CC mitochondrial autophagy by mediating 'Lys-63'-linked
CC polyubiquitination. Acts in the endoplasmic reticulum (ER)-associated
CC degradation (ERAD) pathway, which targets misfolded proteins that
CC accumulate in the endoplasmic reticulum (ER) for ubiquitination and
CC subsequent proteasome-mediated degradation. Protects cells from ER
CC stress-induced apoptosis. Responsible for the cotranslational
CC ubiquitination and degradation of CFTR in the ERAD pathway. Also acts
CC as a regulator of the innate antiviral response by catalyzing 'Lys-27'-
CC linked polyubiquitination of CGAS, thereby promoting CGAS cyclic GMP-
CC AMP synthase activity. Preferentially associates with the E2 enzymes
CC UBE2J1 and UBE2J2 (By similarity). {ECO:0000250|UniProtKB:Q96GF1}.
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:Q96GF1};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q96GF1}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q96GF1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96GF1}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96GF1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96GF1}.
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC ubiquitin ligase activity. {ECO:0000250|UniProtKB:Q96GF1}.
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DR EMBL; AJ720715; CAG32374.1; -; mRNA.
DR RefSeq; NP_001007841.1; NM_001007840.1.
DR RefSeq; XP_015130814.1; XM_015275328.1.
DR RefSeq; XP_015130815.1; XM_015275329.1.
DR AlphaFoldDB; Q5ZIR9; -.
DR SMR; Q5ZIR9; -.
DR STRING; 9031.ENSGALP00000011262; -.
DR PaxDb; Q5ZIR9; -.
DR Ensembl; ENSGALT00000011276; ENSGALP00000011262; ENSGALG00000006960.
DR GeneID; 416965; -.
DR KEGG; gga:416965; -.
DR CTD; 6048; -.
DR VEuPathDB; HostDB:geneid_416965; -.
DR eggNOG; KOG0823; Eukaryota.
DR GeneTree; ENSGT00390000014107; -.
DR HOGENOM; CLU_055198_2_2_1; -.
DR InParanoid; Q5ZIR9; -.
DR OrthoDB; 1510545at2759; -.
DR PhylomeDB; Q5ZIR9; -.
DR TreeFam; TF317334; -.
DR Reactome; R-GGA-382556; ABC-family proteins mediated transport.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5ZIR9; -.
DR Proteomes; UP000000539; Chromosome 15.
DR Bgee; ENSGALG00000006960; Expressed in testis and 13 other tissues.
DR ExpressionAtlas; Q5ZIR9; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
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:0044390; F:ubiquitin-like protein conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045103; RNF5/RNF185-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12313; PTHR12313; 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 Autophagy; Endoplasmic reticulum; Immunity; Innate immunity; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..194
FT /note="E3 ubiquitin-protein ligase RNF185"
FT /id="PRO_0000247524"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 41..82
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..82
FT /note="Required for ubiquitin ligase activity and
FT protection against ER stress-induced cell death"
FT /evidence="ECO:0000250|UniProtKB:Q96GF1"
FT REGION 92..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 194 AA; 20828 MW; 1162DE994BC8D635 CRC64;
MASKGPTTSA STKSSSTGGT SGSSSSNGAG DNTNQDNTFE CNICLDTAKD AVISLCGHLF
CWPCLHQWLE TRPNRQVCPV CKAGISRDKV IPLYGRGSTG QQDPREKTPP RPQGQRPEPE
NRGGFQGFGF GDGGFQMSFG IGAFPFGIFA TAFNINDGRP PPAVPGTPQY VDEQFLSRLF
LFVALVIMFW LLIA
