RN185_RAT
ID RN185_RAT Reviewed; 192 AA.
AC Q568Y3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that regulates selective
CC mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination
CC of BNIP1. Acts in the endoplasmic reticulum (ER)-associated degradation
CC (ERAD) pathway, which targets misfolded proteins that accumulate in the
CC endoplasmic reticulum (ER) for ubiquitination and subsequent
CC proteasome-mediated degradation. Protects cells from ER stress-induced
CC apoptosis. Responsible for the cotranslational ubiquitination and
CC degradation of CFTR in the ERAD pathway. Also acts as a regulator of
CC the innate antiviral response by catalyzing 'Lys-27'-linked
CC polyubiquitination of CGAS, thereby promoting CGAS cyclic GMP-AMP
CC synthase activity. Preferentially associates with the E2 enzymes UBE2J1
CC and UBE2J2. {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 -!- SUBUNIT: Interacts with ATG5 and BNIP1. {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; BC092655; AAH92655.1; -; mRNA.
DR RefSeq; NP_001019442.1; NM_001024271.1.
DR RefSeq; XP_006251395.1; XM_006251333.2.
DR RefSeq; XP_017454807.1; XM_017599318.1.
DR AlphaFoldDB; Q568Y3; -.
DR SMR; Q568Y3; -.
DR STRING; 10116.ENSRNOP00000026134; -.
DR PhosphoSitePlus; Q568Y3; -.
DR PaxDb; Q568Y3; -.
DR Ensembl; ENSRNOT00000026134; ENSRNOP00000026134; ENSRNOG00000019325.
DR GeneID; 360967; -.
DR KEGG; rno:360967; -.
DR UCSC; RGD:1564777; rat.
DR CTD; 91445; -.
DR RGD; 1564777; Rnf185.
DR eggNOG; KOG0823; Eukaryota.
DR GeneTree; ENSGT00390000014107; -.
DR HOGENOM; CLU_055198_2_2_1; -.
DR InParanoid; Q568Y3; -.
DR OMA; NDKEQNE; -.
DR OrthoDB; 1510545at2759; -.
DR PhylomeDB; Q568Y3; -.
DR TreeFam; TF317334; -.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q568Y3; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000019325; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; Q568Y3; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; ISO:RGD.
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:0036503; P:ERAD pathway; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; ISS:UniProtKB.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:RGD.
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..192
FT /note="E3 ubiquitin-protein ligase RNF185"
FT /id="PRO_0000247523"
FT TOPO_DOM 1..130
FT /note="Cytoplasmic"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..171
FT /note="Mitochondrial intermembrane"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 39..80
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..80
FT /note="Required for ubiquitin ligase activity and
FT protection against ER stress-induced cell death"
FT /evidence="ECO:0000250|UniProtKB:Q96GF1"
FT REGION 90..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 192 AA; 20493 MW; BB3F58FF557089DB CRC64;
MASKGPSASA STENSSAGGP SGSSNGTGES GGQDSTFECN ICLDTAKDAV ISLCGHLFCW
PCLHQWLETR PNRQVCPVCK AGISRDKVIP LYGRGSTGQQ DPREKTPPRP QGQRPEPENR
GGFQGFGFGD GGFQMSFGIG AFPFGIFATA FNINDGRPPP AVPGTPQYVD EQFLSRLFLF
VALVIMFWLL IA
