RN185_MOUSE
ID RN185_MOUSE Reviewed; 192 AA.
AC Q91YT2; Q6ZWS3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Embryo, Eye, Heart, Lung, Placenta, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=129; TISSUE=Mammary tumor;
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).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=27485036; DOI=10.1038/srep30955;
RA Kaneko M., Iwase I., Yamasaki Y., Takai T., Wu Y., Kanemoto S.,
RA Matsuhisa K., Asada R., Okuma Y., Watanabe T., Imaizumi K., Nomura Y.;
RT "Genome-wide identification and gene expression profiling of ubiquitin
RT ligases for endoplasmic reticulum protein degradation.";
RL Sci. Rep. 6:30955-30955(2016).
RN [4]
RP FUNCTION.
RX PubMed=28273161; DOI=10.1371/journal.ppat.1006264;
RA Wang Q., Huang L., Hong Z., Lv Z., Mao Z., Tang Y., Kong X., Li S., Cui Y.,
RA Liu H., Zhang L., Zhang X., Jiang L., Wang C., Zhou Q.;
RT "The E3 ubiquitin ligase RNF185 facilitates the cGAS-mediated innate immune
RT response.";
RL PLoS Pathog. 13:e1006264-e1006264(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that regulates selective
CC mitochondrial autophagy by mediating 'Lys-63'-linked polyubiquitination
CC of BNIP1 (By similarity). Acts in the endoplasmic reticulum (ER)-
CC associated degradation (ERAD) pathway, which targets misfolded proteins
CC that accumulate in the endoplasmic reticulum (ER) for ubiquitination
CC and subsequent proteasome-mediated degradation (By similarity).
CC Protects cells from ER stress-induced apoptosis (By similarity).
CC Responsible for the cotranslational ubiquitination and degradation of
CC CFTR in the ERAD pathway (By similarity). 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 (PubMed:28273161). Preferentially associates with the
CC E2 enzymes UBE2J1 and UBE2J2 (By similarity).
CC {ECO:0000250|UniProtKB:Q96GF1, ECO:0000269|PubMed:28273161}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91YT2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91YT2-2; Sequence=VSP_020005;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in
CC testis. {ECO:0000269|PubMed:27485036}.
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; AK034108; BAC28589.1; -; mRNA.
DR EMBL; AK052436; BAC34989.1; -; mRNA.
DR EMBL; AK053358; BAC35361.1; -; mRNA.
DR EMBL; AK075756; BAC35934.1; -; mRNA.
DR EMBL; AK077638; BAC36918.1; -; mRNA.
DR EMBL; AK149640; BAE29001.1; -; mRNA.
DR EMBL; AK165895; BAE38444.1; -; mRNA.
DR EMBL; AK167455; BAE39541.1; -; mRNA.
DR EMBL; AK168904; BAE40718.1; -; mRNA.
DR EMBL; BC014812; AAH14812.1; -; mRNA.
DR CCDS; CCDS24361.1; -. [Q91YT2-2]
DR CCDS; CCDS70127.1; -. [Q91YT2-1]
DR RefSeq; NP_001277401.1; NM_001290472.1. [Q91YT2-1]
DR RefSeq; NP_001277402.1; NM_001290473.1.
DR RefSeq; NP_663330.2; NM_145355.5. [Q91YT2-2]
DR AlphaFoldDB; Q91YT2; -.
DR SMR; Q91YT2; -.
DR BioGRID; 228751; 2.
DR STRING; 10090.ENSMUSP00000067053; -.
DR iPTMnet; Q91YT2; -.
DR PhosphoSitePlus; Q91YT2; -.
DR MaxQB; Q91YT2; -.
DR PaxDb; Q91YT2; -.
DR PeptideAtlas; Q91YT2; -.
DR PRIDE; Q91YT2; -.
DR ProteomicsDB; 299922; -. [Q91YT2-1]
DR ProteomicsDB; 299923; -. [Q91YT2-2]
DR Antibodypedia; 24963; 152 antibodies from 22 providers.
DR DNASU; 193670; -.
DR Ensembl; ENSMUST00000064364; ENSMUSP00000067053; ENSMUSG00000020448. [Q91YT2-2]
DR Ensembl; ENSMUST00000077078; ENSMUSP00000076333; ENSMUSG00000020448. [Q91YT2-1]
DR GeneID; 193670; -.
DR KEGG; mmu:193670; -.
DR UCSC; uc007hsv.2; mouse. [Q91YT2-2]
DR UCSC; uc007hsw.2; mouse. [Q91YT2-1]
DR CTD; 91445; -.
DR MGI; MGI:1922078; Rnf185.
DR VEuPathDB; HostDB:ENSMUSG00000020448; -.
DR eggNOG; KOG0823; Eukaryota.
DR GeneTree; ENSGT00390000014107; -.
DR HOGENOM; CLU_055198_2_2_1; -.
DR InParanoid; Q91YT2; -.
DR OrthoDB; 1510545at2759; -.
DR PhylomeDB; Q91YT2; -.
DR TreeFam; TF317334; -.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 193670; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Rnf185; mouse.
DR PRO; PR:Q91YT2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91YT2; protein.
DR Bgee; ENSMUSG00000020448; Expressed in animal zygote and 253 other tissues.
DR Genevisible; Q91YT2; MM.
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:MGI.
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:MGI.
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:MGI.
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:MGI.
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 Alternative splicing; Autophagy; Endoplasmic reticulum; Immunity;
KW Innate immunity; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..192
FT /note="E3 ubiquitin-protein ligase RNF185"
FT /id="PRO_0000247521"
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"
FT VAR_SEQ 1
FT /note="M -> MCILLCPHMFCRPINQRQADWDCLENLPWKLCWQAAM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020005"
SQ SEQUENCE 192 AA; 20520 MW; 12B98A1DA309AD5D CRC64;
MASKGPSASA STENSNAGGP SGSSNGTGES GGQDSTFECN ICLDTAKDAV ISLCGHLFCW
PCLHQWLETR PNRQVCPVCK AGISRDKVIP LYGRGSTGQQ DPREKTPPRP QGQRPEPENR
GGFQGFGFGD GGFQMSFGIG AFPFGIFATA FNINDGRPPP AVPGTPQYVD EQFLSRLFLF
VALVIMFWLL IA
