RN185_HUMAN
ID RN185_HUMAN Reviewed; 192 AA.
AC Q96GF1; A8K5C1; A9X3T8; Q8N900;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=E3 ubiquitin-protein ligase RNF185 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:27485036, ECO:0000269|PubMed:28273161};
DE AltName: Full=RING finger protein 185;
GN Name=RNF185 {ECO:0000303|Ref.1, ECO:0000312|HGNC:HGNC:26783};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pancreas, and Testis;
RA Martinez Gamboa L., Stuhlmueller B., Burmester G.R.;
RT "Multiple splice variants of the gene coding for ring finger protein
RT RNF185.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, Lung, Muscle, and Pancreas;
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP INTERACTION WITH ATG5 AND BNIP1.
RX PubMed=21931693; DOI=10.1371/journal.pone.0024367;
RA Tang F., Wang B., Li N., Wu Y., Jia J., Suo T., Chen Q., Liu Y.J., Tang J.;
RT "RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy
RT through interaction with BNIP1.";
RL PLoS ONE 6:E24367-E24367(2011).
RN [8]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24019521; DOI=10.1074/jbc.m113.470500;
RA El Khouri E., Le Pavec G., Toledano M.B., Delaunay-Moisan A.;
RT "RNF185 is a novel E3 ligase of endoplasmic reticulum-associated
RT degradation (ERAD) that targets cystic fibrosis transmembrane conductance
RT regulator (CFTR).";
RL J. Biol. Chem. 288:31177-31191(2013).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, DOMAIN, AND MUTAGENESIS OF CYS-39.
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF CYS-39 AND
RP CYS-79.
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 (PubMed:21931693). 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 (PubMed:27485036).
CC Protects cells from ER stress-induced apoptosis (PubMed:27485036).
CC Responsible for the cotranslational ubiquitination and degradation of
CC CFTR in the ERAD pathway (PubMed:24019521). Also acts as a regulator of
CC the innate antiviral response by catalyzing 'Lys-27'-linked
CC polyubiquitination of CGAS at 'Lys-173' and 'Lys-384', thereby
CC promoting CGAS cyclic GMP-AMP synthase activity (PubMed:28273161).
CC Preferentially associates with the E2 enzymes UBE2J1 and UBE2J2
CC (PubMed:24019521). {ECO:0000269|PubMed:21931693,
CC ECO:0000269|PubMed:24019521, ECO:0000269|PubMed:27485036,
CC 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:0000269|PubMed:21931693,
CC ECO:0000269|PubMed:27485036, ECO:0000269|PubMed:28273161};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:27485036,
CC ECO:0000269|PubMed:28273161}.
CC -!- SUBUNIT: Interacts with ATG5 and BNIP1. {ECO:0000269|PubMed:21931693}.
CC -!- INTERACTION:
CC Q96GF1; O75915: ARL6IP5; NbExp=3; IntAct=EBI-2340249, EBI-2860752;
CC Q96GF1; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-2340249, EBI-2548702;
CC Q96GF1; Q8NBI2: CYB561A3; NbExp=3; IntAct=EBI-2340249, EBI-10269179;
CC Q96GF1; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-2340249, EBI-12118888;
CC Q96GF1; Q13021: MALL; NbExp=3; IntAct=EBI-2340249, EBI-750078;
CC Q96GF1; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-2340249, EBI-12070086;
CC Q96GF1; A6NDP7: MYADML2; NbExp=3; IntAct=EBI-2340249, EBI-17641390;
CC Q96GF1; Q0D2K0: NIPAL4; NbExp=3; IntAct=EBI-2340249, EBI-9550165;
CC Q96GF1; Q99942: RNF5; NbExp=3; IntAct=EBI-2340249, EBI-348482;
CC Q96GF1; P55061: TMBIM6; NbExp=4; IntAct=EBI-2340249, EBI-1045825;
CC Q96GF1; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-2340249, EBI-348587;
CC Q96GF1; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-2340249, EBI-741829;
CC Q96GF1; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-2340249, EBI-12015604;
CC Q96GF1; P51668: UBE2D1; NbExp=4; IntAct=EBI-2340249, EBI-743540;
CC Q96GF1; P62837: UBE2D2; NbExp=4; IntAct=EBI-2340249, EBI-347677;
CC Q96GF1; Q9Y2X8: UBE2D4; NbExp=4; IntAct=EBI-2340249, EBI-745527;
CC Q96GF1; Q96LR5: UBE2E2; NbExp=4; IntAct=EBI-2340249, EBI-2129763;
CC Q96GF1; Q969T4: UBE2E3; NbExp=8; IntAct=EBI-2340249, EBI-348496;
CC Q96GF1; P61086: UBE2K; NbExp=3; IntAct=EBI-2340249, EBI-473850;
CC Q96GF1; Q9BWQ6: YIPF2; NbExp=6; IntAct=EBI-2340249, EBI-751204;
CC Q96GF1; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-2340249, EBI-751253;
CC Q96GF1; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-2340249, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:21931693}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24019521, ECO:0000269|PubMed:27485036}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96GF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96GF1-2; Sequence=VSP_020004;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:27485036}.
CC -!- INDUCTION: Up-regulated by unfolded protein response (UPR) and
CC endoplasmic reticulum (ER) stress triggered by thapsigargin or
CC tunicamycin. {ECO:0000269|PubMed:24019521,
CC ECO:0000269|PubMed:27485036}.
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC ubiquitin ligase activity. {ECO:0000269|PubMed:27485036}.
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DR EMBL; DQ296559; ABB97506.1; -; mRNA.
DR EMBL; DQ296561; ABB97508.1; -; mRNA.
DR EMBL; DQ296562; ABB97509.1; -; mRNA.
DR EMBL; DQ296565; ABB97512.1; -; mRNA.
DR EMBL; CR456349; CAG30235.1; -; mRNA.
DR EMBL; AK095947; BAC04659.1; -; mRNA.
DR EMBL; AK291236; BAF83925.1; -; mRNA.
DR EMBL; AC002073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59947.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW59949.1; -; Genomic_DNA.
DR EMBL; BC009504; AAH09504.1; -; mRNA.
DR EMBL; BC026040; AAH26040.1; -; mRNA.
DR EMBL; BC033166; AAH33166.1; -; mRNA.
DR EMBL; BC012817; AAH12817.1; -; mRNA.
DR EMBL; BC035684; AAH35684.1; -; mRNA.
DR CCDS; CCDS13890.1; -. [Q96GF1-1]
DR CCDS; CCDS46689.1; -. [Q96GF1-2]
DR RefSeq; NP_001129297.1; NM_001135825.1. [Q96GF1-2]
DR RefSeq; NP_689480.2; NM_152267.3. [Q96GF1-1]
DR AlphaFoldDB; Q96GF1; -.
DR SMR; Q96GF1; -.
DR BioGRID; 124834; 185.
DR IntAct; Q96GF1; 43.
DR MINT; Q96GF1; -.
DR STRING; 9606.ENSP00000320508; -.
DR iPTMnet; Q96GF1; -.
DR PhosphoSitePlus; Q96GF1; -.
DR BioMuta; RNF185; -.
DR DMDM; 74751883; -.
DR EPD; Q96GF1; -.
DR jPOST; Q96GF1; -.
DR MassIVE; Q96GF1; -.
DR MaxQB; Q96GF1; -.
DR PaxDb; Q96GF1; -.
DR PeptideAtlas; Q96GF1; -.
DR PRIDE; Q96GF1; -.
DR ProteomicsDB; 76632; -. [Q96GF1-1]
DR ProteomicsDB; 76633; -. [Q96GF1-2]
DR TopDownProteomics; Q96GF1-1; -. [Q96GF1-1]
DR TopDownProteomics; Q96GF1-2; -. [Q96GF1-2]
DR Antibodypedia; 24963; 152 antibodies from 22 providers.
DR DNASU; 91445; -.
DR Ensembl; ENST00000266252.8; ENSP00000266252.7; ENSG00000138942.17. [Q96GF1-2]
DR Ensembl; ENST00000326132.11; ENSP00000320508.5; ENSG00000138942.17. [Q96GF1-1]
DR Ensembl; ENST00000518626.5; ENSP00000427755.1; ENSG00000138942.17. [Q96GF1-1]
DR GeneID; 91445; -.
DR KEGG; hsa:91445; -.
DR MANE-Select; ENST00000326132.11; ENSP00000320508.5; NM_152267.4; NP_689480.2.
DR UCSC; uc003akb.4; human. [Q96GF1-1]
DR CTD; 91445; -.
DR DisGeNET; 91445; -.
DR GeneCards; RNF185; -.
DR HGNC; HGNC:26783; RNF185.
DR HPA; ENSG00000138942; Low tissue specificity.
DR neXtProt; NX_Q96GF1; -.
DR OpenTargets; ENSG00000138942; -.
DR PharmGKB; PA142671056; -.
DR VEuPathDB; HostDB:ENSG00000138942; -.
DR eggNOG; KOG0823; Eukaryota.
DR GeneTree; ENSGT00390000014107; -.
DR HOGENOM; CLU_055198_2_2_1; -.
DR InParanoid; Q96GF1; -.
DR OMA; RTFECNI; -.
DR PhylomeDB; Q96GF1; -.
DR TreeFam; TF317334; -.
DR PathwayCommons; Q96GF1; -.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR SignaLink; Q96GF1; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 91445; 11 hits in 1116 CRISPR screens.
DR ChiTaRS; RNF185; human.
DR GenomeRNAi; 91445; -.
DR Pharos; Q96GF1; Tbio.
DR PRO; PR:Q96GF1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q96GF1; protein.
DR Bgee; ENSG00000138942; Expressed in kidney epithelium and 179 other tissues.
DR ExpressionAtlas; Q96GF1; baseline and differential.
DR Genevisible; Q96GF1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
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; IPI:ParkinsonsUK-UCL.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0036503; P:ERAD pathway; IGI:ParkinsonsUK-UCL.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; IMP:UniProtKB.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:ParkinsonsUK-UCL.
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 1: Evidence at protein 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_0000247520"
FT TOPO_DOM 1..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21931693"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..171
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:21931693"
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:0000269|PubMed:27485036"
FT REGION 90..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 66..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_020004"
FT MUTAGEN 39
FT /note="C->A: Abolished E3 ubiquitin-protein ligase activity
FT and ability to regulate the cGAS-STING pathway; when
FT associated with A-79."
FT /evidence="ECO:0000269|PubMed:28273161"
FT MUTAGEN 39
FT /note="C->S: Decreased ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:27485036"
FT MUTAGEN 79
FT /note="C->A: Abolished E3 ubiquitin-protein ligase activity
FT and ability to regulate the cGAS-STING pathway; when
FT associated with A-39."
FT /evidence="ECO:0000269|PubMed:28273161"
SQ SEQUENCE 192 AA; 20459 MW; F24B49EA566740B3 CRC64;
MASKGPSASA SPENSSAGGP SGSSNGAGES GGQDSTFECN ICLDTAKDAV ISLCGHLFCW
PCLHQWLETR PNRQVCPVCK AGISRDKVIP LYGRGSTGQQ DPREKTPPRP QGQRPEPENR
GGFQGFGFGD GGFQMSFGIG AFPFGIFATA FNINDGRPPP AVPGTPQYVD EQFLSRLFLF
VALVIMFWLL IA
