RN183_MOUSE
ID RN183_MOUSE Reviewed; 190 AA.
AC Q8QZS5; B7ZCH3; Q5NBV8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=E3 ubiquitin-protein ligase RNF183;
DE EC=2.3.2.27 {ECO:0000269|PubMed:29300766};
GN Name=Rnf183;
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].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=29507230; DOI=10.1073/pnas.1716439115;
RA Wu Y., Li X., Jia J., Zhang Y., Li J., Zhu Z., Wang H., Tang J., Hu J.;
RT "Transmembrane E3 ligase RNF183 mediates ER stress-induced apoptosis by
RT degrading Bcl-xL.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2762-E2771(2018).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AUTOUBIQUITINATION,
RP TISSUE SPECIFICITY, INTERACTION WITH SEC16A, AND MUTAGENESIS OF CYS-13 AND
RP CYS-16.
RX PubMed=29300766; DOI=10.1371/journal.pone.0190407;
RA Wu Y., Guo X.P., Kanemoto S., Maeoka Y., Saito A., Asada R., Matsuhisa K.,
RA Ohtake Y., Imaizumi K., Kaneko M.;
RT "Sec16A, a key protein in COPII vesicle formation, regulates the stability
RT and localization of the novel ubiquitin ligase RNF183.";
RL PLoS ONE 13:E0190407-E0190407(2018).
CC -!- FUNCTION: Acts as a E3 ubiquitin ligase catalyzing the covalent
CC attachment of ubiquitin moieties onto substrate proteins
CC (PubMed:29300766). Triggers apoptosis in response to prolonged ER
CC stress by mediating the polyubiquitination and subsequent proteasomal
CC degradation of BCL2L1 (By similarity). May collaborate with FATE1 to
CC restrain BIK protein levels thus regulating apoptotic signaling (By
CC similarity). {ECO:0000250|UniProtKB:Q96D59,
CC ECO:0000269|PubMed:29300766}.
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:29300766};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:29300766}.
CC -!- SUBUNIT: Interacts with FATE1 (By similarity). Interacts with SEC16A
CC (PubMed:29300766). Interacts with BCL2L1 (By similarity).
CC {ECO:0000250|UniProtKB:Q96D59, ECO:0000269|PubMed:29300766}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:29300766}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q96D59}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q96D59}. Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000269|PubMed:29300766}. Lysosome membrane
CC {ECO:0000269|PubMed:29300766}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the kidney and testis.
CC {ECO:0000269|PubMed:29300766, ECO:0000269|PubMed:29507230}.
CC -!- PTM: Autoubiquitinated (in vitro). {ECO:0000269|PubMed:29300766}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK017982; BAC25537.1; -; mRNA.
DR EMBL; AL732594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466527; EDL31146.1; -; Genomic_DNA.
DR EMBL; CH466527; EDL31147.1; -; Genomic_DNA.
DR EMBL; BC025512; AAH25512.1; -; mRNA.
DR CCDS; CCDS38775.1; -.
DR RefSeq; NP_705724.1; NM_153504.3.
DR RefSeq; XP_006538402.1; XM_006538339.3.
DR AlphaFoldDB; Q8QZS5; -.
DR SMR; Q8QZS5; -.
DR BioGRID; 217945; 449.
DR IntAct; Q8QZS5; 1.
DR STRING; 10090.ENSMUSP00000103079; -.
DR PaxDb; Q8QZS5; -.
DR PRIDE; Q8QZS5; -.
DR Antibodypedia; 54188; 104 antibodies from 19 providers.
DR DNASU; 76072; -.
DR Ensembl; ENSMUST00000079420; ENSMUSP00000078389; ENSMUSG00000063851.
DR Ensembl; ENSMUST00000107454; ENSMUSP00000103078; ENSMUSG00000063851.
DR Ensembl; ENSMUST00000107455; ENSMUSP00000103079; ENSMUSG00000063851.
DR GeneID; 76072; -.
DR KEGG; mmu:76072; -.
DR UCSC; uc008tes.1; mouse.
DR CTD; 138065; -.
DR MGI; MGI:1923322; Rnf183.
DR VEuPathDB; HostDB:ENSMUSG00000063851; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162965; -.
DR HOGENOM; CLU_122905_0_0_1; -.
DR InParanoid; Q8QZS5; -.
DR OMA; QTGPPQD; -.
DR OrthoDB; 1337075at2759; -.
DR PhylomeDB; Q8QZS5; -.
DR TreeFam; TF337102; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 76072; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Rnf183; mouse.
DR PRO; PR:Q8QZS5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8QZS5; protein.
DR Bgee; ENSMUSG00000063851; Expressed in right kidney and 19 other tissues.
DR Genevisible; Q8QZS5; MM.
DR GO; GO:0033106; C:cis-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP: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; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; IMP: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; ISO:MGI.
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 1: Evidence at protein 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..190
FT /note="E3 ubiquitin-protein ligase RNF183"
FT /id="PRO_0000247359"
FT TOPO_DOM 1..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 160..180
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..190
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT ZN_FING 13..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 13
FT /note="C->S: Decrease in autoubiquitination; when
FT associated with S-16."
FT /evidence="ECO:0000269|PubMed:29300766"
FT MUTAGEN 16
FT /note="C->S: Decrease in autoubiquitination; when
FT associated with S-13."
FT /evidence="ECO:0000269|PubMed:29300766"
SQ SEQUENCE 190 AA; 21625 MW; 0671BD5D56DB7FB1 CRC64;
MSEPQGQELR AECPVCWNPF NNTFHTPKVL DCCHSFCVEC LAHLSLVTPA RRRLLCPLCR
QPTVLASGQP VTDLPTDTAM LTLLRLEPHH VILEGHQLCL KDQPKSRYFL RQPRVYTLDL
GAEPGSQTGL PQDTAPDTRP VPIPSHYSLR ECVRNPHFRI FAYLMAVILS VTLLLIFSIF
WTKQFFWGMG
