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RecName: Full=E3 ubiquitin-protein ligase RNF183

UniProtKB/Swiss-Prot: Q8QZS5.1

Identical Proteins FASTA Graphics 

LOCUS       RN183_MOUSE              190 aa            linear   ROD 27-NOV-2024
DEFINITION  RecName: Full=E3 ubiquitin-protein ligase RNF183.
ACCESSION   Q8QZS5
VERSION     Q8QZS5.1
DBSOURCE    UniProtKB: locus RN183_MOUSE, accession Q8QZS5;
            class: standard.
            extra accessions:B7ZCH3,Q5NBV8
            created: Jul 25, 2006.
            sequence updated: Jun 1, 2002.
            annotation updated: Nov 27, 2024.
            xrefs: AK017982.1, BAC25537.1, AL732594.5, CH466527.2, EDL31146.1,
            EDL31147.1, BC025512.1, AAH25512.1, NP_705724.1, XP_006538402.1
            xrefs (non-sequence databases): CCDS:CCDS38775.1,
            AlphaFoldDB:Q8QZS5, SMR:Q8QZS5, BioGRID:217945, IntAct:Q8QZS5,
            STRING:10090.ENSMUSP00000103079, PaxDb:10090-ENSMUSP00000103079,
            Antibodypedia:54188, DNASU:76072, Ensembl:ENSMUST00000079420.7,
            Ensembl:ENSMUSP00000078389.7, Ensembl:ENSMUSG00000063851.13,
            Ensembl:ENSMUST00000107454.2, Ensembl:ENSMUSP00000103078.2,
            Ensembl:ENSMUST00000107455.8, Ensembl:ENSMUSP00000103079.2,
            GeneID:76072, KEGG:mmu:76072, UCSC:uc008tes.1, AGR:MGI:1923322,
            CTD:138065, MGI:1923322, VEuPathDB:HostDB:ENSMUSG00000063851,
            eggNOG:KOG2177, GeneTree:ENSGT00940000162965,
            HOGENOM:CLU_122905_0_0_1, InParanoid:Q8QZS5, OMA:PNHIILE,
            OrthoDB:52495at2759, PhylomeDB:Q8QZS5, TreeFam:TF337102,
            UniPathway:UPA00143, BioGRID-ORCS:76072, ChiTaRS:Rnf183,
            PRO:PR:Q8QZS5, Proteomes:UP000000589, RNAct:Q8QZS5,
            Bgee:ENSMUSG00000063851, GO:0033106, GO:0005789, GO:0005765,
            GO:0046872, GO:0061630, GO:0006915, GO:1902237, GO:0051865,
            GO:0000209, GO:0034976, CDD:cd16556, FunFam:3.30.40.10:FF:000409,
            Gene3D:3.30.40.10, InterPro:IPR051435, InterPro:IPR001841,
            InterPro:IPR013083, InterPro:IPR017907, PANTHER:PTHR22791:SF7,
            PANTHER:PTHR22791, Pfam:PF13639, SMART:SM00184, SUPFAM:SSF57850,
            PROSITE:PS00518, PROSITE:PS50089
KEYWORDS    Apoptosis; Endoplasmic reticulum; Golgi apparatus; Lysosome;
            Membrane; Metal-binding; Reference proteome; Transferase;
            Transmembrane; Transmembrane helix; Ubl conjugation; Ubl
            conjugation pathway; Zinc; Zinc-finger.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Carninci,P., Kasukawa,T., Katayama,S., Gough,J., Frith,M.C.,
            Maeda,N., Oyama,R., Ravasi,T., Lenhard,B., Wells,C., Kodzius,R.,
            Shimokawa,K., Bajic,V.B., Brenner,S.E., Batalov,S., Forrest,A.R.,
            Zavolan,M., Davis,M.J., Wilming,L.G., Aidinis,V., Allen,J.E.,
            Ambesi-Impiombato,A., Apweiler,R., Aturaliya,R.N., Bailey,T.L.,
            Bansal,M., Baxter,L., Beisel,K.W., Bersano,T., Bono,H., Chalk,A.M.,
            Chiu,K.P., Choudhary,V., Christoffels,A., Clutterbuck,D.R.,
            Crowe,M.L., Dalla,E., Dalrymple,B.P., de Bono,B., Della Gatta,G.,
            di Bernardo,D., Down,T., Engstrom,P., Fagiolini,M., Faulkner,G.,
            Fletcher,C.F., Fukushima,T., Furuno,M., Futaki,S., Gariboldi,M.,
            Georgii-Hemming,P., Gingeras,T.R., Gojobori,T., Green,R.E.,
            Gustincich,S., Harbers,M., Hayashi,Y., Hensch,T.K., Hirokawa,N.,
            Hill,D., Huminiecki,L., Iacono,M., Ikeo,K., Iwama,A., Ishikawa,T.,
            Jakt,M., Kanapin,A., Katoh,M., Kawasawa,Y., Kelso,J., Kitamura,H.,
            Kitano,H., Kollias,G., Krishnan,S.P., Kruger,A., Kummerfeld,S.K.,
            Kurochkin,I.V., Lareau,L.F., Lazarevic,D., Lipovich,L., Liu,J.,
            Liuni,S., McWilliam,S., Madan Babu,M., Madera,M., Marchionni,L.,
            Matsuda,H., Matsuzawa,S., Miki,H., Mignone,F., Miyake,S.,
            Morris,K., Mottagui-Tabar,S., Mulder,N., Nakano,N., Nakauchi,H.,
            Ng,P., Nilsson,R., Nishiguchi,S., Nishikawa,S., Nori,F., Ohara,O.,
            Okazaki,Y., Orlando,V., Pang,K.C., Pavan,W.J., Pavesi,G.,
            Pesole,G., Petrovsky,N., Piazza,S., Reed,J., Reid,J.F., Ring,B.Z.,
            Ringwald,M., Rost,B., Ruan,Y., Salzberg,S.L., Sandelin,A.,
            Schneider,C., Schonbach,C., Sekiguchi,K., Semple,C.A., Seno,S.,
            Sessa,L., Sheng,Y., Shibata,Y., Shimada,H., Shimada,K., Silva,D.,
            Sinclair,B., Sperling,S., Stupka,E., Sugiura,K., Sultana,R.,
            Takenaka,Y., Taki,K., Tammoja,K., Tan,S.L., Tang,S., Taylor,M.S.,
            Tegner,J., Teichmann,S.A., Ueda,H.R., van Nimwegen,E., Verardo,R.,
            Wei,C.L., Yagi,K., Yamanishi,H., Zabarovsky,E., Zhu,S., Zimmer,A.,
            Hide,W., Bult,C., Grimmond,S.M., Teasdale,R.D., Liu,E.T.,
            Brusic,V., Quackenbush,J., Wahlestedt,C., Mattick,J.S., Hume,D.A.,
            Kai,C., Sasaki,D., Tomaru,Y., Fukuda,S., Kanamori-Katayama,M.,
            Suzuki,M., Aoki,J., Arakawa,T., Iida,J., Imamura,K., Itoh,M.,
            Kato,T., Kawaji,H., Kawagashira,N., Kawashima,T., Kojima,M.,
            Kondo,S., Konno,H., Nakano,K., Ninomiya,N., Nishio,T., Okada,M.,
            Plessy,C., Shibata,K., Shiraki,T., Suzuki,S., Tagami,M., Waki,K.,
            Watahiki,A., Okamura-Oho,Y., Suzuki,H., Kawai,J. and Hayashizaki,Y.
  CONSRTM   FANTOM Consortium; RIKEN Genome Exploration Research Group and
            Genome Science Group (Genome Network Project Core Group)
  TITLE     The transcriptional landscape of the mammalian genome
  JOURNAL   Science 309 (5740), 1559-1563 (2005)
   PUBMED   16141072
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            STRAIN=C57BL/6J; TISSUE=Thymus
            Erratum:[Science. 2006 Mar 24;311(5768):1713]
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Church,D.M., Goodstadt,L., Hillier,L.W., Zody,M.C., Goldstein,S.,
            She,X., Bult,C.J., Agarwala,R., Cherry,J.L., DiCuccio,M.,
            Hlavina,W., Kapustin,Y., Meric,P., Maglott,D., Birtle,Z.,
            Marques,A.C., Graves,T., Zhou,S., Teague,B., Potamousis,K.,
            Churas,C., Place,M., Herschleb,J., Runnheim,R., Forrest,D.,
            Amos-Landgraf,J., Schwartz,D.C., Cheng,Z., Lindblad-Toh,K.,
            Eichler,E.E. and Ponting,C.P.
  CONSRTM   Mouse Genome Sequencing Consortium
  TITLE     Lineage-specific biology revealed by a finished genome assembly of
            the mouse
  JOURNAL   PLoS Biol 7 (5), e1000112 (2009)
   PUBMED   19468303
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
            STRAIN=C57BL/6J
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Mural,R.J., Adams,M.D., Myers,E.W., Smith,H.O. and Venter,J.C.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-SEP-2005) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].;
            TISSUE=Mammary tumor
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Wu,Y., Li,X., Jia,J., Zhang,Y., Li,J., Zhu,Z., Wang,H., Tang,J. and
            Hu,J.
  TITLE     Transmembrane E3 ligase RNF183 mediates ER stress-induced apoptosis
            by degrading Bcl-xL
  JOURNAL   Proc Natl Acad Sci U S A 115 (12), E2762-E2771 (2018)
   PUBMED   29507230
  REMARK    TISSUE SPECIFICITY.
REFERENCE   6  (residues 1 to 190)
  AUTHORS   Wu,Y., Guo,X.P., Kanemoto,S., Maeoka,Y., Saito,A., Asada,R.,
            Matsuhisa,K., Ohtake,Y., Imaizumi,K. and Kaneko,M.
  TITLE     Sec16A, a key protein in COPII vesicle formation, regulates the
            stability and localization of the novel ubiquitin ligase RNF183
  JOURNAL   PLoS One 13 (1), e0190407 (2018)
   PUBMED   29300766
  REMARK    FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
            AUTOUBIQUITINATION, TISSUE SPECIFICITY, INTERACTION WITH SEC16A,
            AND MUTAGENESIS OF CYS-13 AND CYS-16.
            Publication Status: Online-Only
COMMENT     On Jul 28, 2006 this sequence version replaced gi:81871672.
            [FUNCTION] Acts as an E3 ubiquitin ligase catalyzing the covalent
            attachment of ubiquitin moieties onto substrate proteins
            (PubMed:29300766). Triggers apoptosis in response to prolonged ER
            stress by mediating the polyubiquitination and subsequent
            proteasomal degradation of BCL2L1 (By similarity). May collaborate
            with FATE1 to restrain BIK protein levels thus regulating apoptotic
            signaling (By similarity). {ECO:0000250|UniProtKB:Q96D59,
            ECO:0000269|PubMed:29300766}.
            [CATALYTIC ACTIVITY] Reaction=S-ubiquitinyl-[E2
            ubiquitin-conjugating enzyme]-L-cysteine + [acceptor
            protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine +
            N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
            Evidence={ECO:0000269|PubMed:29300766}.
            [PATHWAY] Protein modification; protein ubiquitination.
            {ECO:0000269|PubMed:29300766}.
            [SUBUNIT] Interacts with FATE1 (By similarity). Interacts with
            SEC16A (PubMed:29300766). Interacts with BCL2L1 (By similarity).
            {ECO:0000250|UniProtKB:Q96D59, ECO:0000269|PubMed:29300766}.
            [SUBCELLULAR LOCATION] Endoplasmic reticulum membrane
            {ECO:0000269|PubMed:29300766}; Single-pass type IV membrane protein
            {ECO:0000250|UniProtKB:Q96D59}. Endoplasmic reticulum
            {ECO:0000250|UniProtKB:Q96D59}. Golgi apparatus, cis-Golgi network
            membrane {ECO:0000269|PubMed:29300766}. Lysosome membrane
            {ECO:0000269|PubMed:29300766}.
            [TISSUE SPECIFICITY] Highly expressed in the kidney and testis.
            {ECO:0000269|PubMed:29300766, ECO:0000269|PubMed:29507230}.
            [PTM] Autoubiquitinated (in vitro). {ECO:0000269|PubMed:29300766}.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
     gene            1..190
                     /gene="Rnf183"
     Protein         1..190
                     /product="E3 ubiquitin-protein ligase RNF183"
                     /EC_number="2.3.2.27"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..190
                     /region_name="Mature chain"
                     /note="E3 ubiquitin-protein ligase RNF183.
                     /id=PRO_0000247359."
     Region          1..159
                     /region_name="Topological domain"
                     /note="Cytoplasmic. /evidence=ECO:0000305."
     Region          11..66
                     /region_name="RING-HC_RNF183-like"
                     /note="RING finger, HC subclass, found in RING finger
                     protein RNF183, RNF223, RNF225 and similar proteins;
                     cd16556"
                     /db_xref="CDD:438218"
     Region          13..60
                     /region_name="Zinc finger region"
                     /note="RING-type.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00175."
     Site            13
                     /site_type="mutagenized"
                     /note="C->S: Decrease in autoubiquitination; when
                     associated with S-16.
                     /evidence=ECO:0000269|PubMed:29300766."
     Site            16
                     /site_type="mutagenized"
                     /note="C->S: Decrease in autoubiquitination; when
                     associated with S-13.
                     /evidence=ECO:0000269|PubMed:29300766."
     Region          160..180
                     /region_name="Transmembrane region"
                     /note="Helical; Anchor for type IV membrane protein.
                     /evidence=ECO:0000255."
     Region          181..190
                     /region_name="Topological domain"
                     /note="Lumenal. /evidence=ECO:0000305."
ORIGIN      
        1 msepqgqelr aecpvcwnpf nntfhtpkvl dcchsfcvec lahlslvtpa rrrllcplcr
       61 qptvlasgqp vtdlptdtam ltllrlephh vileghqlcl kdqpksryfl rqprvytldl
      121 gaepgsqtgl pqdtapdtrp vpipshyslr ecvrnphfri faylmavils vtlllifsif
      181 wtkqffwgmg
//
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