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
//