SELS_MOUSE
ID SELS_MOUSE Reviewed; 190 AA.
AC Q9BCZ4; Q921S1; Q9DB55;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Selenoprotein S {ECO:0000250|UniProtKB:Q9BQE4};
DE Short=SelS {ECO:0000250|UniProtKB:Q9BQE4};
DE AltName: Full=Minor histocompatibility antigen H47 {ECO:0000303|PubMed:11254699};
GN Name=Selenos {ECO:0000312|MGI:MGI:95994};
GN Synonyms=H47 {ECO:0000303|PubMed:11254699},
GN Vimp {ECO:0000312|MGI:MGI:95994};
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 [MRNA], AND VARIANT PHE-46.
RC STRAIN=C57BL/6J;
RX PubMed=11254699; DOI=10.4049/jimmunol.166.7.4438;
RA Mendoza L.M., Villaflor G., Eden P., Roopenian D., Shastri N.;
RT "Distinguishing self from nonself: immunogenicity of the murine H47 locus
RT is determined by a single amino acid substitution in an unusual peptide.";
RL J. Immunol. 166:4438-4445(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH CCDC47.
RX PubMed=25009997; DOI=10.1016/j.ydbio.2014.06.024;
RA Yamamoto S., Yamazaki T., Komazaki S., Yamashita T., Osaki M.,
RA Matsubayashi M., Kidoya H., Takakura N., Yamazaki D., Kakizawa S.;
RT "Contribution of calumin to embryogenesis through participation in the
RT endoplasmic reticulum-associated degradation activity.";
RL Dev. Biol. 393:33-43(2014).
CC -!- FUNCTION: Involved in the degradation process of misfolded endoplasmic
CC reticulum (ER) luminal proteins. Participates in the transfer of
CC misfolded proteins from the ER to the cytosol, where they are destroyed
CC by the proteasome in a ubiquitin-dependent manner. Probably acts by
CC serving as a linker between DERL1, which mediates the
CC retrotranslocation of misfolded proteins into the cytosol, and the
CC ATPase complex VCP, which mediates the translocation and ubiquitination
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DERL1 and (via VIM motif) with VCP, suggesting
CC that it forms a membrane complex with DERL1 that serves as a receptor
CC for VCP. Also interacts with DERL2, DERL3 and SELENOK. The SELENOK-
CC SELENOS complex interacts with VCP (By similarity). Interacts with
CC CCDC47 (PubMed:25009997). {ECO:0000250, ECO:0000250|UniProtKB:Q9BQE4,
CC ECO:0000269|PubMed:25009997}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- PTM: Truncated SELENOS proteins produced by failed UGA/Sec decoding are
CC ubiquitinated by the CRL2(KLHDC2) and CRL2(KLHDC3) complexes, which
CC recognizes the glycine (Gly) at the C-terminus of truncated SELENOS
CC proteins. Truncated SELENOS proteins produced by failed UGA/Sec
CC decoding are also ubiquitinated by the CRL5(KLHDC1) complex.
CC {ECO:0000250|UniProtKB:Q9BQE4}.
CC -!- MISCELLANEOUS: One of the histocompatibility antigen responsible for
CC chronic graft rejection.
CC -!- SIMILARITY: Belongs to the selenoprotein S family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11091.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK07659.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB23882.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF335543; AAK07659.1; ALT_SEQ; mRNA.
DR EMBL; AK005204; BAB23882.1; ALT_SEQ; mRNA.
DR EMBL; BC011091; AAH11091.1; ALT_SEQ; mRNA.
DR CCDS; CCDS39977.1; -.
DR RefSeq; NP_001335175.1; NM_001348246.1.
DR RefSeq; NP_077759.3; NM_024439.3.
DR BioGRID; 225064; 1.
DR STRING; 10090.ENSMUSP00000099301; -.
DR iPTMnet; Q9BCZ4; -.
DR PhosphoSitePlus; Q9BCZ4; -.
DR EPD; Q9BCZ4; -.
DR MaxQB; Q9BCZ4; -.
DR PaxDb; Q9BCZ4; -.
DR PeptideAtlas; Q9BCZ4; -.
DR PRIDE; Q9BCZ4; -.
DR ProteomicsDB; 261147; -.
DR Antibodypedia; 2437; 148 antibodies from 25 providers.
DR DNASU; 109815; -.
DR Ensembl; ENSMUST00000101801; ENSMUSP00000099301; ENSMUSG00000075701.
DR GeneID; 109815; -.
DR KEGG; mmu:109815; -.
DR UCSC; uc009hha.1; mouse.
DR CTD; 55829; -.
DR MGI; MGI:95994; Selenos.
DR VEuPathDB; HostDB:ENSMUSG00000075701; -.
DR eggNOG; ENOG502RXYU; Eukaryota.
DR GeneTree; ENSGT00390000015688; -.
DR HOGENOM; CLU_117238_0_0_1; -.
DR InParanoid; Q9BCZ4; -.
DR OMA; LSLYGWY; -.
DR OrthoDB; 1489479at2759; -.
DR PhylomeDB; Q9BCZ4; -.
DR TreeFam; TF329454; -.
DR BioGRID-ORCS; 109815; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Selenos; mouse.
DR PRO; PR:Q9BCZ4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9BCZ4; protein.
DR Bgee; ENSMUSG00000075701; Expressed in lacrimal gland and 257 other tissues.
DR ExpressionAtlas; Q9BCZ4; baseline and differential.
DR Genevisible; Q9BCZ4; MM.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:MGI.
DR GO; GO:0036502; C:Derlin-1-VIMP complex; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0034362; C:low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0016209; F:antioxidant activity; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
DR GO; GO:0045454; P:cell redox homeostasis; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:MGI.
DR GO; GO:0006983; P:ER overload response; ISO:MGI.
DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; ISO:MGI.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IC:BHF-UCL.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:BHF-UCL.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; ISO:MGI.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:BHF-UCL.
DR GO; GO:0080164; P:regulation of nitric oxide metabolic process; ISO:MGI.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0051775; P:response to redox state; ISO:MGI.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR InterPro; IPR009703; Selenoprotein_S.
DR PANTHER; PTHR28621; PTHR28621; 1.
DR Pfam; PF06936; Selenoprotein_S; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Membrane; Reference proteome;
KW Selenocysteine; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..190
FT /note="Selenoprotein S"
FT /id="PRO_0000097673"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 78..90
FT /note="VCP/p97-interacting motif (VIM)"
FT /evidence="ECO:0000250|UniProtKB:Q9BQE4"
FT REGION 115..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 189
FT /note="Selenocysteine"
FT /evidence="ECO:0000250"
FT VARIANT 46
FT /note="I -> F (in allele H47b)"
FT /evidence="ECO:0000269|PubMed:11254699"
FT CONFLICT 10
FT /note="A -> P (in Ref. 3; AAH11091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 21509 MW; 2C65830750A37D5E CRC64;
MDRDEEPLSA RPALETESLR FLHVTVGSLL ASYGWYILFS CILLYIVIQR LSLRLRALRQ
RQLDQAETVL EPDVVVKRQE ALAAARLRMQ EDLNAQVEKH KEKLRQLEEE KRRQKIEMWD
SMQEGRSYKR NSGRPQEEDG PGPSTSSVIP KGKSDKKPLR GGGYNPLTGE GGGTCSWRPG
RRGPSSGGUN
