SELW_MOUSE
ID SELW_MOUSE Reviewed; 88 AA.
AC P63300; O35965; P49904; Q9JIC2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Selenoprotein W {ECO:0000303|PubMed:9256076};
DE Short=SelW {ECO:0000303|PubMed:12062442};
GN Name=Selenow {ECO:0000312|MGI:MGI:1100878};
GN Synonyms=Selw {ECO:0000303|PubMed:12062442},
GN Sepw1 {ECO:0000312|MGI:MGI:1100878};
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].
RC TISSUE=Skeletal muscle;
RX PubMed=9256076; DOI=10.1016/s0378-1119(97)00113-3;
RA Gu Q.-P., Beilstein M.A., Vendeland S.C., Lugade A., Ream W., Whanger P.D.;
RT "Conserved features of selenocysteine insertion sequence (SECIS) elements
RT in selenoprotein W cDNAs from five species.";
RL Gene 193:187-196(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF SEC-13 AND CYS-37.
RC TISSUE=Brain;
RX PubMed=12062442; DOI=10.1016/s0014-5793(02)02628-5;
RA Jeong D., Kim T.S., Chung Y.W., Lee B.J., Kim I.Y.;
RT "Selenoprotein W is a glutathione-dependent antioxidant in vivo.";
RL FEBS Lett. 517:225-228(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH YWHAB; YWHAG;
RP DPYSL2; PRDX1; HSP70 AND HSP90, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=17503775; DOI=10.1021/bi602462q;
RA Dikiy A., Novoselov S.V., Fomenko D.E., Sengupta A., Carlson B.A.,
RA Cerny R.L., Ginalski K., Grishin N.V., Hatfield D.L., Gladyshev V.N.;
RT "SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the
RT functions of selenoproteins of a novel thioredoxin-like family.";
RL Biochemistry 46:6871-6882(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetus;
RA Bellingham J., Gregory-Evans C.Y.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Stomach;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16876868; DOI=10.1016/j.jinorgbio.2006.05.018;
RA Loflin J., Lopez N., Whanger P.D., Kioussi C.;
RT "Selenoprotein W during development and oxidative stress.";
RL J. Inorg. Biochem. 100:1679-1684(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [9]
RP STRUCTURE BY NMR OF MUTANT SER-10/CYS-13, AND INTERACTION WITH YWHAB AND
RP YWHAG.
RX PubMed=17928294; DOI=10.1074/jbc.m705410200;
RA Aachmann F.L., Fomenko D.E., Soragni A., Gladyshev V.N., Dikiy A.;
RT "Solution structure of selenoprotein W and NMR analysis of its interaction
RT with 14-3-3 proteins.";
RL J. Biol. Chem. 282:37036-37044(2007).
CC -!- FUNCTION: Plays a role as a glutathione (GSH)-dependent antioxidant.
CC May be involved in a redox-related process. May play a role in the
CC myopathies of selenium deficiency. {ECO:0000269|PubMed:12062442,
CC ECO:0000269|PubMed:16876868, ECO:0000269|PubMed:17503775}.
CC -!- SUBUNIT: Interacts with DPYSL2, PRDX1, YWHAB, YWHAG, HSP70 and HSP90.
CC {ECO:0000269|PubMed:17503775, ECO:0000269|PubMed:17928294}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: In the embryo, expressed in the developing nervous
CC system and in mesoderm-derived tissues such as heart and limbs. In the
CC adult, predominantly expressed in brain, skeletal muscle and heart.
CC {ECO:0000269|PubMed:16876868, ECO:0000269|PubMed:17503775}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected in the newly
CC implanted embryo. Levels increase gradually during embryonic
CC development with a steady increase during the second week and a
CC dramatic increase by the end of gestation. Expression increases
CC gradually in proliferating myotubes but is low in terminally
CC differentiated myobutubes. {ECO:0000269|PubMed:16876868}.
CC -!- INDUCTION: Down-regulated by hydrogen peroxide. Increased levels are
CC detected after treatment with L-buthionine sulfoxide (BSO) before
CC exposure to hydrogen peroxide. {ECO:0000269|PubMed:16876868}.
CC -!- SIMILARITY: Belongs to the SelWTH family. Selenoprotein W subfamily.
CC {ECO:0000305}.
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DR EMBL; U67890; AAC53317.1; -; mRNA.
DR EMBL; AF241527; AAF64481.1; -; mRNA.
DR EMBL; AF015284; AAB69860.1; -; mRNA.
DR EMBL; AK002870; BAC55247.1; -; mRNA.
DR EMBL; AK028124; BAC55256.1; -; mRNA.
DR EMBL; BC052719; AAH52719.2; -; mRNA.
DR CCDS; CCDS39778.1; -.
DR RefSeq; NP_033182.1; NM_009156.2.
DR PDB; 2NPB; NMR; -; A=1-88.
DR PDBsum; 2NPB; -.
DR BMRB; P63300; -.
DR SMR; P63300; -.
DR STRING; 10090.ENSMUSP00000038943; -.
DR PhosphoSitePlus; P63300; -.
DR EPD; P63300; -.
DR MaxQB; P63300; -.
DR PaxDb; P63300; -.
DR PeptideAtlas; P63300; -.
DR PRIDE; P63300; -.
DR ProteomicsDB; 261148; -.
DR Antibodypedia; 61829; 98 antibodies from 16 providers.
DR DNASU; 20364; -.
DR Ensembl; ENSMUST00000044355; ENSMUSP00000038943; ENSMUSG00000041571.
DR GeneID; 20364; -.
DR KEGG; mmu:20364; -.
DR UCSC; uc009fgp.1; mouse.
DR CTD; 6415; -.
DR MGI; MGI:1100878; Selenow.
DR VEuPathDB; HostDB:ENSMUSG00000041571; -.
DR eggNOG; ENOG502S9W8; Eukaryota.
DR GeneTree; ENSGT00940000161069; -.
DR HOGENOM; CLU_170012_0_0_1; -.
DR InParanoid; P63300; -.
DR OMA; AGYKPKY; -.
DR OrthoDB; 1594709at2759; -.
DR PhylomeDB; P63300; -.
DR TreeFam; TF326627; -.
DR BioGRID-ORCS; 20364; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Selenow; mouse.
DR EvolutionaryTrace; P63300; -.
DR PRO; PR:P63300; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P63300; protein.
DR Bgee; ENSMUSG00000041571; Expressed in floor plate of midbrain and 247 other tissues.
DR Genevisible; P63300; MM.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
DR GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; TAS:UniProtKB.
DR GO; GO:0010269; P:response to selenium ion; IBA:GO_Central.
DR InterPro; IPR011893; Selenoprotein_Rdx-typ.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF10262; Rdx; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02174; CXXU_selWTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Cytoplasm; Glutathionylation;
KW Redox-active center; Reference proteome; Selenocysteine.
FT CHAIN 1..88
FT /note="Selenoprotein W"
FT /id="PRO_0000097680"
FT NON_STD 13
FT /note="Selenocysteine"
FT MOD_RES 37
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 10..13
FT /note="Cysteinyl-selenocysteine (Cys-Sec); redox-active"
FT /evidence="ECO:0000250"
FT MUTAGEN 10
FT /note="C->S: Disrupts redox reaction."
FT MUTAGEN 13
FT /note="U->C: Increased sensitivity to hydrogen peroxide-
FT induced toxicity."
FT /evidence="ECO:0000269|PubMed:12062442"
FT MUTAGEN 13
FT /note="U->S: Impairs protection against hydrogen peroxide-
FT induced toxicity."
FT /evidence="ECO:0000269|PubMed:12062442"
FT MUTAGEN 37
FT /note="C->S: Impairs protection against hydrogen peroxide-
FT induced toxicity."
FT /evidence="ECO:0000269|PubMed:12062442"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2NPB"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:2NPB"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:2NPB"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2NPB"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2NPB"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:2NPB"
FT HELIX 70..87
FT /evidence="ECO:0007829|PDB:2NPB"
SQ SEQUENCE 88 AA; 9687 MW; 03E297B668D3D7E0 CRC64;
MALAVRVVYC GAUGYKPKYL QLKEKLEHEF PGCLDICGEG TPQVTGFFEV TVAGKLVHSK
KRGDGYVDTE SKFRKLVTAI KAALAQCQ
