ID   SELW_HUMAN              Reviewed;          87 AA.
AC   P63302; A8MRR7; O15532; O19096; Q86TI9; Q96KM5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Selenoprotein W {ECO:0000303|PubMed:27645994, ECO:0000303|PubMed:9256076};
DE            Short=SelW {ECO:0000303|PubMed:27645994};
GN   Name=SELENOW {ECO:0000303|PubMed:27645994, ECO:0000312|HGNC:HGNC:10752};
GN   Synonyms=SELW {ECO:0000303|PubMed:27645994},
GN   SEPW1 {ECO:0000303|PubMed:12818432, ECO:0000312|HGNC:HGNC:10752};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=12818432; DOI=10.1016/s0167-4781(03)00078-2;
RA   Bellingham J., Gregory-Evans K., Fox M.F., Gregory-Evans C.Y.;
RT   "Gene structure and tissue expression of human selenoprotein W, SEPW1, and
RT   identification of a retroprocessed pseudogene, SEPW1P.";
RL   Biochim. Biophys. Acta 1627:140-146(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, PNS, Testis, and Uterus;
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, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10718624; DOI=10.1023/a:1007065829068;
RA   Gu Q.P., Sun Y., Ream L.W., Whanger P.D.;
RT   "Selenoprotein W accumulates primarily in primate skeletal muscle, heart,
RT   brain and tongue.";
RL   Mol. Cell. Biochem. 204:49-56(2000).
RN   [6]
RP   NOMENCLATURE.
RX   PubMed=27645994; DOI=10.1074/jbc.m116.756155;
RA   Gladyshev V.N., Arner E.S., Berry M.J., Brigelius-Flohe R., Bruford E.A.,
RA   Burk R.F., Carlson B.A., Castellano S., Chavatte L., Conrad M.,
RA   Copeland P.R., Diamond A.M., Driscoll D.M., Ferreiro A., Flohe L.,
RA   Green F.R., Guigo R., Handy D.E., Hatfield D.L., Hesketh J., Hoffmann P.R.,
RA   Holmgren A., Hondal R.J., Howard M.T., Huang K., Kim H.Y., Kim I.Y.,
RA   Koehrle J., Krol A., Kryukov G.V., Lee B.J., Lee B.C., Lei X.G., Liu Q.,
RA   Lescure A., Lobanov A.V., Loscalzo J., Maiorino M., Mariotti M.,
RA   Sandeep Prabhu K., Rayman M.P., Rozovsky S., Salinas G., Schmidt E.E.,
RA   Schomburg L., Schweizer U., Simonovic M., Sunde R.A., Tsuji P.A.,
RA   Tweedie S., Ursini F., Whanger P.D., Zhang Y.;
RT   "Selenoprotein gene nomenclature.";
RL   J. Biol. Chem. 291:24036-24040(2016).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DPYSL2, PRDX1, YWHAB, YWHAG, HSP70 and HSP90.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC       skeletal muscle and heart, moderate levels in brain, spinal cord,
CC       thyroid, spleen, prostate, ovary, small intestine and colon, and lowest
CC       levels in liver and lymph node. {ECO:0000269|PubMed:10718624,
CC       ECO:0000269|PubMed:12818432}.
CC   -!- SIMILARITY: Belongs to the SelWTH family. Selenoprotein W subfamily.
CC       {ECO:0000305}.
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; U67171; AAC51665.1; -; mRNA.
DR   EMBL; AF015283; AAB69859.1; -; mRNA.
DR   EMBL; AF247455; AAL00898.1; -; Genomic_DNA.
DR   EMBL; AF247454; AAL00898.1; JOINED; Genomic_DNA.
DR   EMBL; AC008745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000581; AAH00581.1; -; mRNA.
DR   EMBL; BC032546; AAH32546.1; -; mRNA.
DR   EMBL; BC039597; AAH39597.1; -; mRNA.
DR   EMBL; BC047893; AAH47893.2; -; mRNA.
DR   CCDS; CCDS59402.1; -.
DR   RefSeq; NP_003000.1; NM_003009.2.
DR   BioGRID; 112314; 8.
DR   IntAct; P63302; 2.
DR   MINT; P63302; -.
DR   STRING; 9606.ENSP00000473185; -.
DR   iPTMnet; P63302; -.
DR   PhosphoSitePlus; P63302; -.
DR   BioMuta; SELENOW; -.
DR   DMDM; 190358772; -.
DR   EPD; P63302; -.
DR   jPOST; P63302; -.
DR   MassIVE; P63302; -.
DR   PaxDb; P63302; -.
DR   PeptideAtlas; P63302; -.
DR   PRIDE; P63302; -.
DR   ProteomicsDB; 57518; -.
DR   Antibodypedia; 61829; 98 antibodies from 16 providers.
DR   DNASU; 6415; -.
DR   Ensembl; ENST00000593892.5; ENSP00000471149.1; ENSG00000178980.16.
DR   Ensembl; ENST00000595615.1; ENSP00000470941.1; ENSG00000178980.16.
DR   Ensembl; ENST00000601048.6; ENSP00000473185.1; ENSG00000178980.16.
DR   GeneID; 6415; -.
DR   KEGG; hsa:6415; -.
DR   MANE-Select; ENST00000601048.6; ENSP00000473185.1; NM_003009.4; NP_003000.1.
DR   UCSC; uc021uwp.2; human.
DR   CTD; 6415; -.
DR   DisGeNET; 6415; -.
DR   GeneCards; SELENOW; -.
DR   HGNC; HGNC:10752; SELENOW.
DR   HPA; ENSG00000178980; Tissue enhanced (brain, skeletal muscle, tongue).
DR   MIM; 603235; gene.
DR   neXtProt; NX_P63302; -.
DR   OpenTargets; ENSG00000178980; -.
DR   PharmGKB; PA35673; -.
DR   VEuPathDB; HostDB:ENSG00000178980; -.
DR   eggNOG; ENOG502S9W8; Eukaryota.
DR   GeneTree; ENSGT00940000161069; -.
DR   InParanoid; P63302; -.
DR   OrthoDB; 1594709at2759; -.
DR   PhylomeDB; P63302; -.
DR   PathwayCommons; P63302; -.
DR   SignaLink; P63302; -.
DR   BioGRID-ORCS; 6415; 26 hits in 1069 CRISPR screens.
DR   ChiTaRS; SELENOW; human.
DR   GeneWiki; SEPW1; -.
DR   GenomeRNAi; 6415; -.
DR   Pharos; P63302; Tbio.
DR   PRO; PR:P63302; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P63302; protein.
DR   Bgee; ENSG00000178980; Expressed in apex of heart and 207 other tissues.
DR   ExpressionAtlas; P63302; baseline and differential.
DR   Genevisible; P63302; HS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
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   Antioxidant; Cytoplasm; Glutathionylation; Redox-active center;
KW   Reference proteome; Selenocysteine.
FT   CHAIN           1..87
FT                   /note="Selenoprotein W"
FT                   /id="PRO_0000097678"
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"
SQ   SEQUENCE   87 AA;  9448 MW;  F8FDF3194B0654E9 CRC64;
     MALAVRVVYC GAUGYKSKYL QLKKKLEDEF PGRLDICGEG TPQATGFFEV MVAGKLIHSK
     KKGDGYVDTE SKFLKLVAAI KAALAQG