ID   SELW_MACMU              Reviewed;          87 AA.
AC   P63303; O15532; O19096; Q86TI9; Q96KM5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   29-SEP-2021, entry version 72.
DE   RecName: Full=Selenoprotein W {ECO:0000303|PubMed:9256076};
DE            Short=SelW {ECO:0000250|UniProtKB:P63302};
GN   Name=SELENOW {ECO:0000250|UniProtKB:P63302};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
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   FUNCTION, MASS SPECTROMETRY, AND GLUTATHIONYLATION AT CYS-37.
RX   PubMed=9882425; DOI=10.1006/abbi.1998.0949;
RA   Gu Q.P., Beilstein M.A., Barofsky E., Ream W., Whanger P.D.;
RT   "Purification, characterization, and glutathione binding to selenoprotein W
RT   from monkey muscle.";
RL   Arch. Biochem. Biophys. 361:25-33(1999).
RN   [3]
RP   TISSUE SPECIFICITY.
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).
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       ECO:0000269|PubMed:9882425}.
CC   -!- SUBUNIT: Interacts with DPYSL2, PRDX1, YWHAB, YWHAG, HSP70 and HSP90.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highest levels detected in skeletal muscle, tongue,
CC       heart and brain. Expressed at significantly higher levels in female
CC       skeletal muscle than in male and at slightly higher levels in female
CC       cardiac muscle than in male (at protein level). Also detected at low
CC       levels in liver. {ECO:0000269|PubMed:10718624}.
CC   -!- MASS SPECTROMETRY: Mass=9635; Method=MALDI; Note=With bound
CC       glutathione. Major form in muscle.;
CC       Evidence={ECO:0000269|PubMed:9882425};
CC   -!- MASS SPECTROMETRY: Mass=9371; Method=MALDI; Note=With an undetermined
CC       modification.; Evidence={ECO:0000269|PubMed:9882425};
CC   -!- MASS SPECTROMETRY: Mass=9330; Method=MALDI; Note=Without bound
CC       glutathione or undetermined modification.;
CC       Evidence={ECO:0000269|PubMed:9882425};
CC   -!- SIMILARITY: Belongs to the SelWTH family. Selenoprotein W subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U67450; AAC51666.1; -; mRNA.
DR   RefSeq; NP_001036202.1; NM_001042737.1.
DR   GeneID; 718370; -.
DR   KEGG; mcc:718370; -.
DR   CTD; 6415; -.
DR   InParanoid; P63303; -.
DR   OrthoDB; 1594709at2759; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
DR   GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; NAS: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   Antioxidant; Cytoplasm; Glutathionylation; Redox-active center;
KW   Reference proteome; Selenocysteine.
FT   CHAIN           1..87
FT                   /note="Selenoprotein W"
FT                   /id="PRO_0000097679"
FT   NON_STD         13
FT                   /note="Selenocysteine"
FT   MOD_RES         37
FT                   /note="S-glutathionyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:9882425"
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