ID   SELW_SHEEP              Reviewed;          87 AA.
AC   O19097;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 4.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Selenoprotein W {ECO:0000303|PubMed:9256076};
DE            Short=SelW {ECO:0000250|UniProtKB:P63302};
GN   Name=SELENOW {ECO:0000250|UniProtKB:P63302};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   TISSUE SPECIFICITY.
RX   PubMed=7896009; DOI=10.1096/fasebj.9.5.7896009;
RA   Yeh J.-Y., Beilstein M.A., Andrews J.S., Whanger P.D.;
RT   "Tissue distribution and influence of selenium status on levels of
RT   selenoprotein W.";
RL   FASEB J. 9:392-396(1995).
RN   [3]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=9082022; DOI=10.1093/jn/127.3.394;
RA   Yeh J.Y., Gu Q.P., Beilstein M.A., Forsberg N.E., Whanger P.D.;
RT   "Selenium influences tissue levels of selenoprotein W in sheep.";
RL   J. Nutr. 127:394-402(1997).
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 {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in muscle, heart, tongue, brain, lung,
CC       spleen, kidney and liver. Highest levels expressed in muscle and heart
CC       whereas lowest levels detected in liver (at protein level).
CC       {ECO:0000269|PubMed:7896009, ECO:0000269|PubMed:9082022}.
CC   -!- INDUCTION: Up-regulated by dietary selenium.
CC       {ECO:0000269|PubMed:9082022}.
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; U67853; AAC48757.1; -; Genomic_DNA.
DR   STRING; 9940.ENSOARP00000012280; -.
DR   Ensembl; ENSOART00020020649; ENSOARP00020017096; ENSOARG00020013536.
DR   eggNOG; ENOG502S9W8; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
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_0000097683"
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;  9475 MW;  A1BE510559047B5E CRC64;
     MAVVVRVVYC GAUGYKPKYL QLKKKLEDEF PSRLDICGEG TPQVTGFFEV FVAGKLVHSK
     KGGDGYVDTE SKFLKLVAAI KAALAQA