SELW_RAT
ID SELW_RAT Reviewed; 88 AA.
AC P63301; O35965; P49904; Q9JIC2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Selenoprotein W {ECO:0000303|PubMed:7568010};
DE Short=SelW {ECO:0000303|PubMed:7568010};
GN Name=Selenow {ECO:0000312|RGD:3661};
GN Synonyms=Selw {ECO:0000303|PubMed:7568010}, Sepw1 {ECO:0000312|RGD:3661};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=7568010; DOI=10.1073/pnas.92.19.8749;
RA Vendeland S.C., Beilstein M.A., Yeh J.-Y., Ream W., Whanger P.D.;
RT "Rat skeletal muscle selenoprotein W: cDNA clone and mRNA modulation by
RT dietary selenium.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8749-8753(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [3]
RP PROTEIN SEQUENCE OF 2-77.
RC TISSUE=Skeletal muscle;
RA Beilstein M.A., Vendeland S.C., Andrews J.S., Whanger P.D.;
RT "Immunization with a synthetic peptide to produce antibodies to a rat
RT muscle selenoprotein.";
RL FASEB J. 7:A289-A289(1993).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=8349599; DOI=10.1016/s0021-9258(19)85307-3;
RA Vendeland S.C., Beilstein M.A., Chen C.L., Jensen O.N., Barofsky E.,
RA Whanger P.D.;
RT "Purification and properties of selenoprotein W from rat muscle.";
RL J. Biol. Chem. 268:17103-17107(1993).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
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 [6]
RP GLUTATHIONYLATION, AND MASS SPECTROMETRY.
RC TISSUE=Muscle;
RX PubMed=8576706; DOI=10.1016/0162-0134(95)00045-3;
RA Beilstein M.A., Vendeland S.C., Barofsky E., Jensen O.N., Whanger P.D.;
RT "Selenoprotein W of rat muscle binds glutathione and an unknown small
RT molecular weight moiety.";
RL J. Inorg. Biochem. 61:117-124(1996).
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.
CC -!- SUBUNIT: Interacts with DPYSL2, PRDX1, YWHAB, YWHAG, HSP70 and HSP90.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7896009}.
CC -!- TISSUE SPECIFICITY: Higher levels are seen in the muscle and brain
CC while lower levels are seen in the spleen and testis. Not detected in
CC liver, heart, kidney, intestinal mucosa, intestinal muscle, lung,
CC plasma or erythrocytes (at protein level).
CC {ECO:0000269|PubMed:7896009}.
CC -!- INDUCTION: In skeletal muscle, by dietary selenium.
CC {ECO:0000269|PubMed:7896009}.
CC -!- MASS SPECTROMETRY: Mass=9898; Method=MALDI; Note=With bound glutathione
CC and undetermined modification.; Evidence={ECO:0000269|PubMed:8576706};
CC -!- MASS SPECTROMETRY: Mass=9853; Method=MALDI; Note=With bound
CC glutathione.; Evidence={ECO:0000269|PubMed:8576706};
CC -!- MASS SPECTROMETRY: Mass=9592; Method=MALDI; Note=With undetermined
CC modification.; Evidence={ECO:0000269|PubMed:8576706};
CC -!- MASS SPECTROMETRY: Mass=9549; Method=MALDI; Note=Without bound
CC glutathione or undetermined modification.;
CC Evidence={ECO:0000269|PubMed:8576706};
CC -!- SIMILARITY: Belongs to the SelWTH family. Selenoprotein W subfamily.
CC {ECO:0000305}.
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DR EMBL; U25264; AAC52255.2; -; mRNA.
DR EMBL; BC087625; AAH87625.1; -; mRNA.
DR RefSeq; NP_037159.4; NM_013027.3.
DR BMRB; P63301; -.
DR SMR; P63301; -.
DR STRING; 10116.ENSRNOP00000018559; -.
DR iPTMnet; P63301; -.
DR PhosphoSitePlus; P63301; -.
DR PaxDb; P63301; -.
DR GeneID; 25545; -.
DR KEGG; rno:25545; -.
DR UCSC; RGD:3661; rat.
DR CTD; 6415; -.
DR RGD; 3661; Selenow.
DR eggNOG; ENOG502S9W8; Eukaryota.
DR InParanoid; P63301; -.
DR OrthoDB; 1594709at2759; -.
DR PhylomeDB; P63301; -.
DR PRO; PR:P63301; -.
DR Proteomes; UP000002494; Unplaced.
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; IEP:RGD.
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; Direct protein sequencing; Glutathionylation;
KW Redox-active center; Reference proteome; Selenocysteine.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..88
FT /note="Selenoprotein W"
FT /id="PRO_0000097682"
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 88 AA; 9687 MW; 03E297B668D3D7E0 CRC64;
MALAVRVVYC GAUGYKPKYL QLKEKLEHEF PGCLDICGEG TPQVTGFFEV TVAGKLVHSK
KRGDGYVDTE SKFRKLVTAI KAALAQCQ
