ID   SELT_CHICK              Reviewed;         199 AA.
AC   Q5ZJN8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Thioredoxin reductase-like selenoprotein T {ECO:0000305};
DE            Short=SelT {ECO:0000250|UniProtKB:P62341};
DE            EC=1.8.1.9 {ECO:0000250|UniProtKB:Q1H5H1};
DE   Flags: Precursor;
GN   Name=SELENOT {ECO:0000250|UniProtKB:P62341};
GN   ORFNames=RCJMB04_16o1 {ECO:0000312|EMBL:CAG32055.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1] {ECO:0000312|EMBL:CAG32055.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB {ECO:0000312|EMBL:CAG32055.1};
RC   TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG32055.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Selenoprotein with thioredoxin reductase-like oxidoreductase
CC       activity. {ECO:0000250|UniProtKB:Q1H5H1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC         Evidence={ECO:0000250|UniProtKB:Q1H5H1};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q1H5H1}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: May contain a selenide-sulfide bond between Cys-50 and Sec-53.
CC       This bond is speculated to serve as redox-active pair (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SelWTH family. Selenoprotein T subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG32055.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ720396; CAG32055.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001006557.3; NM_001006557.3.
DR   STRING; 9031.ENSGALP00000016915; -.
DR   PaxDb; Q5ZJN8; -.
DR   Ensembl; ENSGALT00000016934; ENSGALP00000016915; ENSGALG00000010399.
DR   GeneID; 425041; -.
DR   KEGG; gga:425041; -.
DR   CTD; 51714; -.
DR   VEuPathDB; HostDB:geneid_425041; -.
DR   eggNOG; KOG3286; Eukaryota.
DR   GeneTree; ENSGT00390000011725; -.
DR   HOGENOM; CLU_113870_2_0_1; -.
DR   InParanoid; Q5ZJN8; -.
DR   OMA; CISXGYR; -.
DR   OrthoDB; 1542197at2759; -.
DR   PhylomeDB; Q5ZJN8; -.
DR   PRO; PR:Q5ZJN8; -.
DR   Proteomes; UP000000539; Chromosome 9.
DR   Bgee; ENSGALG00000010399; Expressed in spermatid and 12 other tissues.
DR   ExpressionAtlas; Q5ZJN8; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; ISS:UniProtKB.
DR   GO; GO:0045454; P:cell redox homeostasis; ISS:UniProtKB.
DR   GO; GO:0098869; P:cellular oxidant detoxification; ISS:UniProtKB.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR   GO; GO:0031016; P:pancreas development; ISS:UniProtKB.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR   GO; GO:0060124; P:positive regulation of growth hormone secretion; ISS:UniProtKB.
DR   GO; GO:0009749; P:response to glucose; ISS:UniProtKB.
DR   InterPro; IPR011893; Selenoprotein_Rdx-typ.
DR   InterPro; IPR019389; Selenoprotein_T.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR13544; PTHR13544; 1.
DR   Pfam; PF10262; Rdx; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02174; CXXU_selWTH; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; Redox-active center;
KW   Reference proteome; Selenocysteine; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..199
FT                   /note="Thioredoxin reductase-like selenoprotein T"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000252040"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_STD         53
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        50..53
FT                   /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   199 AA;  22318 MW;  FD80F70B96800D92 CRC64;
     MRAAGLGLGI GLLLLAALAG PGGSAEQGGV PAKKLRMAYA TGPLLKFQIC VSUGYRRVFE
     EYMRVISQRY PDIRIEGENY LPQPIYRHIA SFLSVFKLVL IGLIIVGKDP FAFFGMQAPS
     IWQWGQENKV YACMMVFFLS NMIENQCMST GAFEITLNDV PVWSKLESGH LPSMQQLVQI
     LDNEMKLNVH MESMPHHRS