SELTB_DANRE
ID SELTB_DANRE Reviewed; 193 AA.
AC Q6PHY8; Q802G5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Thioredoxin reductase-like selenoprotein T1b {ECO:0000305};
DE EC=1.8.1.9 {ECO:0000250|UniProtKB:Q1H5H1};
DE Flags: Precursor;
GN Name=selenot1b {ECO:0000305};
GN Synonyms=selt1b {ECO:0000312|EMBL:AAH53147.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AAH53147.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH53147.2};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAO86700.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-193, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney {ECO:0000269|PubMed:12915322};
RX PubMed=12915322; DOI=10.1016/s1567-133x(03)00054-1;
RA Thisse C., Degrave A., Kryukov G.V., Gladyshev V.N., Obrecht-Pflumio S.,
RA Krol A., Thisse B., Lescure A.;
RT "Spatial and temporal expression patterns of selenoprotein genes during
RT embryogenesis in zebrafish.";
RL Gene Expr. Patterns 3:525-532(2003).
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}.
CC -!- TISSUE SPECIFICITY: Widely expressed in the embryo. High level in
CC embryonic blood at 24 hours post-fertilization (hpf).
CC {ECO:0000269|PubMed:12915322}.
CC -!- PTM: May contain a selenide-sulfide bond between Cys-44 and Sec-47.
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=AAH53147.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO86700.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC053147; AAH53147.2; ALT_INIT; mRNA.
DR EMBL; AY216586; AAO86700.1; ALT_INIT; mRNA.
DR RefSeq; NP_840077.3; NM_178292.5.
DR STRING; 7955.ENSDARP00000120681; -.
DR PaxDb; Q6PHY8; -.
DR PRIDE; Q6PHY8; -.
DR Ensembl; ENSDART00000146972; ENSDARP00000120681; ENSDARG00000027595.
DR GeneID; 352921; -.
DR KEGG; dre:352921; -.
DR CTD; 352921; -.
DR ZFIN; ZDB-GENE-030411-1; selenot1b.
DR eggNOG; KOG3286; Eukaryota.
DR GeneTree; ENSGT00390000011725; -.
DR HOGENOM; CLU_113870_1_0_1; -.
DR InParanoid; Q6PHY8; -.
DR OrthoDB; 1542197at2759; -.
DR PhylomeDB; Q6PHY8; -.
DR TreeFam; TF321235; -.
DR PRO; PR:Q6PHY8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000027595; Expressed in mature ovarian follicle and 27 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..193
FT /note="Thioredoxin reductase-like selenoprotein T1b"
FT /evidence="ECO:0000255"
FT /id="PRO_0000252042"
FT NON_STD 47
FT /note="Selenocysteine"
FT /evidence="ECO:0000312|EMBL:AAH53147.2"
FT CROSSLNK 44..47
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000255"
FT CONFLICT 53
FT /note="F -> L (in Ref. 2; AAO86700)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="I -> F (in Ref. 2; AAO86700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 22386 MW; 6BFD3994A4324031 CRC64;
METRCLYLLL VCVLSVNHAT ADNGSIKKMK MQYTGFPLLK FQICVSUGYR RVFEEYTRVL
TQRYPDIRIE GENFLPQPLY RHIASFLSVF KLVVIGLIIL GKNPFTYLHI ETPGIWLWAQ
ENKIYACTMV FFLSNMIENQ CMSTGAFEVT LNDVPVWSKL QSGHLPSMQQ LVQILENEMK
LSVHMDSLPH RRA