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SELT_XENTR
ID   SELT_XENTR              Reviewed;         201 AA.
AC   Q6PBD1; Q28CY0;
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; Synonyms=selt {ECO:0000312|EMBL:AAH59764.1};
GN   ORFNames=TNeu015n05.1 {ECO:0000312|EMBL:CAJ82619.1},
GN   TTpA003b03.1 {ECO:0000312|EMBL:CAJ82896.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAJ82619.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula, and Tadpole;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305, ECO:0000312|EMBL:CAJ82619.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-201.
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH59764.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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-51 and Sec-54.
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=AAH59764.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAJ82619.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CR760355; CAJ82619.1; ALT_INIT; mRNA.
DR   EMBL; CR855814; CAJ82896.1; -; mRNA.
DR   EMBL; BC059764; AAH59764.1; ALT_INIT; mRNA.
DR   RefSeq; NP_988868.2; NM_203537.2.
DR   STRING; 8364.ENSXETP00000060967; -.
DR   PaxDb; Q6PBD1; -.
DR   DNASU; 394463; -.
DR   GeneID; 394463; -.
DR   KEGG; xtr:394463; -.
DR   CTD; 51714; -.
DR   Xenbase; XB-GENE-5780991; selenot.
DR   eggNOG; KOG3286; Eukaryota.
DR   HOGENOM; CLU_113870_2_0_1; -.
DR   InParanoid; Q6PBD1; -.
DR   OrthoDB; 1542197at2759; -.
DR   PhylomeDB; Q6PBD1; -.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000020094; Expressed in embryo and 27 other tissues.
DR   ExpressionAtlas; Q6PBD1; 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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..201
FT                   /note="Thioredoxin reductase-like selenoprotein T"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000252044"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_STD         54
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        51..54
FT                   /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        143
FT                   /note="M -> N (in Ref. 1; CAJ82896)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   201 AA;  22529 MW;  604B88EC17846F73 CRC64;
     MARSSGPLCL LLLGGLVAGI LSGASADGNG LPSKKLKMQY TAGPLLKFQI CVSUGYRRVF
     EDYMRVISQR YPDIRIEGEN YLPHPIYRNI ASFLSVFKLV LIGLIIAGKD PFAFFGMQAP
     SVWQWGQENK VYACMMVFFV SNMIENQCMS TGAFEITLND VPVWSKLESG HLPSVQQLVQ
     IIDNEMKLNV HMDAIPHHHR S
 
 
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