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SELT_BOVIN
ID   SELT_BOVIN              Reviewed;         195 AA.
AC   A6QP01;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 66.
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};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Selenoprotein with thioredoxin reductase-like oxidoreductase
CC       activity (By similarity). Protects dopaminergic neurons against
CC       oxidative stress and cell death (By similarity). Involved in
CC       ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion
CC       (By similarity). Plays a role in fibroblast anchorage and redox
CC       regulation (By similarity). In gastric smooth muscle, modulates the
CC       contraction processes through the regulation of calcium release and
CC       MYLK activation (By similarity). In pancreatic islets, involved in the
CC       control of glucose homeostasis, contributes to prolonged ADCYAP1/PACAP-
CC       induced insulin secretion (By similarity).
CC       {ECO:0000250|UniProtKB:P62341, ECO:0000250|UniProtKB:P62342,
CC       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-46 and Sec-49.
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=AAI49083.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC149082; AAI49083.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001096573.2; NM_001103103.2.
DR   STRING; 9913.ENSBTAP00000042037; -.
DR   PaxDb; A6QP01; -.
DR   Ensembl; ENSBTAT00000044548; ENSBTAP00000042037; ENSBTAG00000031435.
DR   GeneID; 783831; -.
DR   KEGG; bta:783831; -.
DR   CTD; 51714; -.
DR   VEuPathDB; HostDB:ENSBTAG00000031435; -.
DR   VGNC; VGNC:53604; SELENOT.
DR   eggNOG; KOG3286; Eukaryota.
DR   GeneTree; ENSGT00390000011725; -.
DR   InParanoid; A6QP01; -.
DR   OMA; CISXGYR; -.
DR   OrthoDB; 1150650at2759; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000031435; Expressed in prostate gland and 106 other tissues.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..195
FT                   /note="Thioredoxin reductase-like selenoprotein T"
FT                   /id="PRO_0000318656"
FT   TRANSMEM        85..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_STD         49
FT                   /note="Selenocysteine"
FT   CROSSLNK        46..49
FT                   /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   195 AA;  22248 MW;  9F68E7A4C3A083AE CRC64;
     MRLLLLLLVA ASAVVRSDAS ANLGGVPGKR LKMQYATGPL LKFQICVSUG YRRVFEEYMR
     VISQRYPDIR IEGENYLPQP IYRHIASFLS VFKLVLIGLI IVGKDPFAFF GMQAPSIWQW
     GQENKVYACM MVFFLSNMIE NQCMSTGAFE ITLNDVPVWS KLESGHLPSM QQLVQILDNE
     MKLNVHMDSI PHHRS
 
 
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