SELT_RAT
ID SELT_RAT Reviewed; 195 AA.
AC Q1H5H1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Thioredoxin reductase-like selenoprotein T {ECO:0000305};
DE Short=SelT {ECO:0000250|UniProtKB:P62341};
DE EC=1.8.1.9 {ECO:0000269|PubMed:26866473};
DE Flags: Precursor;
GN Name=Selenot {ECO:0000312|RGD:1359128};
GN Synonyms=Selt {ECO:0000312|RGD:1359128};
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], SUBCELLULAR LOCATION, INDUCTION BY CAMP,
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND MUTAGENESIS OF SEC-49.
RX PubMed=18198219; DOI=10.1096/fj.06-075820;
RA Grumolato L., Ghzili H., Montero-Hadjadje M., Gasman S., Lesage J.,
RA Tanguy Y., Galas L., Ait-Ali D., Leprince J., Guerineau N.C.,
RA Elkahloun A.G., Fournier A., Vieau D., Vaudry H., Anouar Y.;
RT "Selenoprotein T is a PACAP-regulated gene involved in intracellular Ca2+
RT mobilization and neuroendocrine secretion.";
RL FASEB J. 22:1756-1768(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 46-CYS--SEC-49.
RX PubMed=26866473; DOI=10.1089/ars.2015.6478;
RA Boukhzar L., Hamieh A., Cartier D., Tanguy Y., Alsharif I., Castex M.,
RA Arabo A., El Hajji S., Bonnet J.J., Errami M., Falluel-Morel A.,
RA Chagraoui A., Lihrmann I., Anouar Y.;
RT "Selenoprotein T exerts an essential oxidoreductase activity that protects
RT dopaminergic neurons in mouse models of Parkinson's Disease.";
RL Antioxid. Redox Signal. 24:557-574(2016).
RN [3]
RP FUNCTION.
RX PubMed=26779623; DOI=10.1007/s12011-016-0620-8;
RA Li J.P., Zhou J.X., Wang Q., Gu G.Q., Yang S.J., Li C.Y., Qiu C.W.,
RA Deng G.Z., Guo M.Y.;
RT "Se enhances MLCK activation by regulating selenoprotein T (SelT) in the
RT gastric smooth muscle of rats.";
RL Biol. Trace Elem. Res. 173:116-125(2016).
CC -!- FUNCTION: Selenoprotein with thioredoxin reductase-like oxidoreductase
CC activity (PubMed:26866473). Protects dopaminergic neurons against
CC oxidative stress and cell death (By similarity). Involved in
CC ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion
CC (PubMed:18198219). 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 (PubMed:26779623). In pancreatic islets, involved in
CC the control of glucose homeostasis, contributes to prolonged
CC ADCYAP1/PACAP-induced insulin secretion (By similarity).
CC {ECO:0000250|UniProtKB:P62341, ECO:0000250|UniProtKB:P62342,
CC ECO:0000269|PubMed:18198219, ECO:0000269|PubMed:26779623,
CC ECO:0000269|PubMed:26866473}.
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:0000269|PubMed:26866473};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18198219}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, detected in all tissues tested.
CC {ECO:0000269|PubMed:18198219}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed as early as E7.
CC {ECO:0000269|PubMed:18198219}.
CC -!- INDUCTION: Rapidly induced by ADCYAP1/PACAP neuropeptide and cAMP.
CC {ECO:0000269|PubMed:18198219}.
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}.
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DR EMBL; AY995234; AAY45888.1; -; mRNA.
DR RefSeq; NP_001014275.2; NM_001014253.2.
DR STRING; 10116.ENSRNOP00000018248; -.
DR jPOST; Q1H5H1; -.
DR PaxDb; Q1H5H1; -.
DR PRIDE; Q1H5H1; -.
DR Ensembl; ENSRNOT00000018248; ENSRNOP00000018248; ENSRNOG00000013507.
DR GeneID; 365802; -.
DR KEGG; rno:365802; -.
DR UCSC; RGD:1359128; rat.
DR CTD; 51714; -.
DR RGD; 1359128; Selenot.
DR eggNOG; KOG3286; Eukaryota.
DR GeneTree; ENSGT00390000011725; -.
DR InParanoid; Q1H5H1; -.
DR OrthoDB; 1542197at2759; -.
DR PhylomeDB; Q1H5H1; -.
DR PRO; PR:Q1H5H1; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; ISS:UniProtKB.
DR GO; GO:0098869; P:cellular oxidant detoxification; IDA: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; IMP:UniProtKB.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; IMP: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 1: Evidence at protein 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 /evidence="ECO:0000255"
FT /id="PRO_0000252038"
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:18198219"
FT NON_STD 49
FT /note="Selenocysteine"
FT /evidence="ECO:0000312|EMBL:AAY45888.1"
FT CROSSLNK 46..49
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000255"
FT MUTAGEN 46..49
FT /note="CVSU->SVSS: Highly reduces thioredoxin reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:26779623"
FT MUTAGEN 49
FT /note="U->A: Abolishes regulation of calcium mobilization."
FT /evidence="ECO:0000269|PubMed:18198219"
SQ SEQUENCE 195 AA; 22292 MW; 4F2602FA6C1ABE96 CRC64;
MRLLLLLLVA ASAVVRSEAS ANLGGVPSKR LKMQYATGPL LKFQICVSUG YRRVFEEYMR
VISQRYPDIR IEGENYLPQP IYRHIASFLS VFKLVLIGLI IVGKDPFAFF GMQAPSIWQW
GQENKVYACM MVFFLSNMIE NQCMSTGAFE ITLNDVPVWS KLESGHLPSM QQLVQILDNE
MKLNVHMDSI PHHRS
