SELT_MOUSE
ID SELT_MOUSE Reviewed; 195 AA.
AC P62342; A2RTC6; O95904; Q8CHV4; Q9CZ45; Q9NZJ3;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
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:0000312|MGI:MGI:1916477};
GN Synonyms=Selt {ECO:0000312|MGI:MGI:1916477};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=19935881; DOI=10.1139/o09-064;
RA Sengupta A., Carlson B.A., Labunskyy V.M., Gladyshev V.N., Hatfield D.L.;
RT "Selenoprotein T deficiency alters cell adhesion and elevates selenoprotein
RT W expression in murine fibroblast cells.";
RL Biochem. Cell Biol. 87:953-961(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY ADCYAP1.
RX PubMed=23913443; DOI=10.1210/en.2013-1167;
RA Prevost G., Arabo A., Jian L., Quelennec E., Cartier D., Hassan S.,
RA Falluel-Morel A., Tanguy Y., Gargani S., Lihrmann I., Kerr-Conte J.,
RA Lefebvre H., Pattou F., Anouar Y.;
RT "The PACAP-regulated gene selenoprotein T is abundantly expressed in mouse
RT and human beta-cells and its targeted inactivation impairs glucose
RT tolerance.";
RL Endocrinology 154:3796-3806(2013).
RN [6]
RP FUNCTION, INDUCTION BY NEUROTOXINS, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
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).
CC -!- FUNCTION: Selenoprotein with thioredoxin reductase-like oxidoreductase
CC activity (By similarity). Protects dopaminergic neurons against
CC oxidative stress and cell death (PubMed:26866473). Involved in
CC ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion
CC (By similarity). Plays a role in fibroblast anchorage and redox
CC regulation (PubMed:19935881). 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 (PubMed:23913443).
CC {ECO:0000250|UniProtKB:Q1H5H1, ECO:0000269|PubMed:19935881,
CC ECO:0000269|PubMed:23913443, 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:0000250|UniProtKB:Q1H5H1};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23913443}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in the endocrine
CC pancreas (PubMed:23913443). Expressed at low levels in the adult brain
CC (PubMed:26866473). {ECO:0000269|PubMed:23913443,
CC ECO:0000269|PubMed:26866473}.
CC -!- INDUCTION: Rapidly induced by ADCYAP1/PACAP neuropeptide
CC (PubMed:23913443). In striatum neurons and astrocytes, induced by
CC Parkinson disease-inducing neurotoxins such as 1-methyl-4-phenyl-
CC 1,2,3,6-tetrahydropyridine (MPTP) or rotenone (PubMed:26866473).
CC {ECO:0000269|PubMed:23913443, ECO:0000269|PubMed:26866473}.
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 -!- DISRUPTION PHENOTYPE: Knockout embryos die before E8 (PubMed:26866473).
CC Male conditional pancreatic beta-cell knockout mice display impaired
CC glucose tolerance with an increased number of smaller islets compared
CC to wild-type littermates (PubMed:23913443). Brain conditional knockout
CC mice treated with Parkinson disease-inducing neurotoxins such as 1-
CC methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) rapidly show tremor
CC and absence of movement to die within 2h after treatment
CC (PubMed:26866473). {ECO:0000269|PubMed:23913443,
CC ECO:0000269|PubMed:26866473}.
CC -!- SIMILARITY: Belongs to the SelWTH family. Selenoprotein T subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19970.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH38867.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC55254.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC55259.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC55261.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK013022; BAC55254.1; ALT_INIT; mRNA.
DR EMBL; AK032838; BAC55259.1; ALT_INIT; mRNA.
DR EMBL; AK047958; BAC55261.1; ALT_INIT; mRNA.
DR EMBL; BC019970; AAH19970.1; ALT_INIT; mRNA.
DR EMBL; BC038867; AAH38867.2; ALT_INIT; mRNA.
DR EMBL; BC132453; AAI32454.2; -; mRNA.
DR EMBL; BC138424; AAI38425.1; -; mRNA.
DR CCDS; CCDS38437.1; -.
DR RefSeq; NP_001035486.2; NM_001040396.2.
DR BioGRID; 213304; 2.
DR STRING; 10090.ENSMUSP00000103557; -.
DR iPTMnet; P62342; -.
DR PhosphoSitePlus; P62342; -.
DR EPD; P62342; -.
DR jPOST; P62342; -.
DR MaxQB; P62342; -.
DR PaxDb; P62342; -.
DR PeptideAtlas; P62342; -.
DR PRIDE; P62342; -.
DR ProteomicsDB; 257119; -.
DR Antibodypedia; 48150; 67 antibodies from 15 providers.
DR Ensembl; ENSMUST00000107924; ENSMUSP00000103557; ENSMUSG00000075700.
DR GeneID; 69227; -.
DR KEGG; mmu:69227; -.
DR UCSC; uc008phx.2; mouse.
DR CTD; 51714; -.
DR MGI; MGI:1916477; Selenot.
DR VEuPathDB; HostDB:ENSMUSG00000075700; -.
DR eggNOG; KOG3286; Eukaryota.
DR GeneTree; ENSGT00390000011725; -.
DR HOGENOM; CLU_113870_1_0_1; -.
DR InParanoid; P62342; -.
DR OMA; CISXGYR; -.
DR OrthoDB; 1542197at2759; -.
DR PhylomeDB; P62342; -.
DR TreeFam; TF321235; -.
DR BioGRID-ORCS; 69227; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Selt; mouse.
DR PRO; PR:P62342; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P62342; protein.
DR Bgee; ENSMUSG00000075700; Expressed in olfactory epithelium and 254 other tissues.
DR Genevisible; P62342; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
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; IMP:UniProtKB.
DR GO; GO:0098869; P:cellular oxidant detoxification; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0031016; P:pancreas development; IMP:MGI.
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; IMP:MGI.
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 /id="PRO_0000032291"
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT NON_STD 49
FT /note="Selenocysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 46..49
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000255"
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
