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Protein

Thioredoxin reductase-like selenoprotein T

Gene

SELENOT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Selenoprotein with thioredoxin reductase-like oxidoreductase activity (By similarity). Protects dopaminergic neurons against oxidative stress ans cell death (PubMed:26866473). Involved in ADCYAP1/PACAP-induced calcium mobilization and neuroendocrine secretion (By similarity). Plays a role in fibroblast anchorage and redox regulation (By similarity). In gastric smooth muscle, modulates the contraction processes through the regulation of calcium release and MYLK activation (By similarity). In pancreatic islets, involved in the control of glucose homeostasis, contributes to prolonged ADCYAP1/PACAP-induced insulin secretion (By similarity).By similarity1 Publication

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.By similarity

GO - Molecular functioni

  • selenium binding Source: UniProtKB
  • thioredoxin-disulfide reductase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandNADP

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase-like selenoprotein TCurated (EC:1.8.1.9By similarity)
Short name:
SelT1 Publication
Gene namesi
Name:SELENOT1 PublicationImported
Synonyms:SELT1 Publication
ORF Names:UNQ150/PRO176Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:18136. SELENOT.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei85 – 103HelicalSequence analysisAdd BLAST19

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

mRNA levels are increased more than 200-folds in the caudate putamen from Parkinson disease (PD) patients compared to control subjects. In conditional brain knockout mice, treatment with PD-inducing neurotoxins provoke rapid and severe parkinsonian-like motor defects.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49U → S: Increases ROS levels induced by neurotoxins. 1 Publication1

Organism-specific databases

DisGeNETi51714.
OpenTargetsiENSG00000198843.

Polymorphism and mutation databases

BioMutaiSELT.
DMDMi190358765.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000003229020 – 195Thioredoxin reductase-like selenoprotein TAdd BLAST176

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki46 ↔ 49Cysteinyl-selenocysteine (Cys-Sec)Sequence analysis

Post-translational modificationi

May contain a selenide-sulfide bond between Cys-46 and Sec-49. This bond is speculated to serve as redox-active pair (By similarity).By similarity

Proteomic databases

EPDiP62341.
MaxQBiP62341.
PaxDbiP62341.
PeptideAtlasiP62341.
PRIDEiP62341.

PTM databases

iPTMnetiP62341.
PhosphoSitePlusiP62341.
SwissPalmiP62341.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in the endocrine pancreas.1 Publication

Inductioni

Induced by Parkinson disease-inducing neurotoxins such as 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP).1 Publication

Gene expression databases

ExpressionAtlasiP62341. baseline and differential.

Organism-specific databases

HPAiHPA039780.

Interactioni

Protein-protein interaction databases

BioGridi119693. 16 interactors.
IntActiP62341. 1 interactor.
MINTiMINT-1404117.
STRINGi9606.ENSP00000418910.

Structurei

3D structure databases

ProteinModelPortaliP62341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3286. Eukaryota.
ENOG4111J49. LUCA.
GeneTreeiENSGT00390000011725.
HOGENOMiHOG000045222.
HOVERGENiHBG056808.
InParanoidiP62341.
PhylomeDBiP62341.

Family and domain databases

InterProiView protein in InterPro
IPR011893. Selenoprotein_Rdx-typ.
IPR019389. Selenoprotein_T.
IPR036249. Thioredoxin-like_sf.
PANTHERiPTHR13544. PTHR13544. 1 hit.
PfamiView protein in Pfam
PF10262. Rdx. 1 hit.
SUPFAMiSSF52833. SSF52833. 2 hits.
TIGRFAMsiTIGR02174. CXXU_selWTH. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLLLLLVA ASAMVRSEAS ANLGGVPSKR LKMQYATGPL LKFQICVSUG
60 70 80 90 100
YRRVFEEYMR VISQRYPDIR IEGENYLPQP IYRHIASFLS VFKLVLIGLI
110 120 130 140 150
IVGKDPFAFF GMQAPSIWQW GQENKVYACM MVFFLSNMIE NQCMSTGAFE
160 170 180 190
ITLNDVPVWS KLESGHLPSM QQLVQILDNE MKLNVHMDSI PHHRS
Length:195
Mass (Da):22,324
Last modified:February 26, 2008 - v2
Checksum:i5B7949FA7711AE9D
GO

Sequence cautioni

The sequence AAD20063 differs from that shown. Reason: Erroneous termination at position 49. Translated as Sec.Curated
The sequence AAF13696 differs from that shown. Reason: Frameshift at position 27.Curated
The sequence AAQ88462 differs from that shown. Reason: Erroneous termination at position 49. Translated as Sec.Curated
The sequence AAQ88463 differs from that shown. Reason: Erroneous termination at position 49. Translated as Sec.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16 – 18RSE → WSD in AAH09611 (PubMed:15489334).Curated3
Sequence conflicti26V → M in AAH09611 (PubMed:15489334).Curated1

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei49Selenocysteine1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195141 mRNA. Translation: AAF13696.1. Frameshift.
AF131856 mRNA. Translation: AAD20063.1. Sequence problems.
AY358095 mRNA. Translation: AAQ88462.1. Sequence problems.
AY358096 mRNA. Translation: AAQ88463.1. Sequence problems.
BC006012 mRNA. Translation: AAH06012.2.
BC008411 mRNA. Translation: AAH08411.2.
BC009556 mRNA. Translation: AAH09556.2.
BC009611 mRNA. Translation: AAH09611.2.
BC026350 mRNA. Translation: AAH26350.2.
BC036738 mRNA. Translation: AAH36738.3.
BC071699 mRNA. Translation: AAH71699.1.
CCDSiCCDS46936.1.
RefSeqiNP_057359.2. NM_016275.3.
UniGeneiHs.369052.

Genome annotation databases

EnsembliENST00000471696; ENSP00000418910; ENSG00000198843.
GeneIDi51714.
KEGGihsa:51714.

Keywords - Coding sequence diversityi

Selenocysteine

Similar proteinsi

Entry informationi

Entry nameiSELT_HUMAN
AccessioniPrimary (citable) accession number: P62341
Secondary accession number(s): O95904
, Q8IY80, Q9CZ45, Q9NZJ3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: February 26, 2008
Last modified: October 25, 2017
This is version 110 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families