SELT1_CAEEL
ID SELT1_CAEEL Reviewed; 247 AA.
AC Q9U3N5; Q93327;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Thioredoxin reductase-like selenoprotein T homolog selt-1.1 {ECO:0000305};
DE EC=1.8.1.9 {ECO:0000305};
DE Flags: Precursor;
GN Name=selt-1.1 {ECO:0000312|WormBase:C35C5.3b};
GN ORFNames=C35C5.3 {ECO:0000312|WormBase:C35C5.3b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=28347729; DOI=10.1016/j.freeradbiomed.2017.03.021;
RA Romanelli-Cedrez L., Carrera I., Otero L., Miranda-Vizuete A., Mariotti M.,
RA Alkema M.J., Salinas G.;
RT "Selenoprotein T is required for pathogenic bacteria avoidance in
RT Caenorhabditis elegans.";
RL Free Radic. Biol. Med. 108:174-182(2017).
CC -!- FUNCTION: Probably has thioredoxin reductase-like oxidoreductase
CC activity. Plays a role in regulating the oxidative stress response, and
CC odorant and pathogenic bacteria avoidance behavior (PubMed:28347729).
CC {ECO:0000269|PubMed:28347729, ECO:0000305}.
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:0000305};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:28347729}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:C35C5.3b};
CC IsoId=Q9U3N5-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C35C5.3a};
CC IsoId=Q9U3N5-2; Sequence=VSP_006041;
CC -!- TISSUE SPECIFICITY: Broadly expressed in neurons of nervous system
CC including ADL, ASH, ASI, ASJ, ASK and AWB amphid sensilla neurons, in
CC epithelial cells including hypodermal, arcade, pharyngeal, vulval and
CC rectal cells, and in somatic muscle cells of the head, neck and body
CC wall, and non-striated pharyngeal muscles.
CC {ECO:0000269|PubMed:28347729}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from the pre-bean
CC embryonic stages to the adult stage. {ECO:0000269|PubMed:28347729}.
CC -!- DISRUPTION PHENOTYPE: Viable with normal development, anatomy,
CC motility, lifespan and brood size. Increased sensitivity to oxidative
CC stress induced by rotenone and impaired avoidance behavior in response
CC to the odorants 2-nonanone and 1-octanol and the pathogenic bacterium
CC S.marcescens. Double knockouts with selt-1.2 are also viable with no
CC visible phenotype. {ECO:0000269|PubMed:28347729}.
CC -!- SIMILARITY: Belongs to the SelWTH family. SELT subfamily.
CC {ECO:0000305}.
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DR EMBL; Z78417; CAB01692.2; -; Genomic_DNA.
DR EMBL; Z78417; CAB01684.2; -; Genomic_DNA.
DR PIR; T19747; T19747.
DR PIR; T19755; T19755.
DR RefSeq; NP_509929.2; NM_077528.3. [Q9U3N5-1]
DR RefSeq; NP_509930.2; NM_077529.2. [Q9U3N5-2]
DR AlphaFoldDB; Q9U3N5; -.
DR BioGRID; 46251; 19.
DR STRING; 6239.C35C5.3b; -.
DR EPD; Q9U3N5; -.
DR PaxDb; Q9U3N5; -.
DR PeptideAtlas; Q9U3N5; -.
DR EnsemblMetazoa; C35C5.3a.1; C35C5.3a.1; WBGene00007955. [Q9U3N5-2]
DR EnsemblMetazoa; C35C5.3b.1; C35C5.3b.1; WBGene00007955. [Q9U3N5-1]
DR GeneID; 181343; -.
DR KEGG; cel:CELE_C35C5.3; -.
DR UCSC; C35C5.3b; c. elegans. [Q9U3N5-1]
DR CTD; 181343; -.
DR WormBase; C35C5.3a; CE43224; WBGene00007955; selt-1.1. [Q9U3N5-2]
DR WormBase; C35C5.3b; CE43266; WBGene00007955; selt-1.1. [Q9U3N5-1]
DR eggNOG; KOG3286; Eukaryota.
DR GeneTree; ENSGT00390000011725; -.
DR HOGENOM; CLU_1278648_0_0_1; -.
DR InParanoid; Q9U3N5; -.
DR OMA; YKQAFDQ; -.
DR OrthoDB; 1212835at2759; -.
DR PhylomeDB; Q9U3N5; -.
DR PRO; PR:Q9U3N5; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00007955; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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 Alternative splicing; Disulfide bond; Endoplasmic reticulum; NADP;
KW Oxidoreductase; Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..247
FT /note="Thioredoxin reductase-like selenoprotein T homolog
FT selt-1.1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000032293"
FT DISULFID 92..95
FT /note="Redox-active"
FT /evidence="ECO:0000305"
FT VAR_SEQ 24..26
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_006041"
SQ SEQUENCE 247 AA; 27690 MW; 0D6DCDE23FA881EE CRC64;
MSRFGVFIIG VLFFMSVCDV LRTVSAEEHS HDENHVHEKD DFEAEFGDET DSQSFSQGTE
EDHIEVREQS SFVKPTAVHH AKDLPTLRIF YCVSCGYKQA FDQFTTFAKE KYPNMPIEGA
NFAPVLWKAY VAQALSFVKM AVLVLVLGGI NPFERFGLGY PQILQHAHGN KMSSCMLVFM
LGNLVEQSLI STGAFEVYLG NEQIWSKIES GRVPSPQEFM QLIDAQLAVL GKAPVNTESF
GEFQQTV
