ID   SELT2_CAEEL             Reviewed;         216 AA.
AC   Q19892;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Thioredoxin reductase-like selenoprotein T homolog selt-1.2 {ECO:0000305};
DE            EC=1.8.1.9 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=selt-1.2 {ECO:0000312|WormBase:F28H7.4};
GN   ORFNames=F28H7.4 {ECO:0000312|WormBase:F28H7.4};
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   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   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. {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: Cytoplasm {ECO:0000269|PubMed:28347729}.
CC       Perikaryon {ECO:0000269|PubMed:28347729}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:28347729}. Cell projection, axon
CC       {ECO:0000269|PubMed:28347729}.
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in AWB chemosensory amphid
CC       neurons. {ECO:0000269|PubMed:28347729}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from the L1 stage of larval development
CC       to adults. {ECO:0000269|PubMed:28347729}.
CC   -!- DISRUPTION PHENOTYPE: Viable with normal development, anatomy,
CC       motility, lifespan and brood size. Double knockouts with selt-1.1 are
CC       also viable with no visible phenotype. {ECO:0000269|PubMed:28347729}.
CC   -!- SIMILARITY: Belongs to the SelWTH family. SELT subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z72508; CAA96637.2; -; Genomic_DNA.
DR   PIR; T21526; T21526.
DR   RefSeq; NP_505741.2; NM_073340.2.
DR   AlphaFoldDB; Q19892; -.
DR   STRING; 6239.F28H7.4; -.
DR   PaxDb; Q19892; -.
DR   EnsemblMetazoa; F28H7.4.1; F28H7.4.1; WBGene00009238.
DR   GeneID; 185097; -.
DR   KEGG; cel:CELE_F28H7.4; -.
DR   UCSC; F28H7.4; c. elegans.
DR   CTD; 185097; -.
DR   WormBase; F28H7.4; CE36142; WBGene00009238; selt-1.2.
DR   eggNOG; KOG3286; Eukaryota.
DR   GeneTree; ENSGT00390000011725; -.
DR   HOGENOM; CLU_1278648_0_0_1; -.
DR   InParanoid; Q19892; -.
DR   OrthoDB; 1542197at2759; -.
DR   PhylomeDB; Q19892; -.
DR   PRO; PR:Q19892; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00009238; Expressed in adult organism and 2 other tissues.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
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   Cell projection; Cytoplasm; Disulfide bond; NADP; Oxidoreductase;
KW   Redox-active center; Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..216
FT                   /note="Thioredoxin reductase-like selenoprotein T homolog
FT                   selt-1.2"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000032294"
FT   DISULFID        77..80
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   216 AA;  24219 MW;  85764CE4E44BE638 CRC64;
     MSRSGAIIIG LFFIASIFDV FRAEKEPPAE DSRLEDYLSS ELETTAIPTV VNENSHSQDV
     VDSGFSKDLP KLTILYCVSC GYKQAFNQFY EFAKEKYPGL VIEGGNFSPD FWKGCLAQIV
     GVAKIGLIAI VITGSNPFEY IGFGYPQILQ TAHYNRFSYS LLVFMIGNLF ESTLSSTGAF
     EIFLGDKQIW SKISKERVPT QEEFLNLIDL QLKTIR