THIO2_CAEEL
ID THIO2_CAEEL Reviewed; 145 AA.
AC Q17424;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable thioredoxin-2;
GN Name=trx-2; ORFNames=B0024.9;
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).
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyzes dithiol-disulfide exchange reactions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; Z71178; CAA94881.2; -; Genomic_DNA.
DR PIR; T18644; T18644.
DR RefSeq; NP_001256207.1; NM_001269278.1.
DR AlphaFoldDB; Q17424; -.
DR SMR; Q17424; -.
DR BioGRID; 44464; 1.
DR IntAct; Q17424; 1.
DR STRING; 6239.B0024.9a; -.
DR EPD; Q17424; -.
DR PaxDb; Q17424; -.
DR EnsemblMetazoa; B0024.9a.1; B0024.9a.1; WBGene00007099.
DR GeneID; 179434; -.
DR KEGG; cel:CELE_B0024.9; -.
DR UCSC; B0024.9; c. elegans.
DR CTD; 34281; -.
DR WormBase; B0024.9a; CE42941; WBGene00007099; trx-2.
DR eggNOG; KOG0910; Eukaryota.
DR GeneTree; ENSGT00530000064086; -.
DR HOGENOM; CLU_090389_11_1_1; -.
DR InParanoid; Q17424; -.
DR OMA; CTPCKAL; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q17424; -.
DR Reactome; R-CEL-1614558; Degradation of cysteine and homocysteine.
DR Reactome; R-CEL-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q17424; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007099; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q17424; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Electron transport; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..145
FT /note="Probable thioredoxin-2"
FT /id="PRO_0000120028"
FT DOMAIN 39..144
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 68
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 71
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 62
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 69
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 70
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 68..71
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 145 AA; 15702 MW; CB323515396BCD6C CRC64;
MQKALKLGSF FARSAISVKP TLATSKMTQL RHFSHGASVF DIDSVEDFTE KVIQSSVPVI
VDFHAEWCGP CQALGPRLEE KVNGRQGSVL LAKINVDHAG ELAMDYGISA VPTVFAFKNG
EKISGFSGVL DDEQLDDFIE DVLAA
