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Database: UniProt
Entry: Q9XVR3_CAEEL
LinkDB: Q9XVR3_CAEEL
Original site: Q9XVR3_CAEEL 
ID   Q9XVR3_CAEEL            Unreviewed;       178 AA.
AC   Q9XVR3;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE            EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN   ORFNames=C30H6.8 {ECO:0000313|EMBL:CAB02808.1,
GN   ECO:0000313|WormBase:C30H6.8}, CELE_C30H6.8
GN   {ECO:0000313|EMBL:CAB02808.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB02808.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAB02808.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB02808.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC         NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000696};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC         COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001346};
CC   -!- SIMILARITY: Belongs to the nucleoredoxin family.
CC       {ECO:0000256|ARBA:ARBA00025782}.
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DR   EMBL; BX284604; CAB02808.1; -; Genomic_DNA.
DR   PIR; T19587; T19587.
DR   RefSeq; NP_503101.1; NM_070700.4.
DR   AlphaFoldDB; Q9XVR3; -.
DR   SMR; Q9XVR3; -.
DR   STRING; 6239.C30H6.8.2; -.
DR   EPD; Q9XVR3; -.
DR   PaxDb; 6239-C30H6-8; -.
DR   PeptideAtlas; Q9XVR3; -.
DR   EnsemblMetazoa; C30H6.8.1; C30H6.8.1; WBGene00007825.
DR   UCSC; C30H6.8; c. elegans.
DR   AGR; WB:WBGene00007825; -.
DR   WormBase; C30H6.8; CE15652; WBGene00007825; -.
DR   eggNOG; KOG2501; Eukaryota.
DR   HOGENOM; CLU_116457_1_0_1; -.
DR   InParanoid; Q9XVR3; -.
DR   OMA; WCGSCKF; -.
DR   OrthoDB; 2874159at2759; -.
DR   PhylomeDB; Q9XVR3; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00007825; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   CDD; cd02964; TryX_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR13871; THIOREDOXIN; 1.
DR   PANTHER; PTHR13871:SF18; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13905; Thioredoxin_8; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:Q9XVR3,
KW   ECO:0007829|PeptideAtlas:Q9XVR3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT   DOMAIN          24..177
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   178 AA;  20138 MW;  E9C509554C1746ED CRC64;
     MSPSLLGSSF LRSASGNFTK FASIRNAHFL SSVPMKKRGV DGNLPKDYFE NKTVVVYFSA
     GWCGSCKFLT PKIKKFYNAV KESDAGKNLE IVWVSKDKEA AHQEEYYEKN LPDWPYIPFG
     DENIQKLSEK YKAVVIPVLK LVNSNGDVVH DRVRADVEAG IKADPVKTME EWKKLLNQ
//
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