ID Q9N3H9_CAEEL Unreviewed; 149 AA.
AC Q9N3H9;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN ORFNames=CELE_Y52E8A.3 {ECO:0000313|EMBL:CCD62413.1}, Y52E8A.3
GN {ECO:0000313|EMBL:CCD62413.1, ECO:0000313|WormBase:Y52E8A.3};
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:CCD62413.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD62413.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD62413.1,
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}.
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; BX284602; CCD62413.1; -; Genomic_DNA.
DR RefSeq; NP_494757.1; NM_062356.1.
DR AlphaFoldDB; Q9N3H9; -.
DR SMR; Q9N3H9; -.
DR DIP; DIP-25846N; -.
DR IntAct; Q9N3H9; 1.
DR STRING; 6239.Y52E8A.3.2; -.
DR EPD; Q9N3H9; -.
DR PaxDb; 6239-Y52E8A-3; -.
DR PeptideAtlas; Q9N3H9; -.
DR EnsemblMetazoa; Y52E8A.3.1; Y52E8A.3.1; WBGene00021796.
DR GeneID; 190187; -.
DR KEGG; cel:CELE_Y52E8A.3; -.
DR UCSC; Y52E8A.3; c. elegans.
DR AGR; WB:WBGene00021796; -.
DR WormBase; Y52E8A.3; CE25389; WBGene00021796; -.
DR eggNOG; KOG2501; Eukaryota.
DR HOGENOM; CLU_116457_1_0_1; -.
DR InParanoid; Q9N3H9; -.
DR OMA; QFYNEFK; -.
DR OrthoDB; 3073590at2759; -.
DR PhylomeDB; Q9N3H9; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00021796; Expressed in larva and 3 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; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR13871; THIOREDOXIN; 1.
DR PANTHER; PTHR13871:SF34; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:Q9N3H9,
KW ECO:0007829|PeptideAtlas:Q9N3H9};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 1..149
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 149 AA; 17359 MW; 9C7599D93C4E4CB2 CRC64;
MPQFLKGVTL ENREGDELPA EEHLKGKIIG LYFSASWCPP CRAFTPKLKE FFEEIKKTHP
EFEIIFVSRD RNSSDLVTYF KEHQGEWTYI PFGSDKIMSL MQKYEVKTIP AMRIVNDQGE
VIVQDARTEI QNKGENVEGL WAEWMALIK
//
