ID G3PA84_GASAC Unreviewed; 420 AA.
AC G3PA84;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Nucleoredoxin {ECO:0000256|ARBA:ARBA00026178};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000014508.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000014508.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000014508.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; G3PA84; -.
DR STRING; 69293.ENSGACP00000014508; -.
DR Ensembl; ENSGACT00000014534.1; ENSGACP00000014508.1; ENSGACG00000010966.1.
DR eggNOG; KOG2501; Eukaryota.
DR GeneTree; ENSGT00940000165363; -.
DR InParanoid; G3PA84; -.
DR OMA; NAPCRQF; -.
DR TreeFam; TF331873; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000010966; Expressed in testis and 9 other cell types or tissues.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR CDD; cd03009; TryX_like_TryX_NRX; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
DR PANTHER; PTHR46472; NUCLEOREDOXIN; 1.
DR PANTHER; PTHR46472:SF1; NUCLEOREDOXIN; 1.
DR Pfam; PF13905; Thioredoxin_8; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT DOMAIN 109..309
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 420 AA; 47755 MW; B8A524346D643CA6 CRC64;
MSEFLVSLLG ERLVDREKAE VDVQSAGAKL SLVGLFFGCS LNAPCKQFNG SLCEFYGRFK
KASEHKDKLE IVFVSSDQDQ KHWQDFLQEM PWPALPFKDR HKKMKLWNKY KVTSIPSLVF
VDATTGKVVC RNGLLVVRDD PKGLEFPWGP KPFAEVVAGP LLRNNRQTTD SSSLEGHYVG
VYFSAHWCPP CRSLTRVLVE TYRAVKESGQ KFEIVFVSAD RSEESFQQYF SEMPWLAVPY
SDEARRSRLN RLYGIQGIPT LILLDAEGHM ITRQGRVEVL NDPECRLFPW HPRPVLELSE
SNAVQLHEGP CLVLFVGSDA EEEGELEPAK ELIQPIAEKL MVKYKAKEEE MPLLFFVAGE
DDMSDSLRDY TNLPEAAPLL TILDMSARAK YVRDVEEITP AEVEQFVSDF LAEKLKPEPI
//
