NXN_DANRE
ID NXN_DANRE Reviewed; 418 AA.
AC Q503L9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Nucleoredoxin;
DE EC=1.8.1.8;
GN Name=nxn; ORFNames=zgc:110449;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a redox-dependent negative regulator of the Wnt
CC signaling pathway. {ECO:0000250}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P97346}. Nucleus {ECO:0000250|UniProtKB:P97346}.
CC -!- SIMILARITY: Belongs to the nucleoredoxin family. {ECO:0000305}.
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DR EMBL; BC095273; AAH95273.1; -; mRNA.
DR RefSeq; NP_001018431.1; NM_001020595.1.
DR AlphaFoldDB; Q503L9; -.
DR STRING; 7955.ENSDARP00000037350; -.
DR PaxDb; Q503L9; -.
DR GeneID; 553621; -.
DR KEGG; dre:553621; -.
DR CTD; 64359; -.
DR ZFIN; ZDB-GENE-050522-75; nxn.
DR eggNOG; KOG2501; Eukaryota.
DR InParanoid; Q503L9; -.
DR OrthoDB; 1350271at2759; -.
DR PhylomeDB; Q503L9; -.
DR PRO; PR:Q503L9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0072359; P:circulatory system development; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd03009; TryX_like_TryX_NRX; 1.
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 Pfam; PF13905; Thioredoxin_8; 2.
DR SUPFAM; SSF52833; SSF52833; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Differentiation; NAD; Nucleus;
KW Oxidoreductase; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..418
FT /note="Nucleoredoxin"
FT /id="PRO_0000332935"
FT DOMAIN 109..309
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 418 AA; 47410 MW; 42EA5F582152A88D CRC64;
MSEFLVNLLG ERLVNGEKAE VDVQALGSRL SLLGLYFGCS LNGPCKQFNA SLTEFYSKFK
KSSEHKDKLE IVFISSDQDQ KQWQDFLQEM QWPALPFKDR HKKMKLWNKY KVTSIPSLVF
IDAATGKVVC RNGLLVVRDD PKGLEFPWGP KPFAEVVSGP LLRNNRQTTD STALEGSYVG
VYFSAHWCPP CRSLTRVLVE SYRKVKETGQ KFEIVFVSAD RSEESFTQYF SEMPWLAVPY
SDEARRSRLN RLYGIQGIPT LILLDTEGHM ITRQGRVEIL NDPDCGLFPW HPRPVLELSE
SNAVQLHEGP CLVLFVDAEE EGELDPAKEL IQPIAEKIMA KYKAKEEETP LLFFVAGEDD
MSDSLRDYTN LPEAAPLLTI LDMSARAKYV KDVEEITPAV VEQFVSGFLA EKLKPEPI