ID   NXN_XENLA               Reviewed;         414 AA.
AC   Q6GM16;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Nucleoredoxin;
DE            EC=1.8.1.8;
GN   Name=nxn;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16604061; DOI=10.1038/ncb1405;
RA   Funato Y., Michiue T., Asashima M., Miki H.;
RT   "The thioredoxin-related redox-regulating protein nucleoredoxin inhibits
RT   Wnt-beta-catenin signalling through dishevelled.";
RL   Nat. Cell Biol. 8:501-508(2006).
CC   -!- FUNCTION: Functions as a redox-dependent negative regulator of the Wnt
CC       signaling pathway. {ECO:0000269|PubMed:16604061}.
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   -!- DISRUPTION PHENOTYPE: Depletion causes significant defects in head
CC       formation with absence of eye structures.
CC       {ECO:0000269|PubMed:16604061}.
CC   -!- SIMILARITY: Belongs to the nucleoredoxin family. {ECO:0000305}.
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DR   EMBL; BC074275; AAH74275.1; -; mRNA.
DR   RefSeq; NP_001086161.1; NM_001092692.1.
DR   AlphaFoldDB; Q6GM16; -.
DR   SMR; Q6GM16; -.
DR   DNASU; 444590; -.
DR   GeneID; 444590; -.
DR   KEGG; xla:444590; -.
DR   CTD; 444590; -.
DR   Xenbase; XB-GENE-1001776; nxn.S.
DR   OMA; EIIYIPM; -.
DR   OrthoDB; 1350271at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 444590; Expressed in liver and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:InterPro.
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; cd03071; PDI_b'_NRX; 1.
DR   CDD; cd03009; TryX_like_TryX_NRX; 1.
DR   InterPro; IPR041861; NRX_PDI_b.
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..414
FT                   /note="Nucleoredoxin"
FT                   /id="PRO_0000332936"
FT   DOMAIN          131..305
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   414 AA;  46844 MW;  9990342C03078C1F CRC64;
     MSGPGLLVEL LGEKLVNSER EEADVQALGS RVSLIGLLFG CGMSAPCLQL LPGLKDFYCK
     TRDRLEIVFV SSDPDQKKWQ LFVKDMPWLA LPYQEKHRKL KLWNKFRISN IPSLIFIEAS
     TVKTVCRNGL LLVKDDPEGL EFPWGPKPFC EVIAGPLIRN NSQSQESSTL EGSYVGIYFS
     AYWCPPCRSL TRVLVESYRK IKESGQKFEI VLVSADRSEE SFKQYFSEMP WLAVPYSDEA
     RRSRLNRLYG IQGIPNLIIL DPKGEVITRQ GRVEVLRDID CKEFPWHPKP VVELTELNAV
     QLNEGPCLVL FVDSEDEGES EAAKQLIQPI AEKIIAQHKA KDEDAPLLFF VAGEDDMTDS
     LRDFTNLPEA APLLTILDMS ARAKYVMDVE EITPEIVQSF VTDFLAEKLK PEPI