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   16-JUN-2009, entry version 35.
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;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   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
RT   inhibits 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
CC       Wnt signaling pathway. May function as a transcriptional
CC       regulator. May regulate phosphatase 2A.
CC   -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein
CC       disulfide + NAD(P)H.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Nucleus
CC       (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Depletion causes significant defects in head
CC       formation with absence of eye structures.
CC   -!- SIMILARITY: Belongs to the nucleoredoxin family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; BC074275; AAH74275.1; -; mRNA.
DR   RefSeq; NP_001086161.1; -.
DR   UniGene; Xl.12749; -.
DR   GeneID; 444590; -.
DR   KEGG; xla:444590; -.
DR   Xenbase; XB-FEAT-1001771; nxn.
DR   HOVERGEN; Q6GM16; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0047134; F:protein-disulfide reductase activity; IEA:EC.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR000866; Alkyl_hydroperoxide_Rdtase.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 2.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   ProDom; PD003679; Thioredoxin_like; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; FALSE_NEG.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Differentiation; NAD; Nucleus;
KW   Oxidoreductase; Wnt signaling pathway.
FT   CHAIN         1    414       Nucleoredoxin.
FT                                /FTId=PRO_0000332936.
FT   DOMAIN      131    305       Thioredoxin.
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
//