[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Eye; NIH - Xenopus Gene Collection (XGC) project; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[2]	FUNCTION. DOI=10.1038/ncb1405; PubMed=16604061 [NCBI, ExPASy, EBI, Israel, Japan] Funato Y., Michiue T., Asashima M., Miki H.; "The thioredoxin-related redox-regulating protein nucleoredoxin inhibits Wnt-beta-catenin signalling through dishevelled."; Nat. Cell Biol. 8:501-508(2006).

Comments

FUNCTION: Functions as a redox-dependent negative regulator of the Wnt signaling pathway. May function as a transcriptional regulator. May regulate phosphatase 2A.
CATALYTIC ACTIVITY: Protein dithiol + NAD(P)⁺ = protein disulfide + NAD(P)H.
SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Nucleus (By similarity).
MISCELLANEOUS: Depletion of nxn causes significant defects in head formation with absence of eye structures.
SIMILARITY: Belongs to the nucleoredoxin family.
SIMILARITY: Contains 1 thioredoxin domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BC074275; AAH74275.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001086161.1; -.

UniGene

Xl.12749

3D structure databases

ModBase

Q6GM16.

Organism-specific databases

Xenbase

XB-FEAT-1001771; nxn.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0016209;	Molecular function: antioxidant activity (inferred from electronic annotation from InterPro).
GO:0047134;	Molecular function: protein-disulfide reductase activity (inferred from electronic annotation from EC).
GO:0030154;	Biological process: cell differentiation (inferred from electronic annotation from UniProtKB-KW).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0007275;	Biological process: multicellular organismal development (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0016055;	Biological process: Wnt receptor signaling pathway (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000866; AhpC-TSA.
IPR006662; Thioredoxin-like.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.30.10; Thioredoxin_fold; 2.

Pfam

PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.

PRINTS

PR00421; THIOREDOXIN.

ProDom

PD003679; Thioredoxin_like; 2.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00194; THIOREDOXIN_1; FALSE_NEG.
PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

444590; -.

KEGG

xla:444590; -.

Phylogenomic databases

HOVERGEN

Q6GM16; -.

Other

ProtoNet

Q6GM16.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Developmental protein; Differentiation; NAD; Nucleus; Oxidoreductase; Wnt signaling pathway.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 414`	`414`	`Nucleoredoxin.`	`PRO_0000332936`
`DOMAIN`	`131 305`	`175`	`Thioredoxin.`

Sequence information

Length: 414 AA [This is the length of the unprocessed precursor]

Molecular weight: 46844 Da [This is the MW of the unprocessed precursor]

CRC64: 9990342C03078C1F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGPGLLVEL LGEKLVNSER EEADVQALGS RVSLIGLLFG CGMSAPCLQL LPGLKDFYCK 

        70         80         90        100        110        120 
TRDRLEIVFV SSDPDQKKWQ LFVKDMPWLA LPYQEKHRKL KLWNKFRISN IPSLIFIEAS 

       130        140        150        160        170        180 
TVKTVCRNGL LLVKDDPEGL EFPWGPKPFC EVIAGPLIRN NSQSQESSTL EGSYVGIYFS 

       190        200        210        220        230        240 
AYWCPPCRSL TRVLVESYRK IKESGQKFEI VLVSADRSEE SFKQYFSEMP WLAVPYSDEA 

       250        260        270        280        290        300 
RRSRLNRLYG IQGIPNLIIL DPKGEVITRQ GRVEVLRDID CKEFPWHPKP VVELTELNAV 

       310        320        330        340        350        360 
QLNEGPCLVL FVDSEDEGES EAAKQLIQPI AEKIIAQHKA KDEDAPLLFF VAGEDDMTDS 

       370        380        390        400        410 
LRDFTNLPEA APLLTILDMS ARAKYVMDVE EITPEIVQSF VTDFLAEKLK PEPI

Q6GM16 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools