[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain cortex, and Kidney; The German cDNA consortium; Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: Thioredoxin + NADP⁺ = thioredoxin disulfide + NADPH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
MISCELLANEOUS: The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity (By similarity).
SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

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

CR860816; CAH92925.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR926483; CAI30275.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001127133.1; -.

3D structure databases

SMR

Q5NVA2; 10-493.

ModBase

Q5NVA2.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0016654;	Molecular function: oxidoreductase activity, acting on NADH or NADPH, disulfide as acceptor (inferred from electronic annotation from InterPro).
GO:0008430;	Molecular function: selenium binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004791;	Molecular function: thioredoxin-disulfide reductase activity (inferred from electronic annotation from EC).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
IPR006338; Reduct_Se.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

PANTHER

PTHR22912:SF23; Reduct_Se; 1.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01438; TGR; 1.

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

ProtoNet

Q5NVA2.

Genome annotation databases

GeneID

100174180; -.

Phylogenomic databases

HOVERGEN

Q5NVA2; -.

Other

UniRef

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

Keywords

Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Phosphoprotein; Redox-active center; Selenium; Selenocysteine.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 499`	`499`	`Thioredoxin reductase 1, cytoplasmic.`	`PRO_0000067984`
`NP_BIND`	`42 59`	`18`	`FAD (By similarity).`
`ACT_SITE`	`472 472`		`Proton acceptor (By similarity).`
`NON_STD`	`498 498`		`Selenocysteine.`
`MOD_RES`	`11 11`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`13 13`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`131 131`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`422 422`		`Phosphotyrosine (By similarity).`
`DISULFID`	`59 64`		`Redox-active (By similarity).`
`CROSSLNK`	`497 498`		`Cysteinyl-selenocysteine (Cys-Sec) (By similarity).`
`CONFLICT`	`56 56`		`G -> E (in Ref. 1; CAH92925).`
`CONFLICT`	`108 108`		`H -> R (in Ref. 1; CAI30275).`
`CONFLICT`	`254 254`		`I -> V (in Ref. 1; CAI30275).`
`CONFLICT`	`257 257`		`E -> G (in Ref. 1; CAH92925).`
`CONFLICT`	`411 411`		`W -> R (in Ref. 1; CAH92925).`
`CONFLICT`	`485 485`		`T -> A (in Ref. 1; CAI30275).`

Sequence information

Length: 499 AA [This is the length of the unprocessed precursor]

Molecular weight: 54751 Da [This is the MW of the unprocessed precursor]

CRC64: D0535BE1F2405DA7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNGPEDLPES YDYDLIIIGG GSGGLAAAKE AAQYGKKVMV LDFVTPTPLG TRWGLGGTCV 

        70         80         90        100        110        120 
NVGCIPKKLM HQAALLGQAL QDSRNYGWKV EETVKHDWDR MIEAVQNHIG SLNWGYRVAL 

       130        140        150        160        170        180 
REKKVVYENA YGQFIGPHRI KATNNKGKEK IYSAERFLIA TGERPRYLGI PGDKEYCISS 

       190        200        210        220        230        240 
DDLFSLPYCP GKTLIVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM 

       250        260        270        280        290        300 
EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV AQSTNSEEII EGEYNTVLLA IGRDACTRKI 

       310        320        330        340        350        360 
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEDKV ELTPVAIQAG RLLAQRLYAG 

       370        380        390        400        410        420 
STVKCDYENV PTTVFTPLEY GACGLSEEKA VEKFGEENIE VYHSYFWPLE WTIPSRDNNK 

       430        440        450        460        470        480 
CYAKIICNTK DNERVVGFHV LGPNAGEVTQ GFAAALKCGL TKKQLDSTIG IHPVCAEVFT 

       490 
TLSVTKRSGA SILQAGCUG

Q5NVA2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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