[1]	NUCLEOTIDE SEQUENCE [MRNA]. Lee K.S., Xu L., Xu J.Y., Cheung P.Y.; "Cloning and sequencing of thioredoxin reductase gene from porcine reticulocyte."; Submitted (JUN-2000) 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

AF277894; AAF78791.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_999319.1; -.

UniGene

Ssc.15974

3D structure databases

HSSP

Q94655; 1ONF. [HSSP ENTRY / PDB]

SMR

Q9MYY8; 11-493.

ModBase

Q9MYY8.

Ontologies

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: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; FALSE_NEG.

Genome annotation databases

GeneID

397299; -.

KEGG

ssc:397299; -.

Phylogenomic databases

HOVERGEN

Q9MYY8; -.

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_0000067983`
`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).`

Sequence information

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

Molecular weight: 54904 Da [This is the MW of the unprocessed precursor]

CRC64: CFE9C9F51998FBB4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNGAEELPEM YDYDLIIIGG GSGGLAAAKE AARFNKRVMV LDFVTPTPLG TRWGLGGTCV 

        70         80         90        100        110        120 
NVSCIPKKLM HQAALLGQAL RDSRNYGWNV EETIKHDWER MTEAVQNHIG SLNWGYRVAL 

       130        140        150        160        170        180 
REKKVTYENA YGQFVGPHRI KATNNKGKEK IYSAEKFLIA TGERPRYLGI PGDKEYCISS 

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

       250        260        270        280        290        300 
EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV AQSTNSEEII EGEYNTVMLA 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

Q9MYY8 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