[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. TISSUE=Liver; DOI=10.1016/S0167-4781(99)00129-3; PubMed=10500251 [NCBI, ExPASy, EBI, Israel, Japan] Miranda-Vizuete A., Damdimopoulos A.E., Spyrou G.; "cDNA cloning, expression and chromosomal localization of the mouse mitochondrial thioredoxin reductase gene."; Biochim. Biophys. Acta 1447:113-118(1999).
[2]	NUCLEOTIDE SEQUENCE (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. TISSUE=Thymocyte; DOI=10.1016/S0378-1119(99)00498-9; PubMed=10721726 [NCBI, ExPASy, EBI, Israel, Japan] Kawai H., Ota T., Suzuki F., Tatsuka M.; "Molecular cloning of mouse thioredoxin reductases."; Gene 242:321-330(2000).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 35-44; 65-76; 255-277 AND 341-373, AND TISSUE SPECIFICITY. TISSUE=Liver; DOI=10.1074/jbc.274.35.24522; PubMed=10455115 [NCBI, ExPASy, EBI, Israel, Japan] Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L., Gladyshev V.N.; "Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases."; J. Biol. Chem. 274:24522-24530(1999).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 4), AND ALTERNATIVE SPLICING. STRAIN=BALB/c; PubMed=12132591 [NCBI, ExPASy, EBI, Israel, Japan] Miranda-Vizuete A., Spyrou G.; "Genomic organization and identification of a novel alternative splicing variant of mouse mitochondrial thioredoxin reductase (TrxR2) gene."; Mol. Cells 13:488-492(2002).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). STRAIN=FVB/N; TISSUE=Limb, and Mammary tumor; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	ALTERNATIVE SPLICING. DOI=10.1074/jbc.M004750200; PubMed=11060283 [NCBI, ExPASy, EBI, Israel, Japan] Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., Gladyshev V.N.; "Heterogeneity within animal thioredoxin reductases: evidence for alternative first exon splicing."; J. Biol. Chem. 276:3106-3114(2001).

Comments

FUNCTION: Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.
CATALYTIC ACTIVITY: Thioredoxin + NADP⁺ = thioredoxin disulfide + NADPH.
COFACTOR: FAD (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Mitochondrion.

ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q9JLT4-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q9JLT4-2
Features which should be applied to build the isoform sequence: VSP_008293.

Name	3
Isoform ID	Q9JLT4-3
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_008294, VSP_008295.

Name	4
Isoform ID	Q9JLT4-4
Features which should be applied to build the isoform sequence: VSP_008296.

TISSUE SPECIFICITY: Expressed in liver, heart, testis and kidney.
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

AF136399; AAF03359.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF171053; AAD51323.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB027566; BAA86986.2; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF414359; AAL90457.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF414356; AAL90457.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF414357; AAL90457.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF414358; AAL90457.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF412308; AAQ03230.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013688; AAH13688.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC052157; AAH52157.3; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_038739.2; -.

UniGene

Mm.390906

3D structure databases

PDB

1ZDL; X-ray; 3.00 A; A=31-524.	[ExPASy / RCSB / EBI]
1ZKQ; X-ray; 2.60 A; A=31-524.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1ZDL; -.
1ZKQ; -.

ModBase

Q9JLT4.

Protein-protein interaction databases

IntAct

Q9JLT4; -.

PTM databases

PhosphoSite

Q9JLT4; -.

Organism-specific databases

MGI

MGI:1347023; Txnrd2.

Gene expression databases

ArrayExpress

Q9JLT4; -.

CleanEx

MM_TXNRD2; -.

GermOnline

ENSMUSG00000075704; Mus musculus.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
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:0005515;	Molecular function: protein binding (inferred from physical interaction from MGI).
GO:0008430;	Molecular function: selenium binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004791;	Molecular function: thioredoxin-disulfide reductase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0007507;	Biological process: heart development (inferred from mutant phenotype from MGI).
GO:0030097;	Biological process: hemopoiesis (inferred from mutant phenotype from MGI).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0000305;	Biological process: response to oxygen radical (traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
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.
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.

Genome annotation databases

Ensembl

ENSMUSG00000075704; Mus musculus. [Contig view]

GeneID

26462; -.

KEGG

mmu:26462; -.

Phylogenomic databases

HOVERGEN

Q9JLT4; -.

Other

NextBio

304577; -.

SOURCE

Txnrd2; Mus musculus.

UniRef

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

Keywords

3D-structure; Alternative splicing; Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Redox-active center; Selenium; Selenocysteine; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 34`	`34`	`Mitochondrion.`
`CHAIN`	`35 524`	`490`	`Thioredoxin reductase 2, mitochondrial.`	`PRO_0000030289`
`NP_BIND`	`41 70`	`30`	`FAD (By similarity).`
`ACT_SITE`	`497 497`		`Proton acceptor (By similarity).`
`NON_STD`	`523 523`		`Selenocysteine (By similarity).`
`DISULFID`	`86 91`		`Redox-active (By similarity).`
`CROSSLNK`	`522 523`		`Cysteinyl-selenocysteine (Cys-Sec) (By similarity).`
`VAR_SEQ`	`1 36`		`MVAAMVAALRGPSRRFRPRTRALTRGTRGAASAAGG -> MEG (in isoform 2).`	`VSP_008293`
`VAR_SEQ`	`318 356`		`RVPETRTLNLEKAGISTNPKNQKIIVDAQEATSVPHIYA -> KDAASHTDTVSSSRKPYFLGRRVFAFLPITSWILHSAGS (in isoform 3).`	`VSP_008294`
`VAR_SEQ`	`357 524`		`Missing (in isoform 3).`	`VSP_008295`
`VAR_SEQ`	`395 425`		`Missing (in isoform 4).`	`VSP_008296`
`CONFLICT`	`4 6`		`AMV -> GRMW (in Ref. 1; AAF03359).`
`STRAND`	`41 45`	`5`
`HELIX`	`49 60`	`12`
`STRAND`	`65 68`	`4`
`HELIX`	`84 89`	`6`
`HELIX`	`91 112`	`22`
`HELIX`	`125 136`	`12`
`HELIX`	`137 139`	`3`
`HELIX`	`140 148`	`9`
`TURN`	`149 151`	`3`
`STRAND`	`159 161`	`3`
`STRAND`	`163 169`	`7`
`STRAND`	`182 186`	`5`
`STRAND`	`190 192`	`3`
`HELIX`	`201 204`	`4`
`HELIX`	`208 211`	`4`
`STRAND`	`220 224`	`5`
`HELIX`	`228 240`	`13`
`STRAND`	`243 246`	`4`
`TURN`	`252 255`	`4`
`HELIX`	`258 269`	`12`
`TURN`	`270 272`	`3`
`STRAND`	`279 286`	`8`
`STRAND`	`292 298`	`7`
`STRAND`	`301 303`	`3`
`STRAND`	`305 314`	`10`
`STRAND`	`318 320`	`3`
`HELIX`	`323 325`	`3`
`HELIX`	`327 329`	`3`
`STRAND`	`336 338`	`3`
`STRAND`	`345 348`	`4`
`STRAND`	`354 356`	`3`
`HELIX`	`369 383`	`15`
`STRAND`	`397 399`	`3`
`STRAND`	`401 409`	`9`
`HELIX`	`412 419`	`8`
`HELIX`	`421 423`	`3`
`STRAND`	`424 430`	`7`
`HELIX`	`434 438`	`5`
`STRAND`	`447 455`	`9`
`STRAND`	`459 467`	`9`
`HELIX`	`470 483`	`14`
`HELIX`	`487 491`	`5`
`HELIX`	`501 506`	`6`
`TURN`	`511 514`	`4`

Sequence information

Length: 524 AA [This is the length of the unprocessed precursor]

Molecular weight: 56603 Da [This is the MW of the unprocessed precursor]

CRC64: 74D4713DC8EF6A80 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVAAMVAALR GPSRRFRPRT RALTRGTRGA ASAAGGQQSF DLLVIGGGSG GLACAKEAAQ 

        70         80         90        100        110        120 
LGKKVAVADY VEPSPRGTKW GLGGTCVNVG CIPKKLMHQA ALLGGMIRDA HHYGWEVAQP 

       130        140        150        160        170        180 
VQHNWKTMAE AVQNHVKSLN WGHRVQLQDR KVKYFNIKAS FVDEHTVRGV DKGGKATLLS 

       190        200        210        220        230        240 
AEHIVIATGG RPRYPTQVKG ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI 

       250        260        270        280        290        300 
GLDTTVMMRS IPLRGFDQQM SSLVTEHMES HGTQFLKGCV PSHIKKLPTN QLQVTWEDHA 

       310        320        330        340        350        360 
SGKEDTGTFD TVLWAIGRVP ETRTLNLEKA GISTNPKNQK IIVDAQEATS VPHIYAIGDV 

       370        380        390        400        410        420 
AEGRPELTPT AIKAGKLLAQ RLFGKSSTLM DYSNVPTTVF TPLEYGCVGL SEEEAVALHG 

       430        440        450        460        470        480 
QEHVEVYHAY YKPLEFTVAD RDASQCYIKM VCMREPPQLV LGLHFLGPNA GEVTQGFALG 

       490        500        510        520 
IKCGASYAQV MQTVGIHPTC SEEVVKLHIS KRSGLEPTVT GCUG

Q9JLT4 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