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Thioredoxin reductase 2, mitochondrial (EC 1.8.1.9) (Thioredoxin reductase TR3)

 TRXR2_MOUSE             Reviewed;         524 AA.
Q9JLT4; Q6KG49; Q80VZ4; Q91YX4; Q9JHA7; Q9JMH5;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 4.
18-JUL-2018, entry version 157.
RecName: Full=Thioredoxin reductase 2, mitochondrial;
EC=1.8.1.9;
AltName: Full=Thioredoxin reductase TR3;
Flags: Precursor;
Name=Txnrd2; Synonyms=Trxr2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAD51323.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10500251; DOI=10.1016/S0167-4781(99)00129-3;
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] {ECO:0000305}
NUCLEOTIDE SEQUENCE (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
TISSUE=Thymocyte;
PubMed=10721726; DOI=10.1016/S0378-1119(99)00498-9;
Kawai H., Ota T., Suzuki F., Tatsuka M.;
"Molecular cloning of mouse thioredoxin reductases.";
Gene 242:321-330(2000).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 35-44;
65-76; 255-277 AND 341-373, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10455115; DOI=10.1074/jbc.274.35.24522;
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/cJ;
PubMed=12132591;
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;
PubMed=15489334; DOI=10.1101/gr.2596504;
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.
PubMed=11060283; DOI=10.1074/jbc.M004750200;
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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-175 AND LYS-329,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Maintains thioredoxin in a reduced state. Implicated in
the defenses against oxidative stress. May play a role in redox-
regulated cell signaling.
-!- FUNCTION: Involved in the control of reactive oxygen species
levels and the regulation of mitochondrial redox homeostasis (By
similarity). Maintains thioredoxin in a reduced state. May play a
role in redox-regulated cell signaling (By similarity).
{ECO:0000250|UniProtKB:Q9NNW7, ECO:0000250|UniProtKB:Q9Z0J5}.
-!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
+ NADPH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000255|RuleBase:RU000402, ECO:0000305};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P38816}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10721726}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9JLT4-1; Sequence=Displayed;
Name=2;
IsoId=Q9JLT4-2; Sequence=VSP_008293;
Name=3;
IsoId=Q9JLT4-3; Sequence=VSP_008294, VSP_008295;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9JLT4-4; Sequence=VSP_008296;
-!- TISSUE SPECIFICITY: Expressed in liver, heart, testis and kidney.
{ECO:0000269|PubMed:10455115, ECO:0000269|PubMed:10500251,
ECO:0000269|PubMed:10721726}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
The selenocysteine residue is also essential for catalytic
activity (By similarity). {ECO:0000250|UniProtKB:Q9ZOJ5}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF03359.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH52157.3; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAL90457.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAQ03230.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA86986.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF136399; AAF03359.1; ALT_INIT; mRNA.
EMBL; AF171053; AAD51323.1; -; mRNA.
EMBL; AB027566; BAA86986.2; ALT_INIT; mRNA.
EMBL; AF414359; AAL90457.1; ALT_INIT; Genomic_DNA.
EMBL; AF414356; AAL90457.1; JOINED; Genomic_DNA.
EMBL; AF414357; AAL90457.1; JOINED; Genomic_DNA.
EMBL; AF414358; AAL90457.1; JOINED; Genomic_DNA.
EMBL; AF412308; AAQ03230.1; ALT_INIT; mRNA.
EMBL; BC013688; AAH13688.1; -; mRNA.
EMBL; BC052157; AAH52157.3; ALT_INIT; mRNA.
RefSeq; NP_038739.2; NM_013711.3.
UniGene; Mm.390906; -.
PDB; 1ZDL; X-ray; 3.00 A; A=31-522.
PDB; 1ZKQ; X-ray; 2.60 A; A=31-522.
PDB; 3DGZ; X-ray; 2.25 A; A=34-521.
PDBsum; 1ZDL; -.
PDBsum; 1ZKQ; -.
PDBsum; 3DGZ; -.
ProteinModelPortal; Q9JLT4; -.
SMR; Q9JLT4; -.
IntAct; Q9JLT4; 4.
MINT; Q9JLT4; -.
STRING; 10090.ENSMUSP00000111269; -.
iPTMnet; Q9JLT4; -.
PhosphoSitePlus; Q9JLT4; -.
PaxDb; Q9JLT4; -.
PeptideAtlas; Q9JLT4; -.
PRIDE; Q9JLT4; -.
GeneID; 26462; -.
KEGG; mmu:26462; -.
UCSC; uc007ynx.1; mouse. [Q9JLT4-3]
UCSC; uc007yny.1; mouse. [Q9JLT4-1]
CTD; 10587; -.
MGI; MGI:1347023; Txnrd2.
eggNOG; KOG0405; Eukaryota.
eggNOG; COG1249; LUCA.
HOGENOM; HOG000276712; -.
HOVERGEN; HBG004959; -.
InParanoid; Q9JLT4; -.
KO; K22182; -.
OrthoDB; EOG091G03IU; -.
TreeFam; TF314782; -.
BRENDA; 1.8.1.9; 3474.
EvolutionaryTrace; Q9JLT4; -.
PRO; PR:Q9JLT4; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_TXNRD2; -.
Genevisible; Q9JLT4; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; ISS:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0000305; P:response to oxygen radical; TAS:UniProtKB.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 3.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 3.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01438; TGR; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
Mitochondrion; NADP; Oxidoreductase; Redox-active center;
Reference proteome; Selenocysteine; Transit peptide.
TRANSIT 1 34 Mitochondrion.
{ECO:0000269|PubMed:10455115}.
CHAIN 35 524 Thioredoxin reductase 2, mitochondrial.
/FTId=PRO_0000030289.
NP_BIND 41 70 FAD. {ECO:0000250}.
ACT_SITE 497 497 Proton acceptor. {ECO:0000250}.
NON_STD 523 523 Selenocysteine. {ECO:0000250}.
MOD_RES 79 79 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 175 175 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 329 329 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
DISULFID 86 91 Redox-active. {ECO:0000250}.
CROSSLNK 522 523 Cysteinyl-selenocysteine (Cys-Sec).
{ECO:0000250}.
VAR_SEQ 1 36 MVAAMVAALRGPSRRFRPRTRALTRGTRGAASAAGG -> M
EG (in isoform 2). {ECO:0000305}.
/FTId=VSP_008293.
VAR_SEQ 318 356 RVPETRTLNLEKAGISTNPKNQKIIVDAQEATSVPHIYA
-> KDAASHTDTVSSSRKPYFLGRRVFAFLPITSWILHSAG
S (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_008294.
VAR_SEQ 357 524 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_008295.
VAR_SEQ 395 425 Missing (in isoform 4).
{ECO:0000303|PubMed:12132591}.
/FTId=VSP_008296.
CONFLICT 4 6 AMV -> GRMW (in Ref. 1; AAF03359).
{ECO:0000305}.
STRAND 39 45 {ECO:0000244|PDB:3DGZ}.
HELIX 49 60 {ECO:0000244|PDB:3DGZ}.
STRAND 65 68 {ECO:0000244|PDB:3DGZ}.
HELIX 85 89 {ECO:0000244|PDB:3DGZ}.
HELIX 91 112 {ECO:0000244|PDB:3DGZ}.
HELIX 125 149 {ECO:0000244|PDB:3DGZ}.
STRAND 153 155 {ECO:0000244|PDB:3DGZ}.
STRAND 158 170 {ECO:0000244|PDB:3DGZ}.
STRAND 176 186 {ECO:0000244|PDB:3DGZ}.
STRAND 190 192 {ECO:0000244|PDB:3DGZ}.
HELIX 201 204 {ECO:0000244|PDB:3DGZ}.
HELIX 208 211 {ECO:0000244|PDB:3DGZ}.
STRAND 220 224 {ECO:0000244|PDB:3DGZ}.
HELIX 228 239 {ECO:0000244|PDB:3DGZ}.
STRAND 244 250 {ECO:0000244|PDB:3DGZ}.
TURN 252 255 {ECO:0000244|PDB:1ZDL}.
HELIX 258 270 {ECO:0000244|PDB:3DGZ}.
STRAND 274 277 {ECO:0000244|PDB:3DGZ}.
STRAND 279 286 {ECO:0000244|PDB:3DGZ}.
STRAND 292 298 {ECO:0000244|PDB:3DGZ}.
TURN 299 301 {ECO:0000244|PDB:3DGZ}.
STRAND 304 314 {ECO:0000244|PDB:3DGZ}.
STRAND 318 321 {ECO:0000244|PDB:3DGZ}.
HELIX 323 325 {ECO:0000244|PDB:3DGZ}.
HELIX 327 330 {ECO:0000244|PDB:3DGZ}.
STRAND 336 338 {ECO:0000244|PDB:3DGZ}.
STRAND 345 348 {ECO:0000244|PDB:1ZDL}.
STRAND 354 356 {ECO:0000244|PDB:3DGZ}.
HELIX 358 360 {ECO:0000244|PDB:3DGZ}.
STRAND 361 364 {ECO:0000244|PDB:1ZKQ}.
HELIX 368 383 {ECO:0000244|PDB:3DGZ}.
STRAND 397 399 {ECO:0000244|PDB:3DGZ}.
STRAND 401 409 {ECO:0000244|PDB:3DGZ}.
HELIX 412 419 {ECO:0000244|PDB:3DGZ}.
HELIX 421 423 {ECO:0000244|PDB:3DGZ}.
STRAND 424 430 {ECO:0000244|PDB:3DGZ}.
HELIX 434 438 {ECO:0000244|PDB:3DGZ}.
STRAND 447 455 {ECO:0000244|PDB:3DGZ}.
STRAND 459 467 {ECO:0000244|PDB:3DGZ}.
HELIX 470 482 {ECO:0000244|PDB:3DGZ}.
HELIX 487 491 {ECO:0000244|PDB:3DGZ}.
HELIX 502 505 {ECO:0000244|PDB:3DGZ}.
TURN 511 514 {ECO:0000244|PDB:3DGZ}.
SEQUENCE 524 AA; 56603 MW; 74D4713DC8EF6A80 CRC64;
MVAAMVAALR GPSRRFRPRT RALTRGTRGA ASAAGGQQSF DLLVIGGGSG GLACAKEAAQ
LGKKVAVADY VEPSPRGTKW GLGGTCVNVG CIPKKLMHQA ALLGGMIRDA HHYGWEVAQP
VQHNWKTMAE AVQNHVKSLN WGHRVQLQDR KVKYFNIKAS FVDEHTVRGV DKGGKATLLS
AEHIVIATGG RPRYPTQVKG ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI
GLDTTVMMRS IPLRGFDQQM SSLVTEHMES HGTQFLKGCV PSHIKKLPTN QLQVTWEDHA
SGKEDTGTFD TVLWAIGRVP ETRTLNLEKA GISTNPKNQK IIVDAQEATS VPHIYAIGDV
AEGRPELTPT AIKAGKLLAQ RLFGKSSTLM DYSNVPTTVF TPLEYGCVGL SEEEAVALHG
QEHVEVYHAY YKPLEFTVAD RDASQCYIKM VCMREPPQLV LGLHFLGPNA GEVTQGFALG
IKCGASYAQV MQTVGIHPTC SEEVVKLHIS KRSGLEPTVT GCUG


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