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Thioredoxin reductase 3 (EC 1.8.1.9) (Thioredoxin and glutathione reductase) (Thioredoxin reductase TR2)

 TRXR3_MOUSE             Reviewed;         652 AA.
Q99MD6; Q9CZE5;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 3.
27-SEP-2017, entry version 119.
RecName: Full=Thioredoxin reductase 3;
EC=1.8.1.9;
AltName: Full=Thioredoxin and glutathione reductase;
AltName: Full=Thioredoxin reductase TR2;
Name=Txnrd3 {ECO:0000312|MGI:MGI:2386711};
Synonyms=Tgr {ECO:0000312|EMBL:AAK31172.1}, Trxr3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAK31172.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, DOMAIN, 3D-STRUCTURE MODELING, AND
SELENOCYSTEINE AT SEC-651.
PubMed=11259642; DOI=10.1073/pnas.051454398;
Sun Q.-A., Kirnarsky L., Sherman S., Gladyshev V.N.;
"Selenoprotein oxidoreductase with specificity for thioredoxin and
glutathione systems.";
Proc. Natl. Acad. Sci. U.S.A. 98:3673-3678(2001).
[2] {ECO:0000312|EMBL:BAB28419.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB28419.1};
TISSUE=Embryo {ECO:0000312|EMBL:BAB28419.1}, and
Thymus {ECO:0000312|EMBL:BAC37890.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000305, ECO:0000312|EMBL:AAH76605.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH76605.1};
TISSUE=Brain {ECO:0000312|EMBL:AAH76605.1};
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).
[4] {ECO:0000305}
PROTEIN SEQUENCE OF 191-202 AND 550-561, AND TISSUE SPECIFICITY.
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).
[5] {ECO:0000305}
DOMAIN, AND MUTAGENESIS OF SEC-651 AND 651-SEC-GLY-652.
PubMed=16262253; DOI=10.1021/bi051321w;
Sun Q.-A., Su D., Novoselov S.V., Carlson B.A., Hatfield D.L.,
Gladyshev V.N.;
"Reaction mechanism and regulation of mammalian
thioredoxin/glutathione reductase.";
Biochemistry 44:14528-14537(2005).
[6] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=15901730; DOI=10.1074/jbc.M503638200;
Su D., Novoselov S.V., Sun Q.-A., Moustafa M.E., Zhou Y., Oko R.,
Hatfield D.L., Gladyshev V.N.;
"Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in
disulfide bond formation and sperm maturation.";
J. Biol. Chem. 280:26491-26498(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Lung, Pancreas, 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]
NON-AUG INITIATOR START CODON, AND TISSUE SPECIFICITY.
PubMed=20018845; DOI=10.1074/jbc.M109.070532;
Gerashchenko M.V., Su D., Gladyshev V.N.;
"CUG start codon generates thioredoxin/glutathione reductase isoforms
in mouse testes.";
J. Biol. Chem. 285:4595-4602(2010).
[9]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-388, 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).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-34, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Displays thioredoxin reductase, glutaredoxin and
glutathione reductase activities. Catalyzes disulfide bond
isomerization. Promotes disulfide bond formation between GPX4 and
various sperm proteins and may play a role in sperm maturation by
promoting formation of sperm structural components.
{ECO:0000269|PubMed:11259642, ECO:0000269|PubMed:15901730}.
-!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
+ NADPH. {ECO:0000269|PubMed:11259642}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:O89049};
Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O89049};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14.7 uM for 5,5'-dithiobis(2-nitrobenzoic acid)
{ECO:0000269|PubMed:11259642};
KM=10.7 uM for NADPH {ECO:0000269|PubMed:11259642};
KM=3.0 uM for thioredoxin {ECO:0000269|PubMed:11259642};
KM=8.84 uM for oxidized glutathione
{ECO:0000269|PubMed:11259642};
KM=45.2 uM for beta-hydroxyethyl disulfide
{ECO:0000269|PubMed:11259642};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O89049}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11259642,
ECO:0000269|PubMed:15901730}. Nucleus
{ECO:0000269|PubMed:11259642, ECO:0000269|PubMed:15901730}.
Microsome {ECO:0000269|PubMed:11259642,
ECO:0000269|PubMed:15901730}. Endoplasmic reticulum. Note=Detected
in cytoplasm and nucleus in late spermatids.
{ECO:0000269|PubMed:11259642, ECO:0000269|PubMed:15901730}.
-!- TISSUE SPECIFICITY: Expressed preferentially in testis where it is
found in spermatids and spermatocytes but not in sperm. In
elongating spermatids, expressed at the site of mitochondrial
sheath formation. Low levels in other tissues including heart,
lung, liver, kidney, brain, muscle and prostate.
{ECO:0000269|PubMed:10455115, ECO:0000269|PubMed:15901730,
ECO:0000269|PubMed:20018845}.
-!- DEVELOPMENTAL STAGE: Accumulates in the testis after puberty. Not
detected in 20-day-old mice but highly expressed in testes of 7-
month-old mice. {ECO:0000269|PubMed:15901730}.
-!- DOMAIN: The N-terminal glutaredoxin domain does not contain the C-
X-X-C redox-active motif normally found in glutaredoxins but
activity may be mediated through a single cysteine. The C-terminal
Cys-Sec motif of one subunit of the homodimer may transfer
electrons from the thiol-disulfide center to the glutaredoxin
domain of the other subunit. {ECO:0000269|PubMed:11259642,
ECO:0000269|PubMed:16262253}.
-!- MISCELLANEOUS: The thioredoxin reductase active site is a redox-
active disulfide bond. The selenocysteine residue is also
essential for catalytic activity (By similarity).
{ECO:0000250|UniProtKB:Q16881}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-!- CAUTION: This sequence initiates at a CTG codon.
{ECO:0000305|PubMed:20018845}.
-!- SEQUENCE CAUTION:
Sequence=AAH76605.1; Type=Erroneous termination; Positions=651; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=AAH76605.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=AAK31172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB28419.1; Type=Erroneous termination; Positions=651; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=BAB28419.1; Type=Frameshift; Positions=29, 38; Evidence={ECO:0000305};
Sequence=BAB28419.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=BAC37890.1; Type=Erroneous termination; Positions=651; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=BAC37890.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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EMBL; AF349659; AAK31172.1; ALT_INIT; mRNA.
EMBL; AK012699; BAB28419.1; ALT_SEQ; mRNA.
EMBL; AK080362; BAC37890.1; ALT_SEQ; mRNA.
EMBL; BC076605; AAH76605.1; ALT_SEQ; mRNA.
RefSeq; NP_001171529.1; NM_001178058.1.
RefSeq; NP_694802.2; NM_153162.3.
UniGene; Mm.229332; -.
PDB; 2LV3; NMR; -; A=44-161.
PDBsum; 2LV3; -.
ProteinModelPortal; Q99MD6; -.
SMR; Q99MD6; -.
STRING; 10090.ENSMUSP00000000828; -.
iPTMnet; Q99MD6; -.
PhosphoSitePlus; Q99MD6; -.
MaxQB; Q99MD6; -.
PaxDb; Q99MD6; -.
PeptideAtlas; Q99MD6; -.
PRIDE; Q99MD6; -.
GeneID; 232223; -.
KEGG; mmu:232223; -.
UCSC; uc009cwj.1; mouse.
CTD; 114112; -.
MGI; MGI:2386711; Txnrd3.
eggNOG; KOG1752; Eukaryota.
eggNOG; KOG4716; Eukaryota.
eggNOG; COG1249; LUCA.
HOGENOM; HOG000276712; -.
HOVERGEN; HBG004959; -.
InParanoid; Q99MD6; -.
KO; K00384; -.
BRENDA; 1.8.1.B1; 3474.
PRO; PR:Q99MD6; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_TXNRD3; -.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:MGI.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0000305; P:response to oxygen radical; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 2.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR011899; Glutaredoxin_euk/vir.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
InterPro; IPR012336; Thioredoxin-like_fold.
InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
Pfam; PF00462; Glutaredoxin; 1.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR02180; GRX_euk; 1.
TIGRFAMs; TIGR01438; TGR; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Developmental protein;
Differentiation; Direct protein sequencing; Disulfide bond;
Electron transport; Endoplasmic reticulum; FAD; Flavoprotein;
Methylation; Microsome; NADP; Nucleus; Oxidoreductase; Phosphoprotein;
Redox-active center; Reference proteome; Selenocysteine;
Spermatogenesis; Transport.
CHAIN 1 652 Thioredoxin reductase 3.
/FTId=PRO_0000320696.
DOMAIN 65 165 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
NP_BIND 167 196 FAD. {ECO:0000250}.
ACT_SITE 625 625 Proton acceptor. {ECO:0000250}.
NON_STD 651 651 Selenocysteine.
MOD_RES 34 34 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 34 34 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:Q86VQ6}.
MOD_RES 388 388 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
DISULFID 212 217 Redox-active. {ECO:0000250}.
CROSSLNK 650 651 Cysteinyl-selenocysteine (Cys-Sec).
{ECO:0000250}.
MUTAGEN 651 652 Missing: Abolishes thioredoxin reductase,
glutaredoxin and gluthioine reductase
activities.
{ECO:0000269|PubMed:16262253}.
MUTAGEN 651 651 U->C: Thioredoxin reductase activity
reduced to 21%. Glutaredoxin activity
reduced to 14%. Glutathione reductase
activity reduced to 18%.
{ECO:0000269|PubMed:16262253}.
MUTAGEN 651 651 U->S: Abolishes thioredoxin reductase,
glutaredoxin and gluthioine reductase
activities.
{ECO:0000269|PubMed:16262253}.
CONFLICT 8 8 P -> R (in Ref. 2; BAB28419).
{ECO:0000305}.
CONFLICT 16 16 S -> W (in Ref. 2; BAB28419).
{ECO:0000305}.
HELIX 61 74 {ECO:0000244|PDB:2LV3}.
STRAND 75 81 {ECO:0000244|PDB:2LV3}.
TURN 86 89 {ECO:0000244|PDB:2LV3}.
HELIX 90 97 {ECO:0000244|PDB:2LV3}.
STRAND 103 106 {ECO:0000244|PDB:2LV3}.
TURN 107 109 {ECO:0000244|PDB:2LV3}.
HELIX 113 124 {ECO:0000244|PDB:2LV3}.
STRAND 126 128 {ECO:0000244|PDB:2LV3}.
STRAND 133 136 {ECO:0000244|PDB:2LV3}.
HELIX 144 151 {ECO:0000244|PDB:2LV3}.
HELIX 155 159 {ECO:0000244|PDB:2LV3}.
SEQUENCE 652 AA; 71319 MW; AC6342C64DDEC1BC CRC64;
MEKPPSPPPP PRAQTSPGLG KVGVLPNRRL GAVRGGLMSS PPGRRARLAS PGTSRPSSEA
REELRRRLRD LIEGNRVMIF SKSYCPHSTR VKELFSSLGV VYNILELDQV DDGASVQEVL
TEISNQKTVP NIFVNKVHVG GCDRTFQAHQ NGLLQKLLQD DSAHDYDLII IGGGSGGLSC
AKEAANLGKK VMVLDFVVPS PQGTTWGLGG TCVNVGCIPK KLMHQAALLG HALQDAKKYG
WEYNQQVKHN WEAMTEAIQS HIGSLNWGYR VTLREKGVTY VNSFGEFVDL HKIKATNKKG
QETFYTASKF VIATGERPRY LGIQGDKEYC ITSDDLFSLP YCPGCTLVVG ASYVGLECAG
FLAGLGLDVT VMVRSVLLRG FDQEMAEKVG SYLEQQGVKF QRKFTPILVQ QLEKGLPGKL
KVVAKSTEGP ETVEGIYNTV LLAIGRDSCT RKIGLEKIGV KINEKNGKIP VNDVEQTNVP
HVYAIGDILD GKPELTPVAI QAGKLLARRL FGVSLEKCDY INIPTTVFTP LEYGCCGLSE
EKAIEMYKKE NLEVYHTLFW PLEWTVAGRD NNTCYAKIIC NKFDNERVVG FHLLGPNAGE
ITQGFAAAMK CGLTKQLLDD TIGIHPTCGE VFTTLEITKS SGLDITQKGC UG


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E1123r ELISA Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T


 

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