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

 TRXR3_HUMAN             Reviewed;         643 AA.
Q86VQ6; Q6PIS8; Q9NNW6; Q9P101;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
29-MAY-2013, sequence version 4.
28-FEB-2018, entry version 147.
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|EMBL:AAH50032.1};
Synonyms=TGR {ECO:0000250|UniProtKB:Q99MD6},
TRXR3 {ECO:0000312|EMBL:AAD39929.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[2] {ECO:0000305, ECO:0000312|EMBL:AAH50032.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis {ECO:0000312|EMBL:AAH50032.1};
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).
[3] {ECO:0000305, ECO:0000312|EMBL:AAD51325.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 65-643, AND SELENOCYSTEINE AT SEC-642.
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] {ECO:0000305, ECO:0000312|EMBL:AAD39929.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 67-643.
Miranda-Vizuete A.;
"TrxR3, a novel human thioredoxin reductase.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[6]
PROBABLE NON-AUG INITIATOR START CODON.
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).
-!- 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 (By
similarity). {ECO:0000250|UniProtKB:Q99MD6}.
-!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
+ NADPH. {ECO:0000250|UniProtKB:Q99MD6}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000250|UniProtKB:O89049};
Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O89049};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O89049}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99MD6}.
Nucleus {ECO:0000250|UniProtKB:Q99MD6}. Microsome
{ECO:0000250|UniProtKB:Q99MD6}. Endoplasmic reticulum
{ECO:0000250}. Note=Detected in cytoplasm and nucleus in late
spermatids. {ECO:0000250|UniProtKB:Q99MD6}.
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:Q99MD6}.
-!- 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=AAH30028.1; Type=Erroneous termination; Positions=642; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=AAH30028.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=AAH50032.1; Type=Erroneous termination; Positions=642; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=AAH50032.1; 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; AC024558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030028; AAH30028.1; ALT_SEQ; mRNA.
EMBL; BC050032; AAH50032.1; ALT_SEQ; mRNA.
EMBL; AF171055; AAD51325.1; -; mRNA.
EMBL; AF133519; AAD39929.1; -; mRNA.
CCDS; CCDS77811.1; -.
RefSeq; NP_001166984.1; NM_001173513.1.
RefSeq; NP_443115.1; NM_052883.1.
UniGene; Hs.477475; -.
PDB; 3H8Q; X-ray; 2.21 A; A/B=51-156.
PDBsum; 3H8Q; -.
ProteinModelPortal; Q86VQ6; -.
SMR; Q86VQ6; -.
STRING; 9606.ENSP00000430031; -.
BindingDB; Q86VQ6; -.
ChEMBL; CHEMBL2096978; -.
iPTMnet; Q86VQ6; -.
PhosphoSitePlus; Q86VQ6; -.
DMDM; 510120859; -.
MaxQB; Q86VQ6; -.
PaxDb; Q86VQ6; -.
PeptideAtlas; Q86VQ6; -.
PRIDE; Q86VQ6; -.
Ensembl; ENST00000640433; ENSP00000492093; ENSG00000197763.
GeneID; 114112; -.
KEGG; hsa:114112; -.
CTD; 114112; -.
DisGeNET; 114112; -.
GeneCards; TXNRD3; -.
HGNC; HGNC:20667; TXNRD3.
HPA; HPA036109; -.
MIM; 606235; gene.
neXtProt; NX_Q86VQ6; -.
OpenTargets; ENSG00000197763; -.
PharmGKB; PA134920642; -.
eggNOG; KOG1752; Eukaryota.
eggNOG; KOG4716; Eukaryota.
eggNOG; COG1249; LUCA.
GeneTree; ENSGT00390000007578; -.
HOGENOM; HOG000276712; -.
HOVERGEN; HBG004959; -.
InParanoid; Q86VQ6; -.
KO; K22182; -.
BRENDA; 1.8.1.9; 2681.
ChiTaRS; TXNRD3; human.
EvolutionaryTrace; Q86VQ6; -.
GenomeRNAi; 114112; -.
PRO; PR:Q86VQ6; -.
Proteomes; UP000005640; Chromosome 3.
CleanEx; HS_TXNRD3; -.
ExpressionAtlas; Q86VQ6; baseline and differential.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0009055; F:electron transfer 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; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; -; 3.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
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; IPR036249; Thioredoxin-like_sf.
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; 3.
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; Disulfide bond; Electron transport;
Endoplasmic reticulum; FAD; Flavoprotein; Methylation; Microsome;
NADP; Nucleus; Oxidoreductase; Phosphoprotein; Redox-active center;
Reference proteome; Selenocysteine; Spermatogenesis; Transport.
CHAIN 1 643 Thioredoxin reductase 3.
/FTId=PRO_0000320695.
DOMAIN 56 156 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
NP_BIND 158 187 FAD. {ECO:0000250}.
ACT_SITE 616 616 Proton acceptor. {ECO:0000250}.
NON_STD 642 642 Selenocysteine.
MOD_RES 26 26 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q99MD6}.
MOD_RES 26 26 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q99MD6}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 379 379 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99MD6}.
DISULFID 203 208 Redox-active. {ECO:0000250}.
CROSSLNK 641 642 Cysteinyl-selenocysteine (Cys-Sec).
{ECO:0000250}.
CONFLICT 65 66 RS -> AE (in Ref. 3; AAD51325).
{ECO:0000305}.
CONFLICT 246 246 T -> I (in Ref. 2; AAH30028).
{ECO:0000305}.
CONFLICT 337 337 T -> P (in Ref. 4; AAD39929).
{ECO:0000305}.
HELIX 53 65 {ECO:0000244|PDB:3H8Q}.
STRAND 67 72 {ECO:0000244|PDB:3H8Q}.
HELIX 77 88 {ECO:0000244|PDB:3H8Q}.
STRAND 94 97 {ECO:0000244|PDB:3H8Q}.
TURN 98 100 {ECO:0000244|PDB:3H8Q}.
HELIX 104 115 {ECO:0000244|PDB:3H8Q}.
STRAND 122 125 {ECO:0000244|PDB:3H8Q}.
STRAND 128 132 {ECO:0000244|PDB:3H8Q}.
HELIX 133 142 {ECO:0000244|PDB:3H8Q}.
HELIX 144 150 {ECO:0000244|PDB:3H8Q}.
SEQUENCE 643 AA; 70683 MW; 6FB04128943A4017 CRC64;
MERSPPQSPG PGKAGDAPNR RSGHVRGARV LSPPGRRARL SSPGPSRSSE AREELRRHLV
GLIERSRVVI FSKSYCPHST RVKELFSSLG VECNVLELDQ VDDGARVQEV LSEITNQKTV
PNIFVNKVHV GGCDQTFQAY QSGLLQKLLQ EDLAYDYDLI IIGGGSGGLS CAKEAAILGK
KVMVLDFVVP SPQGTSWGLG GTCVNVGCIP KKLMHQAALL GQALCDSRKF GWEYNQQVRH
NWETMTKAIQ NHISSLNWGY RLSLREKAVA YVNSYGEFVE HHKIKATNKK GQETYYTAAQ
FVIATGERPR YLGIQGDKEY CITSDDLFSL PYCPGKTLVV GASYVALECA GFLAGFGLDV
TVMVRSILLR GFDQEMAEKV GSYMEQHGVK FLRKFIPVMV QQLEKGSPGK LKVLAKSTEG
TETIEGVYNT VLLAIGRDSC TRKIGLEKIG VKINEKSGKI PVNDVEQTNV PYVYAVGDIL
EDKPELTPVA IQSGKLLAQR LFGASLEKCD YINVPTTVFT PLEYGCCGLS EEKAIEVYKK
ENLEIYHTLF WPLEWTVAGR ENNTCYAKII CNKFDHDRVI GFHILGPNAG EVTQGFAAAM
KCGLTKQLLD DTIGIHPTCG EVFTTLEITK SSGLDITQKG CUG


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