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Thioredoxin reductase 1, cytoplasmic (TR) (EC 1.8.1.9) (NADPH-dependent thioredoxin reductase) (Thioredoxin reductase TR1)

 TRXR1_RAT               Reviewed;         499 AA.
O89049; Q5U344; Q9JKZ3; Q9JKZ4; Q9R1I3;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
16-NOV-2011, sequence version 5.
10-MAY-2017, entry version 146.
RecName: Full=Thioredoxin reductase 1, cytoplasmic;
Short=TR;
EC=1.8.1.9;
AltName: Full=NADPH-dependent thioredoxin reductase;
AltName: Full=Thioredoxin reductase TR1;
Name=Txnrd1; Synonyms=Trxr1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Neuroblastoma;
PubMed=9535831; DOI=10.1074/jbc.273.15.8581;
Zhong L., Arner E.S.J., Ljung J., Aaslund F., Holmgren A.;
"Rat and calf thioredoxin reductase are homologous to glutathione
reductase with a carboxyl-terminal elongation containing a conserved
catalytically active penultimate selenocysteine residue.";
J. Biol. Chem. 273:8581-8591(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SELENOCYSTEINE AT SEC-498.
TISSUE=Kidney, and Liver;
PubMed=10333487; DOI=10.1042/bj3400439;
Fujiwara N., Fujii T., Fujii J., Taniguchi N.;
"Functional expression of rat thioredoxin reductase: selenocysteine
insertion sequence element is essential for the active enzyme.";
Biochem. J. 340:439-444(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Rundlof A., Arner E.S.J.;
"Molecular cloning of thioredoxin reductase 1 from rat liver.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
PROTEIN SEQUENCE OF 1-20; 56-67; 101-116; 316-335; 365-384; 425-430;
435-459 AND 488-499, FUNCTION, MUTAGENESIS OF SEC-498, AND
CHARACTERIZATION.
PubMed=10849437; DOI=10.1074/jbc.M000690200;
Zhong L., Holmgren A.;
"Essential role of selenium in the catalytic activities of mammalian
thioredoxin reductase revealed by characterization of recombinant
enzymes with selenocysteine mutations.";
J. Biol. Chem. 275:18121-18128(2000).
[6]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT CYS-498 IN COMPLEX
WITH NADP, DISULFIDE BOND, AND HOMODIMERIZATION.
PubMed=11481439; DOI=10.1073/pnas.171178698;
Sandalova T., Zhong L., Lindqvist Y., Holmgren A., Schneider G.;
"Three-dimensional structure of a mammalian thioredoxin reductase:
implications for mechanism and evolution of a selenocysteine-dependent
enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 98:9533-9538(2001).
-!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
+ NADPH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD per subunit.;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11481439}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
The selenocysteine residue is also essential for catalytic
activity (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD43039.1; Type=Erroneous termination; Positions=498; Note=Translated as Sec.; Evidence={ECO:0000305};
Sequence=AAH85726.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U63923; AAC35244.2; -; mRNA.
EMBL; AF108213; AAD43039.1; ALT_SEQ; mRNA.
EMBL; AF220760; AAF32362.1; -; mRNA.
EMBL; AF220761; AAF32363.1; -; mRNA.
EMBL; BC085726; AAH85726.1; ALT_INIT; mRNA.
RefSeq; NP_113802.2; NM_031614.2.
UniGene; Rn.67581; -.
PDB; 1H6V; X-ray; 3.00 A; A/B/C/D/E/F=1-497.
PDB; 3EAN; X-ray; 2.75 A; A/B/C/D/E/F=1-499.
PDB; 3EAO; X-ray; 3.10 A; A/B/C/D/E/F=1-499.
PDB; 4KPR; X-ray; 2.40 A; A/B/E/F=1-497.
PDBsum; 1H6V; -.
PDBsum; 3EAN; -.
PDBsum; 3EAO; -.
PDBsum; 4KPR; -.
ProteinModelPortal; O89049; -.
SMR; O89049; -.
BioGrid; 248626; 1.
STRING; 10116.ENSRNOP00000013612; -.
BindingDB; O89049; -.
ChEMBL; CHEMBL6035; -.
iPTMnet; O89049; -.
PhosphoSitePlus; O89049; -.
PaxDb; O89049; -.
PeptideAtlas; O89049; -.
PRIDE; O89049; -.
GeneID; 58819; -.
KEGG; rno:58819; -.
UCSC; RGD:61959; rat.
CTD; 7296; -.
RGD; 61959; Txnrd1.
eggNOG; KOG0405; Eukaryota.
eggNOG; COG1249; LUCA.
HOGENOM; HOG000276712; -.
HOVERGEN; HBG004959; -.
InParanoid; O89049; -.
KO; K00384; -.
BioCyc; MetaCyc:MONOMER-15194; -.
BRENDA; 1.8.1.9; 5301.
SABIO-RK; O89049; -.
EvolutionaryTrace; O89049; -.
PRO; PR:O89049; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0045340; F:mercury ion binding; IDA:RGD.
GO; GO:0016174; F:NAD(P)H oxidase activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0033797; F:selenate reductase activity; IDA:RGD.
GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:RGD.
GO; GO:0042537; P:benzene-containing compound metabolic process; IDA:RGD.
GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
GO; GO:0071280; P:cellular response to copper ion; IEP:RGD.
GO; GO:0071455; P:cellular response to hyperoxia; IEP:RGD.
GO; GO:0070276; P:halogen metabolic process; IEP:RGD.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:RGD.
GO; GO:0070995; P:NADPH oxidation; IDA:RGD.
GO; GO:0001890; P:placenta development; IEP:RGD.
GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
GO; GO:0051262; P:protein tetramerization; IDA:RGD.
GO; GO:0048678; P:response to axon injury; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
GO; GO:0000305; P:response to oxygen radical; IBA:GO_Central.
GO; GO:0010269; P:response to selenium ion; IEP:RGD.
GO; GO:0016259; P:selenocysteine metabolic process; IMP:RGD.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 3.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
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.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01438; TGR; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
Phosphoprotein; Redox-active center; Reference proteome;
Selenocysteine.
CHAIN 1 499 Thioredoxin reductase 1, cytoplasmic.
/FTId=PRO_0000067985.
NP_BIND 42 59 FAD. {ECO:0000250}.
ACT_SITE 472 472 Proton acceptor.
NON_STD 498 498 Selenocysteine.
MOD_RES 68 68 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9JMH6}.
MOD_RES 131 131 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q16881}.
DISULFID 59 64 Redox-active.
{ECO:0000269|PubMed:11481439}.
CROSSLNK 497 498 Cysteinyl-selenocysteine (Cys-Sec).
MUTAGEN 498 498 U->S: Loss of activity.
{ECO:0000269|PubMed:10849437}.
MUTAGEN 498 498 Missing: Loss of activity.
{ECO:0000269|PubMed:10849437}.
CONFLICT 52 53 RW -> NG (in Ref. 1; AAC35244, 2;
AAD43039 and 3; AAF32362). {ECO:0000305}.
CONFLICT 426 426 I -> V (in Ref. 4; AAH85726).
{ECO:0000305}.
CONFLICT 451 455 GFAAA -> ALQP (in Ref. 2; AAD43039 and 3;
AAF32362). {ECO:0000305}.
STRAND 12 18 {ECO:0000244|PDB:4KPR}.
HELIX 22 33 {ECO:0000244|PDB:4KPR}.
STRAND 38 41 {ECO:0000244|PDB:4KPR}.
HELIX 57 62 {ECO:0000244|PDB:4KPR}.
HELIX 64 83 {ECO:0000244|PDB:4KPR}.
TURN 84 87 {ECO:0000244|PDB:4KPR}.
HELIX 98 122 {ECO:0000244|PDB:4KPR}.
STRAND 126 128 {ECO:0000244|PDB:4KPR}.
STRAND 130 136 {ECO:0000244|PDB:4KPR}.
STRAND 139 143 {ECO:0000244|PDB:4KPR}.
STRAND 149 159 {ECO:0000244|PDB:4KPR}.
STRAND 163 165 {ECO:0000244|PDB:4KPR}.
STRAND 169 172 {ECO:0000244|PDB:3EAO}.
HELIX 173 176 {ECO:0000244|PDB:4KPR}.
HELIX 180 183 {ECO:0000244|PDB:4KPR}.
STRAND 192 196 {ECO:0000244|PDB:4KPR}.
HELIX 200 211 {ECO:0000244|PDB:4KPR}.
STRAND 216 222 {ECO:0000244|PDB:4KPR}.
HELIX 230 242 {ECO:0000244|PDB:4KPR}.
STRAND 246 260 {ECO:0000244|PDB:4KPR}.
STRAND 266 277 {ECO:0000244|PDB:4KPR}.
STRAND 279 289 {ECO:0000244|PDB:4KPR}.
STRAND 293 296 {ECO:0000244|PDB:4KPR}.
STRAND 298 300 {ECO:0000244|PDB:4KPR}.
HELIX 302 304 {ECO:0000244|PDB:4KPR}.
TURN 311 313 {ECO:0000244|PDB:4KPR}.
STRAND 329 331 {ECO:0000244|PDB:4KPR}.
HELIX 333 335 {ECO:0000244|PDB:4KPR}.
HELIX 343 358 {ECO:0000244|PDB:4KPR}.
STRAND 372 374 {ECO:0000244|PDB:4KPR}.
STRAND 376 378 {ECO:0000244|PDB:4KPR}.
STRAND 380 384 {ECO:0000244|PDB:4KPR}.
HELIX 387 394 {ECO:0000244|PDB:4KPR}.
HELIX 396 398 {ECO:0000244|PDB:4KPR}.
STRAND 399 406 {ECO:0000244|PDB:4KPR}.
HELIX 409 411 {ECO:0000244|PDB:4KPR}.
TURN 412 415 {ECO:0000244|PDB:4KPR}.
STRAND 421 428 {ECO:0000244|PDB:4KPR}.
HELIX 429 431 {ECO:0000244|PDB:4KPR}.
STRAND 434 442 {ECO:0000244|PDB:4KPR}.
HELIX 445 457 {ECO:0000244|PDB:4KPR}.
HELIX 462 467 {ECO:0000244|PDB:4KPR}.
HELIX 475 480 {ECO:0000244|PDB:4KPR}.
TURN 486 489 {ECO:0000244|PDB:4KPR}.
SEQUENCE 499 AA; 54670 MW; B23E5B5E661B174E CRC64;
MNDSKDAPKS YDFDLIIIGG GSGGLAAAKE AAKFDKKVMV LDFVTPTPLG TRWGLGGTCV
NVGCIPKKLM HQAALLGQAL KDSRNYGWKL EDTVKHDWEK MTESVQNHIG SLNWGYRVAL
REKKVVYENA YGKFIGPHKI MATNNKGKEK VYSAERFLIA TGERPRYLGI PGDKEYCISS
DDLFSLPYCP GKTLVVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM
EEHGIKFIRQ FVPTKIEQIE AGTPGRLKVT AKSTNSEETI EDEFNTVLLA VGRDSCTRTI
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEGKL ELTPVAIQAG RLLAQRLYGG
STVKCDYDNV PTTVFTPLEY GCCGLSEEKA VEKFGEENIE VYHSFFWPLE WTVPSRDNNK
CYAKVICNLK DNERVVGFHV LGPNAGEVTQ GFAAALKCGL TKQQLDSTIG IHPVCAEIFT
TLSVTKRSGG DILQSGCUG


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