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Protein

Thioredoxin reductase 1, cytoplasmic

Gene

Txnrd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei472 – 4721Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 5918FADBy similarityAdd
BLAST

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: InterPro
  • mercury ion binding Source: RGD
  • NAD(P)H oxidase activity Source: RGD
  • protein homodimerization activity Source: RGD
  • selenate reductase activity Source: RGD
  • thioredoxin-disulfide reductase activity Source: RGD

GO - Biological processi

  • benzene-containing compound metabolic process Source: RGD
  • cell redox homeostasis Source: InterPro
  • cellular oxidant detoxification Source: GOC
  • cellular response to copper ion Source: RGD
  • cellular response to hyperoxia Source: RGD
  • glutathione metabolic process Source: RGD
  • halogen metabolic process Source: RGD
  • hydrogen peroxide catabolic process Source: RGD
  • methylmercury metabolic process Source: RGD
  • NADPH oxidation Source: RGD
  • placenta development Source: RGD
  • positive regulation of cell death Source: RGD
  • protein tetramerization Source: RGD
  • response to axon injury Source: RGD
  • response to drug Source: RGD
  • response to hyperoxia Source: RGD
  • response to oxidative stress Source: RGD
  • response to selenium ion Source: RGD
  • selenocysteine metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15194.
BRENDAi1.8.1.9. 5301.
SABIO-RKO89049.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 1, cytoplasmic (EC:1.8.1.9)
Short name:
TR
Alternative name(s):
NADPH-dependent thioredoxin reductase
Thioredoxin reductase TR1
Gene namesi
Name:Txnrd1
Synonyms:Trxr1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61959. Txnrd1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • neuronal cell body Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi498 – 4981U → S: Loss of activity. 1 Publication
Mutagenesisi498 – 4981Missing : Loss of activity. 1 Publication

Chemistry

ChEMBLiCHEMBL6035.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Thioredoxin reductase 1, cytoplasmicPRO_0000067985Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi59 ↔ 64Redox-active1 Publication
Modified residuei68 – 681N6-succinyllysineBy similarity
Modified residuei131 – 1311PhosphotyrosineBy similarity
Cross-linki497 ↔ 498Cysteinyl-selenocysteine (Cys-Sec)

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiO89049.
PRIDEiO89049.

PTM databases

iPTMnetiO89049.
PhosphoSiteiO89049.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi248626. 1 interaction.
STRINGi10116.ENSRNOP00000013612.

Chemistry

BindingDBiO89049.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187Combined sources
Helixi22 – 3312Combined sources
Beta strandi38 – 414Combined sources
Helixi57 – 626Combined sources
Helixi64 – 8320Combined sources
Turni84 – 874Combined sources
Helixi98 – 12225Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi130 – 1367Combined sources
Beta strandi139 – 1435Combined sources
Beta strandi149 – 15911Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi169 – 1724Combined sources
Helixi173 – 1764Combined sources
Helixi180 – 1834Combined sources
Beta strandi192 – 1965Combined sources
Helixi200 – 21112Combined sources
Beta strandi216 – 2227Combined sources
Helixi230 – 24213Combined sources
Beta strandi246 – 26015Combined sources
Beta strandi266 – 27712Combined sources
Beta strandi279 – 28911Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi298 – 3003Combined sources
Helixi302 – 3043Combined sources
Turni311 – 3133Combined sources
Beta strandi329 – 3313Combined sources
Helixi333 – 3353Combined sources
Helixi343 – 35816Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi376 – 3783Combined sources
Beta strandi380 – 3845Combined sources
Helixi387 – 3948Combined sources
Helixi396 – 3983Combined sources
Beta strandi399 – 4068Combined sources
Helixi409 – 4113Combined sources
Turni412 – 4154Combined sources
Beta strandi421 – 4288Combined sources
Helixi429 – 4313Combined sources
Beta strandi434 – 4429Combined sources
Helixi445 – 45713Combined sources
Helixi462 – 4676Combined sources
Helixi475 – 4806Combined sources
Turni486 – 4894Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6VX-ray3.00A/B/C/D/E/F1-497[»]
3EANX-ray2.75A/B/C/D/E/F1-499[»]
3EAOX-ray3.10A/B/C/D/E/F1-499[»]
4KPRX-ray2.40A/B/E/F1-497[»]
ProteinModelPortaliO89049.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO89049.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiO89049.
KOiK00384.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O89049-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDSKDAPKS YDFDLIIIGG GSGGLAAAKE AAKFDKKVMV LDFVTPTPLG
60 70 80 90 100
TRWGLGGTCV NVGCIPKKLM HQAALLGQAL KDSRNYGWKL EDTVKHDWEK
110 120 130 140 150
MTESVQNHIG SLNWGYRVAL REKKVVYENA YGKFIGPHKI MATNNKGKEK
160 170 180 190 200
VYSAERFLIA TGERPRYLGI PGDKEYCISS DDLFSLPYCP GKTLVVGASY
210 220 230 240 250
VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM EEHGIKFIRQ
260 270 280 290 300
FVPTKIEQIE AGTPGRLKVT AKSTNSEETI EDEFNTVLLA VGRDSCTRTI
310 320 330 340 350
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEGKL ELTPVAIQAG
360 370 380 390 400
RLLAQRLYGG STVKCDYDNV PTTVFTPLEY GCCGLSEEKA VEKFGEENIE
410 420 430 440 450
VYHSFFWPLE WTVPSRDNNK CYAKVICNLK DNERVVGFHV LGPNAGEVTQ
460 470 480 490
GFAAALKCGL TKQQLDSTIG IHPVCAEIFT TLSVTKRSGG DILQSGCUG
Length:499
Mass (Da):54,670
Last modified:November 16, 2011 - v5
Checksum:iB23E5B5E661B174E
GO

Sequence cautioni

The sequence AAD43039.1 differs from that shown. Reason: Erroneous termination at position 498. Translated as Sec.Curated
The sequence AAH85726.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 532RW → NG in AAC35244 (PubMed:9535831).Curated
Sequence conflicti52 – 532RW → NG in AAD43039 (PubMed:10333487).Curated
Sequence conflicti52 – 532RW → NG in AAF32362 (Ref. 3) Curated
Sequence conflicti426 – 4261I → V in AAH85726 (PubMed:15489334).Curated
Sequence conflicti451 – 4555GFAAA → ALQP in AAD43039 (PubMed:10333487).Curated
Sequence conflicti451 – 4555GFAAA → ALQP in AAF32362 (Ref. 3) Curated

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei498 – 4981Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63923 mRNA. Translation: AAC35244.2.
AF108213 mRNA. Translation: AAD43039.1. Sequence problems.
AF220760 mRNA. Translation: AAF32362.1.
AF220761 mRNA. Translation: AAF32363.1.
BC085726 mRNA. Translation: AAH85726.1. Different initiation.
RefSeqiNP_113802.2. NM_031614.2.
UniGeneiRn.67581.

Genome annotation databases

GeneIDi58819.
KEGGirno:58819.
UCSCiRGD:61959. rat.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63923 mRNA. Translation: AAC35244.2.
AF108213 mRNA. Translation: AAD43039.1. Sequence problems.
AF220760 mRNA. Translation: AAF32362.1.
AF220761 mRNA. Translation: AAF32363.1.
BC085726 mRNA. Translation: AAH85726.1. Different initiation.
RefSeqiNP_113802.2. NM_031614.2.
UniGeneiRn.67581.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6VX-ray3.00A/B/C/D/E/F1-497[»]
3EANX-ray2.75A/B/C/D/E/F1-499[»]
3EAOX-ray3.10A/B/C/D/E/F1-499[»]
4KPRX-ray2.40A/B/E/F1-497[»]
ProteinModelPortaliO89049.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248626. 1 interaction.
STRINGi10116.ENSRNOP00000013612.

Chemistry

BindingDBiO89049.
ChEMBLiCHEMBL6035.

PTM databases

iPTMnetiO89049.
PhosphoSiteiO89049.

Proteomic databases

PaxDbiO89049.
PRIDEiO89049.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi58819.
KEGGirno:58819.
UCSCiRGD:61959. rat.

Organism-specific databases

CTDi7296.
RGDi61959. Txnrd1.

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiO89049.
KOiK00384.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15194.
BRENDAi1.8.1.9. 5301.
SABIO-RKO89049.

Miscellaneous databases

EvolutionaryTraceiO89049.
PROiO89049.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue."
    Zhong L., Arner E.S.J., Ljung J., Aaslund F., Holmgren A.
    J. Biol. Chem. 273:8581-8591(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Neuroblastoma.
  2. "Functional expression of rat thioredoxin reductase: selenocysteine insertion sequence element is essential for the active enzyme."
    Fujiwara N., Fujii T., Fujii J., Taniguchi N.
    Biochem. J. 340:439-444(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SELENOCYSTEINE AT SEC-498.
    Tissue: Kidney and Liver.
  3. "Molecular cloning of thioredoxin reductase 1 from rat liver."
    Rundlof A., Arner E.S.J.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations."
    Zhong L., Holmgren A.
    J. Biol. Chem. 275:18121-18128(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, CHARACTERIZATION.
  6. "Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme."
    Sandalova T., Zhong L., Lindqvist Y., Holmgren A., Schneider G.
    Proc. Natl. Acad. Sci. U.S.A. 98:9533-9538(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF MUTANT CYS-498 IN COMPLEX WITH NADP, DISULFIDE BOND, HOMODIMERIZATION.

Entry informationi

Entry nameiTRXR1_RAT
AccessioniPrimary (citable) accession number: O89049
Secondary accession number(s): Q5U344
, Q9JKZ3, Q9JKZ4, Q9R1I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 16, 2011
Last modified: June 8, 2016
This is version 141 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.