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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)DescriptionActionsGraphical viewLength
Active sitei472Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi42 – 59FADBy similarityAdd BLAST18

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 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
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi498U → S: Loss of activity. 1 Publication1
Mutagenesisi498Missing : Loss of activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL6035.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000679851 – 499Thioredoxin reductase 1, cytoplasmicAdd BLAST499

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi59 ↔ 64Redox-active1 Publication
Modified residuei68N6-succinyllysineBy similarity1
Modified residuei131PhosphotyrosineBy similarity1
Cross-linki497 ↔ 498Cysteinyl-selenocysteine (Cys-Sec)

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiO89049.
PeptideAtlasiO89049.
PRIDEiO89049.

PTM databases

iPTMnetiO89049.
PhosphoSitePlusiO89049.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi248626. 1 interactor.
STRINGi10116.ENSRNOP00000013612.

Chemistry databases

BindingDBiO89049.

Structurei

Secondary structure

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 18Combined sources7
Helixi22 – 33Combined sources12
Beta strandi38 – 41Combined sources4
Helixi57 – 62Combined sources6
Helixi64 – 83Combined sources20
Turni84 – 87Combined sources4
Helixi98 – 122Combined sources25
Beta strandi126 – 128Combined sources3
Beta strandi130 – 136Combined sources7
Beta strandi139 – 143Combined sources5
Beta strandi149 – 159Combined sources11
Beta strandi163 – 165Combined sources3
Beta strandi169 – 172Combined sources4
Helixi173 – 176Combined sources4
Helixi180 – 183Combined sources4
Beta strandi192 – 196Combined sources5
Helixi200 – 211Combined sources12
Beta strandi216 – 222Combined sources7
Helixi230 – 242Combined sources13
Beta strandi246 – 260Combined sources15
Beta strandi266 – 277Combined sources12
Beta strandi279 – 289Combined sources11
Beta strandi293 – 296Combined sources4
Beta strandi298 – 300Combined sources3
Helixi302 – 304Combined sources3
Turni311 – 313Combined sources3
Beta strandi329 – 331Combined sources3
Helixi333 – 335Combined sources3
Helixi343 – 358Combined sources16
Beta strandi372 – 374Combined sources3
Beta strandi376 – 378Combined sources3
Beta strandi380 – 384Combined sources5
Helixi387 – 394Combined sources8
Helixi396 – 398Combined sources3
Beta strandi399 – 406Combined sources8
Helixi409 – 411Combined sources3
Turni412 – 415Combined sources4
Beta strandi421 – 428Combined sources8
Helixi429 – 431Combined sources3
Beta strandi434 – 442Combined sources9
Helixi445 – 457Combined sources13
Helixi462 – 467Combined sources6
Helixi475 – 480Combined sources6
Turni486 – 489Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiO89049.
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 differs from that shown. Reason: Erroneous termination at position 498. Translated as Sec.Curated
The sequence AAH85726 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti52 – 53RW → NG in AAC35244 (PubMed:9535831).Curated2
Sequence conflicti52 – 53RW → NG in AAD43039 (PubMed:10333487).Curated2
Sequence conflicti52 – 53RW → NG in AAF32362 (Ref. 3) Curated2
Sequence conflicti426I → V in AAH85726 (PubMed:15489334).Curated1
Sequence conflicti451 – 455GFAAA → ALQP in AAD43039 (PubMed:10333487).Curated5
Sequence conflicti451 – 455GFAAA → ALQP in AAF32362 (Ref. 3) Curated5

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei498Selenocysteine1

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
PDB 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.
SMRiO89049.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248626. 1 interactor.
STRINGi10116.ENSRNOP00000013612.

Chemistry databases

BindingDBiO89049.
ChEMBLiCHEMBL6035.

PTM databases

iPTMnetiO89049.
PhosphoSitePlusiO89049.

Proteomic databases

PaxDbiO89049.
PeptideAtlasiO89049.
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...

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: November 2, 2016
This is version 143 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.