Thioredoxin reductase 1, cytoplasmic - Rattus norvegicus (Rat)

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O89049 (TRXR1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Thioredoxin reductase 1, cytoplasmic
Short name=TR
EC=1.8.1.9

Alternative name(s):
NADPH-dependent thioredoxin reductase
Thioredoxin reductase TR1

Gene names

Name:	Txnrd1
Synonyms:	Trxr1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Thioredoxin + NADP⁺ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Homodimer. Ref.6
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Sequence caution	The sequence AAD43039.1 differs from that shown. Reason: Erroneous termination at position 498. Translated as Sec. The sequence AAH85726.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Selenocysteine
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NADPH oxidation Inferred from direct assay PubMed 19054767. Source: RGD benzene-containing compound metabolic process Inferred from direct assay PubMed 20345183. Source: RGD cell proliferation Inferred from electronic annotation. Source: Compara cell redox homeostasis Inferred from electronic annotation. Source: InterPro cellular response to copper ion Inferred from expression pattern PubMed 19781568. Source: RGD cellular response to hyperoxia Inferred from expression pattern PubMed 21505996. Source: RGD glutathione metabolic process Inferred from expression pattern PubMed 21161181. Source: RGD halogen metabolic process Inferred from expression pattern PubMed 21406454. Source: RGD hydrogen peroxide catabolic process Inferred from mutant phenotype Ref.5. Source: RGD mesoderm formation Inferred from electronic annotation. Source: Compara methylmercury metabolic process Inferred from expression pattern PubMed 21106535. Source: RGD placenta development Inferred from expression pattern PubMed 20393169. Source: RGD positive regulation of cell death Inferred from mutant phenotype PubMed 12574159. Source: RGD protein tetramerization Inferred from direct assay PubMed 19146949. Source: RGD response to axon injury Inferred from expression pattern PubMed 19833109. Source: RGD response to drug Inferred from expression pattern PubMed 19768707. Source: RGD response to selenium ion Inferred from expression pattern PubMed 15792362. Source: RGD selenocysteine metabolic process Inferred from mutant phenotype PubMed 10512699. Source: RGD
Cellular_component	cytosol Inferred from direct assay PubMed 9988709. Source: RGD mitochondrion Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from direct assay PubMed 20620191. Source: RGD nucleolus Inferred from electronic annotation. Source: Compara
Molecular_function	NAD(P)H oxidase activity Inferred from direct assay PubMed 16481328. Source: RGD NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro mercury ion binding Inferred from direct assay PubMed 20810785. Source: RGD protein homodimerization activity Inferred from direct assay PubMed 14607844. Source: RGD selenate reductase activity Inferred from direct assay PubMed 20810785. Source: RGD thioredoxin-disulfide reductase activity Inferred from direct assay PubMed 12435734. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 499

499

Thioredoxin reductase 1, cytoplasmic

PRO_0000067985

Regions

Nucleotide binding

42 – 59

FAD By similarity

Sites

Active site

472

Proton acceptor

Amino acid modifications

Non-standard residue

498

Selenocysteine

Modified residue

131

Phosphotyrosine By similarity

Disulfide bond

59 ↔ 64

Redox-active Ref.6

Cross-link

497 ↔ 498

Cysteinyl-selenocysteine (Cys-Sec)

Experimental info

Mutagenesis

498

U → S: Loss of activity. Ref.5

Mutagenesis

498

Missing: Loss of activity. Ref.5

Sequence conflict

52 – 53

RW → NG in AAC35244. Ref.1

Sequence conflict

52 – 53

RW → NG in AAD43039. Ref.2

Sequence conflict

52 – 53

RW → NG in AAF32362. Ref.3

Sequence conflict

426

I → V in AAH85726. Ref.4

Sequence conflict

451 – 455

GFAAA → ALQP in AAD43039. Ref.2

Sequence conflict

451 – 455

GFAAA → ALQP in AAF32362. Ref.3

Secondary structure

499

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

O89049 [UniParc].

Last modified November 16, 2011. Version 5.
Checksum: B23E5B5E661B174E
Show »

FASTA

499

54,670

        10         20         30         40         50         60 
MNDSKDAPKS YDFDLIIIGG GSGGLAAAKE AAKFDKKVMV LDFVTPTPLG TRWGLGGTCV 

        70         80         90        100        110        120 
NVGCIPKKLM HQAALLGQAL KDSRNYGWKL EDTVKHDWEK MTESVQNHIG SLNWGYRVAL 

       130        140        150        160        170        180 
REKKVVYENA YGKFIGPHKI MATNNKGKEK VYSAERFLIA TGERPRYLGI PGDKEYCISS 

       190        200        210        220        230        240 
DDLFSLPYCP GKTLVVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM 

       250        260        270        280        290        300 
EEHGIKFIRQ FVPTKIEQIE AGTPGRLKVT AKSTNSEETI EDEFNTVLLA VGRDSCTRTI 

       310        320        330        340        350        360 
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEGKL ELTPVAIQAG RLLAQRLYGG 

       370        380        390        400        410        420 
STVKCDYDNV PTTVFTPLEY GCCGLSEEKA VEKFGEENIE VYHSFFWPLE WTVPSRDNNK 

       430        440        450        460        470        480 
CYAKVICNLK DNERVVGFHV LGPNAGEVTQ GFAAALKCGL TKQQLDSTIG IHPVCAEIFT 

       490 
TLSVTKRSGG DILQSGCUG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00454559.

RefSeq

NP_113802.2. NM_031614.2.

UniGene

Rn.67581.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H6V	X-ray	3.00	A/B/C/D/E/F	1-499	[»]
3EAN	X-ray	2.75	A/B/C/D/E/F	1-499	[»]
3EAO	X-ray	3.10	A/B/C/D/E/F	1-499	[»]

ProteinModelPortal

O89049.

ModBase

Search...

PTM databases

PhosphoSite

O89049.

Proteomic databases

PaxDb

O89049.

PRIDE

O89049.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

58819.

KEGG

rno:58819.

UCSC

RGD:61959. rat.

Organism-specific databases

CTD

7296.

RGD

61959. Txnrd1.

Phylogenomic databases

eggNOG

COG1249.

HOGENOM

HOG000276712.

HOVERGEN

HBG004959.

InParanoid

Q5U344.

K00384.

OrthoDB

EOG4H463K.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-15194.

SABIO-RK

O89049.

Gene expression databases

ArrayExpress

O89049.

Genevestigator

O89049.

Family and domain databases

Gene3D

3.30.390.30. 1 hit.

InterPro

IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]

PANTHER

PTHR22912:SF23. PTHR22912:SF23. 1 hit.

Pfam

PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

SUPFAM

SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.

TIGRFAMs

TIGR01438. TGR. 1 hit.

PROSITE

PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O89049.

ChEMBL

CHEMBL6035.

EvolutionaryTrace

O89049.

NextBio

611360.

Entry information

Entry name

TRXR1_RAT

Accession

Primary (citable) accession number: O89049
Secondary accession number(s): Q5U344

Q9R1I3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	November 16, 2011
Last modified:	April 3, 2013
This is version 116 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents