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P11232 (THIO_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thioredoxin

Short name=Trx
Gene names
Name:Txn
Synonyms:Txn1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length105 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions By similarity. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity By similarity.

Subunit structure

Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity in a redox-dependent manner By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Secreted By similarity. Note: Secreted by a leaderless secretory pathway. Predominantly in the cytoplasm in non irradiated cells. Radiation induces translocation of TRX from the cytoplasm to the nucleus By similarity.

Post-translational modification

In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins By similarity.

Sequence similarities

Belongs to the thioredoxin family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Biological processElectron transport
Transcription
Transcription regulation
Transport
   Cellular componentCytoplasm
Nucleus
Secreted
   DomainRedox-active center
   Molecular functionActivator
   PTMAcetylation
Disulfide bond
S-nitrosylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

cellular response to antibiotic

Inferred from expression pattern PubMed 21184825. Source: RGD

cellular response to drug

Inferred from expression pattern PubMed 20453393. Source: RGD

cellular response to glucose stimulus

Inferred from expression pattern PubMed 20453393. Source: RGD

cellular response to hyperoxia

Inferred from expression pattern PubMed 21505996. Source: RGD

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation-reduction process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein import into nucleus, translocation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

response to activity

Inferred from expression pattern PubMed 20601738. Source: RGD

response to axon injury

Inferred from expression pattern PubMed 19833109. Source: RGD

response to dexamethasone

Inferred from expression pattern PubMed 20393169. Source: RGD

response to drug

Inferred from expression pattern PubMed 18790005. Source: RGD

response to radiation

Inferred from sequence or structural similarity. Source: UniProtKB

response to selenium ion

Inferred from expression pattern PubMed 15792362. Source: RGD

response to thyroxine

Inferred from expression pattern PubMed 20729758. Source: RGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentaxon

Inferred from direct assay PubMed 20620191. Source: RGD

cytoplasm

Inferred from direct assay PubMed 20620191. Source: RGD

cytosol

Inferred from direct assay PubMed 20536427. Source: RGD

dendrite

Inferred from direct assay PubMed 20620191. Source: RGD

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from direct assay PubMed 20620191. Source: RGD

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 20536427. Source: RGD

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

thioredoxin-disulfide reductase activity

Traceable author statement PubMed 12011048. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 105104Thioredoxin
PRO_0000120011

Regions

Domain2 – 105104Thioredoxin

Sites

Active site321Nucleophile By similarity
Active site351Nucleophile By similarity
Site261Deprotonates C-terminal active site Cys By similarity
Site331Contributes to redox potential value By similarity
Site341Contributes to redox potential value By similarity

Amino acid modifications

Modified residue31N6-acetyllysine By similarity
Modified residue81N6-succinyllysine By similarity
Modified residue391N6-acetyllysine By similarity
Modified residue621S-nitrosocysteine By similarity
Modified residue691S-nitrosocysteine By similarity
Modified residue731S-nitrosocysteine; alternate By similarity
Modified residue941N6-acetyllysine; alternate By similarity
Modified residue941N6-succinyllysine; alternate By similarity
Disulfide bond32 ↔ 35Redox-active By similarity
Disulfide bond73Interchain; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
P11232 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3A39025935FD42DA

FASTA10511,673
        10         20         30         40         50         60 
MVKLIESKEA FQEALAAAGD KLVVVDFSAT WCGPCKMIKP FFHSLCDKYS NVVFLEVDVD 

        70         80         90        100 
DCQDVAADCE VKCMPTFQFY KKGQKVGEFS GANKEKLEAT ITEFA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a cDNA encoding rat thioredoxin."
Tonissen K.F., Robins A.J., Wells J.R.E.
Nucleic Acids Res. 17:3973-3973(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Xie Z.H., Liu C.Z., He Y.H., Wang A.M., Ma C.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
Tissue: Pituitary.
[4]"Characterization of a thioredoxin-related surface protein."
Dean M.F., Martin H., Sansom P.A.
Biochem. J. 304:861-867(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Tissue: Glial cell.
[5]Lubec G., Diao W., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 9-21; 73-81 AND 86-94, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14878 mRNA. Translation: CAA33019.1.
AF311055 mRNA. Translation: AAG49923.1.
BC058454 mRNA. Translation: AAH58454.1.
PIRS04352.
RefSeqNP_446252.1. NM_053800.3.
UniGeneRn.29777.

3D structure databases

ProteinModelPortalP11232.
SMRP11232. Positions 1-104.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250461. 1 interaction.
IntActP11232. 2 interactions.
MINTMINT-4571509.
STRING10116.ENSRNOP00000016447.

Proteomic databases

PaxDbP11232.
PRIDEP11232.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID116484.
KEGGrno:116484.
UCSCRGD:621157. rat.

Organism-specific databases

CTD22166.
RGD621157. Txn1.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000292977.
HOVERGENHBG009243.
InParanoidP11232.
KOK03671.
OrthoDBEOG7H4DX9.
PhylomeDBP11232.
TreeFamTF318932.

Gene expression databases

GenevestigatorP11232.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERPTHR10438. PTHR10438. 1 hit.
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFPIRSF000077. Thioredoxin. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio619063.
PROP11232.

Entry information

Entry nameTHIO_RAT
AccessionPrimary (citable) accession number: P11232
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families