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P11232

- THIO_RAT

UniProt

P11232 - THIO_RAT

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Protein

Thioredoxin

Gene

Txn

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

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei26 – 261Deprotonates C-terminal active site CysBy similarity
Active sitei32 – 321NucleophileBy similarity
Sitei33 – 331Contributes to redox potential valueBy similarity
Sitei34 – 341Contributes to redox potential valueBy similarity
Active sitei35 – 351NucleophileBy similarity

GO - Molecular functioni

  1. enzyme binding Source: RGD
  2. protein disulfide oxidoreductase activity Source: InterPro
  3. thioredoxin-disulfide reductase activity Source: RGD

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. cellular response to antibiotic Source: RGD
  3. cellular response to drug Source: RGD
  4. cellular response to glucose stimulus Source: RGD
  5. cellular response to hyperoxia Source: RGD
  6. glycerol ether metabolic process Source: InterPro
  7. oxidation-reduction process Source: UniProtKB
  8. positive regulation of DNA binding Source: UniProtKB
  9. regulation of protein import into nucleus, translocation Source: UniProtKB
  10. regulation of transcription, DNA-templated Source: UniProtKB-KW
  11. response to activity Source: RGD
  12. response to axon injury Source: RGD
  13. response to dexamethasone Source: RGD
  14. response to drug Source: RGD
  15. response to radiation Source: UniProtKB
  16. response to selenium ion Source: RGD
  17. response to thyroxine Source: RGD
  18. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Electron transport, Transcription, Transcription regulation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin
Short name:
Trx
Gene namesi
Name:Txn
Synonyms:Txn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621157. Txn1.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. axon Source: RGD
  2. cytoplasm Source: RGD
  3. cytosol Source: RGD
  4. dendrite Source: RGD
  5. extracellular region Source: UniProtKB-KW
  6. neuronal cell body Source: RGD
  7. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 105104ThioredoxinPRO_0000120011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N6-acetyllysineBy similarity
Modified residuei8 – 81N6-succinyllysineBy similarity
Disulfide bondi32 ↔ 35Redox-activePROSITE-ProRule annotation
Modified residuei39 – 391N6-acetyllysineBy similarity
Modified residuei62 – 621S-nitrosocysteineBy similarity
Modified residuei69 – 691S-nitrosocysteineBy similarity
Modified residuei73 – 731S-nitrosocysteine; alternateBy similarity
Disulfide bondi73 – 73Interchain; alternateBy similarity
Modified residuei94 – 941N6-acetyllysine; alternateBy similarity
Modified residuei94 – 941N6-succinyllysine; alternateBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Disulfide bond, S-nitrosylation

Proteomic databases

PaxDbiP11232.
PRIDEiP11232.

Expressioni

Gene expression databases

GenevestigatoriP11232.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi250461. 1 interaction.
IntActiP11232. 2 interactions.
MINTiMINT-4571509.
STRINGi10116.ENSRNOP00000016447.

Structurei

3D structure databases

ProteinModelPortaliP11232.
SMRiP11232. Positions 1-104.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 105104ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000292977.
HOVERGENiHBG009243.
InParanoidiP11232.
KOiK03671.
OrthoDBiEOG7H4DX9.
PhylomeDBiP11232.
TreeFamiTF318932.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11232-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKLIESKEA FQEALAAAGD KLVVVDFSAT WCGPCKMIKP FFHSLCDKYS
60 70 80 90 100
NVVFLEVDVD DCQDVAADCE VKCMPTFQFY KKGQKVGEFS GANKEKLEAT

ITEFA
Length:105
Mass (Da):11,673
Last modified:January 23, 2007 - v2
Checksum:i3A39025935FD42DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14878 mRNA. Translation: CAA33019.1.
AF311055 mRNA. Translation: AAG49923.1.
BC058454 mRNA. Translation: AAH58454.1.
PIRiS04352.
RefSeqiNP_446252.1. NM_053800.3.
UniGeneiRn.29777.

Genome annotation databases

GeneIDi116484.
KEGGirno:116484.
UCSCiRGD:621157. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14878 mRNA. Translation: CAA33019.1 .
AF311055 mRNA. Translation: AAG49923.1 .
BC058454 mRNA. Translation: AAH58454.1 .
PIRi S04352.
RefSeqi NP_446252.1. NM_053800.3.
UniGenei Rn.29777.

3D structure databases

ProteinModelPortali P11232.
SMRi P11232. Positions 1-104.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 250461. 1 interaction.
IntActi P11232. 2 interactions.
MINTi MINT-4571509.
STRINGi 10116.ENSRNOP00000016447.

Proteomic databases

PaxDbi P11232.
PRIDEi P11232.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 116484.
KEGGi rno:116484.
UCSCi RGD:621157. rat.

Organism-specific databases

CTDi 22166.
RGDi 621157. Txn1.

Phylogenomic databases

eggNOGi COG0526.
HOGENOMi HOG000292977.
HOVERGENi HBG009243.
InParanoidi P11232.
KOi K03671.
OrthoDBi EOG7H4DX9.
PhylomeDBi P11232.
TreeFami TF318932.

Miscellaneous databases

NextBioi 619063.
PROi P11232.

Gene expression databases

Genevestigatori P11232.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
PANTHERi PTHR10438. PTHR10438. 1 hit.
Pfami PF00085. Thioredoxin. 1 hit.
[Graphical view ]
PIRSFi PIRSF000077. Thioredoxin. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTHIO_RAT
AccessioniPrimary (citable) accession number: P11232
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3