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P10639 (THIO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Alternative name(s):
ATL-derived factor
Short name=ADF
Gene names
Name:Txn
Synonyms:Txn1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.

ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).

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. Ref.6

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
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from direct assay PubMed 18555775. Source: MGI

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

negative regulation of protein export from nucleus

Inferred from direct assay PubMed 18555775. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 18555775. Source: MGI

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

response to radiation

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 11213470. Source: MGI

cytosol

Inferred from direct assay PubMed 18555775. Source: MGI

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

nucleus

Inferred from direct assay PubMed 11213470PubMed 18555775. Source: MGI

   Molecular_functionpeptide disulfide oxidoreductase activity

Inferred from direct assay PubMed 18555775. Source: MGI

protein binding

Inferred from physical interaction PubMed 18555775. Source: MGI

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 105104Thioredoxin
PRO_0000120007

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 Ref.7
Modified residue391N6-acetyllysine Ref.7
Modified residue621S-nitrosocysteine By similarity
Modified residue691S-nitrosocysteine By similarity
Modified residue731S-nitrosocysteine; alternate By similarity
Modified residue941N6-acetyllysine; alternate Ref.7
Modified residue941N6-succinyllysine; alternate Ref.7
Disulfide bond32 ↔ 35Redox-active By similarity
Disulfide bond73Interchain; alternate By similarity

Experimental info

Sequence conflict1001S → C in BAB25256. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P10639 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3A2B925935F952DA

FASTA10511,675
        10         20         30         40         50         60 
MVKLIESKEA FQEALAAAGD KLVVVDFSAT WCGPCKMIKP FFHSLCDKYS NVVFLEVDVD 

        70         80         90        100 
DCQDVAADCE VKCMPTFQFY KKGQKVGEFS GANKEKLEAS ITEYA 

« Hide

References

« Hide 'large scale' references
[1]"ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction."
Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J., Brown N., Arai K., Yokota T., Wakasugi H., Yodoi J.
EMBO J. 8:757-764(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Erratum
Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J., Brown N., Arai K., Yokota T., Wakasugi H., Yodoi J.
EMBO J. 13:2244-2244(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Structure of the mouse thioredoxin-encoding gene and its processed pseudogene."
Matsui M., Taniguchi Y., Hirota K., Taketo M., Yodoi J.
Gene 152:165-171(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
Tissue: Liver.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Pancreas.
[5]"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].
Strain: C57BL/6J.
Tissue: Colon and Thymus.
[6]"Vitamin D3 up-regulated protein 1 mediates oxidative stress via suppressing the thioredoxin function."
Junn E., Han S.H., Im J.Y., Yang Y., Cho E.W., Um H.D., Kim D.K., Lee K.W., Han P.L., Rhee S.G., Choi I.
J. Immunol. 164:6287-6295(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TXNIP.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39 AND LYS-94, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-8 AND LYS-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast and Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77585 mRNA. Translation: CAA54688.1.
D21859 Genomic DNA. Translation: BAA04881.1.
AK007537 mRNA. Translation: BAB25096.1.
AK007790 mRNA. Translation: BAB25256.1.
BC010756 mRNA. Translation: AAH10756.1.
BC094415 mRNA. Translation: AAH94415.1.
CCDSCCDS18207.1.
PIRS04107. JC4068.
RefSeqNP_035790.1. NM_011660.3.
UniGeneMm.260618.

3D structure databases

ProteinModelPortalP10639.
SMRP10639. Positions 1-103.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204389. 3 interactions.
IntActP10639. 3 interactions.
MINTMINT-1868937.

PTM databases

PhosphoSiteP10639.

2D gel databases

SWISS-2DPAGEP10639.
UCD-2DPAGEP10639.

Proteomic databases

MaxQBP10639.
PaxDbP10639.
PRIDEP10639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030051; ENSMUSP00000030051; ENSMUSG00000028367.
GeneID22166.
KEGGmmu:22166.
UCSCuc008syp.1. mouse.

Organism-specific databases

CTD22166.
MGIMGI:98874. Txn1.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00530000063008.
HOGENOMHOG000292977.
HOVERGENHBG009243.
InParanoidP10639.
KOK03671.
OMACKMISPH.
OrthoDBEOG7H4DX9.
PhylomeDBP10639.
TreeFamTF318932.

Gene expression databases

BgeeP10639.
CleanExMM_TXN1.
GenevestigatorP10639.

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

NextBio302106.
PROP10639.
SOURCESearch...

Entry information

Entry nameTHIO_MOUSE
AccessionPrimary (citable) accession number: P10639
Secondary accession number(s): Q52KC4, Q9D8R0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 134 of the entry and version 3 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot