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Protein

Thioredoxin

Gene

Txn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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
ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).

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. peptide disulfide oxidoreductase activity Source: MGI
  2. poly(A) RNA binding Source: MGI
  3. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: MGI
  2. glycerol ether metabolic process Source: InterPro
  3. negative regulation of hydrogen peroxide-induced cell death Source: MGI
  4. negative regulation of protein export from nucleus Source: MGI
  5. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  6. oxidation-reduction process Source: UniProtKB
  7. positive regulation of DNA binding Source: UniProtKB
  8. positive regulation of peptidyl-serine phosphorylation Source: MGI
  9. regulation of protein import into nucleus, translocation Source: UniProtKB
  10. response to radiation Source: UniProtKB
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Electron transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
REACT_189141. Detoxification of Reactive Oxygen Species.
REACT_198644. The NLRP3 inflammasome.
REACT_238368. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin
Short name:
Trx
Alternative name(s):
ATL-derived factor
Short name:
ADF
Gene namesi
Name:Txn
Synonyms:Txn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:98874. 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. cytoplasm Source: MGI
  2. cytosol Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. mitochondrion Source: MGI
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 105104ThioredoxinPRO_0000120007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N6-acetyllysineBy similarity
Modified residuei8 – 81N6-succinyllysine1 Publication
Disulfide bondi32 ↔ 35Redox-activePROSITE-ProRule annotation
Modified residuei39 – 391N6-acetyllysine1 Publication
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; alternate1 Publication
Modified residuei94 – 941N6-succinyllysine; alternate1 Publication

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

MaxQBiP10639.
PaxDbiP10639.
PRIDEiP10639.

2D gel databases

SWISS-2DPAGEP10639.
UCD-2DPAGEP10639.

PTM databases

PhosphoSiteiP10639.

Expressioni

Gene expression databases

BgeeiP10639.
CleanExiMM_TXN1.
GenevestigatoriP10639.

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

BioGridi204389. 3 interactions.
IntActiP10639. 3 interactions.
MINTiMINT-1868937.

Structurei

3D structure databases

ProteinModelPortaliP10639.
SMRiP10639. Positions 1-103.
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.
GeneTreeiENSGT00530000063008.
HOGENOMiHOG000292977.
HOVERGENiHBG009243.
InParanoidiP10639.
KOiK03671.
OMAiMSEMING.
OrthoDBiEOG7H4DX9.
PhylomeDBiP10639.
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.

P10639-1 [UniParc]FASTAAdd to basket

« Hide

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

ITEYA
Length:105
Mass (Da):11,675
Last modified:January 23, 2007 - v3
Checksum:i3A2B925935F952DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001S → C in BAB25256 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18207.1.
PIRiJC4068. S04107.
RefSeqiNP_035790.1. NM_011660.3.
UniGeneiMm.260618.

Genome annotation databases

EnsembliENSMUST00000030051; ENSMUSP00000030051; ENSMUSG00000028367.
GeneIDi22166.
KEGGimmu:22166.
UCSCiuc008syp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18207.1.
PIRiJC4068. S04107.
RefSeqiNP_035790.1. NM_011660.3.
UniGeneiMm.260618.

3D structure databases

ProteinModelPortaliP10639.
SMRiP10639. Positions 1-103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204389. 3 interactions.
IntActiP10639. 3 interactions.
MINTiMINT-1868937.

PTM databases

PhosphoSiteiP10639.

2D gel databases

SWISS-2DPAGEP10639.
UCD-2DPAGEP10639.

Proteomic databases

MaxQBiP10639.
PaxDbiP10639.
PRIDEiP10639.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030051; ENSMUSP00000030051; ENSMUSG00000028367.
GeneIDi22166.
KEGGimmu:22166.
UCSCiuc008syp.1. mouse.

Organism-specific databases

CTDi22166.
MGIiMGI:98874. Txn1.

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00530000063008.
HOGENOMiHOG000292977.
HOVERGENiHBG009243.
InParanoidiP10639.
KOiK03671.
OMAiMSEMING.
OrthoDBiEOG7H4DX9.
PhylomeDBiP10639.
TreeFamiTF318932.

Enzyme and pathway databases

ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
REACT_189141. Detoxification of Reactive Oxygen Species.
REACT_198644. The NLRP3 inflammasome.
REACT_238368. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

NextBioi302106.
PROiP10639.
SOURCEiSearch...

Gene expression databases

BgeeiP10639.
CleanExiMM_TXN1.
GenevestigatoriP10639.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.

Entry informationi

Entry nameiTHIO_MOUSE
AccessioniPrimary (citable) accession number: P10639
Secondary accession number(s): Q52KC4, Q9D8R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.