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P97493 (THIOM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. 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, mitochondrial

Short name=MTRX
Short name=Mt-Trx
Alternative name(s):
Thioredoxin-2
Gene names
Name:Txn2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length166 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has an anti-apoptotic function and plays an important role in the regulation of mitochondrial membrane potential By similarity. Possesses a dithiol-reducing activity. Ref.5

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the thioredoxin family.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentMitochondrion
   DomainRedox-active center
Transit peptide
   PTMAcetylation
Disulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

cellular response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to hormone

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentdendrite

Inferred from electronic annotation. Source: Ensembl

mitochondrion

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

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5959Mitochondrion By similarity
Chain60 – 166107Thioredoxin, mitochondrial
PRO_0000034151

Regions

Domain61 – 166106Thioredoxin

Sites

Active site901Nucleophile By similarity
Active site931Nucleophile By similarity
Site841Deprotonates C-terminal active site Cys By similarity
Site911Contributes to redox potential value By similarity
Site921Contributes to redox potential value By similarity

Amino acid modifications

Modified residue1521N6-acetyllysine; alternate By similarity
Modified residue1521N6-succinyllysine; alternate Ref.6
Disulfide bond90 ↔ 93Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
P97493 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: C9A803DF571F3A7D

FASTA16618,255
        10         20         30         40         50         60 
MAQRLLLGRF LTSVISRKPP QGVWASLTSK TLQTPQYNAG GLTVMPSPAR TVHTTRVCLT 

        70         80         90        100        110        120 
TFNVQDGPDF QDRVVNSETP VVVDFHAQWC GPCKILGPRL EKMVAKQHGK VVMAKVDIDD 

       130        140        150        160 
HTDLAIEYEV SAVPTVLAIK NGDVVDKFVG IKDEDQLEAF LKKLIG 

« Hide

References

« Hide 'large scale' references
[1]Miranda-Vizuete A., Gustafsson J.-A., Spyrou G.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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 and DBA/2.
Tissue: Bone marrow, Kidney and Liver.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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].
Strain: C57BL/6.
Tissue: Brain.
[5]"The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice."
Nonn L., Williams R.R., Erickson R.P., Powis G.
Mol. Cell. Biol. 23:916-922(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85089 mRNA. Translation: AAB41900.1.
AK002358 mRNA. Translation: BAB22037.1.
AK010917 mRNA. Translation: BAB27267.1.
AK147164 mRNA. Translation: BAE27729.1.
AK149855 mRNA. Translation: BAE29126.1.
AK167754 mRNA. Translation: BAE39789.1.
AK167925 mRNA. Translation: BAE39930.1.
AK168322 mRNA. Translation: BAE40261.1.
AL583886 Genomic DNA. Translation: CAM23427.1.
BC068182 mRNA. Translation: AAH68182.1.
CCDSCCDS27606.1.
RefSeqNP_064297.1. NM_019913.5.
UniGeneMm.291917.
Mm.462887.

3D structure databases

ProteinModelPortalP97493.
SMRP97493. Positions 60-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97493. 1 interaction.
MINTMINT-4137662.
STRING10090.ENSMUSP00000105370.

PTM databases

PhosphoSiteP97493.

Proteomic databases

MaxQBP97493.
PaxDbP97493.
PRIDEP97493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005487; ENSMUSP00000005487; ENSMUSG00000005354.
ENSMUST00000109748; ENSMUSP00000105370; ENSMUSG00000005354.
GeneID56551.
KEGGmmu:56551.
UCSCuc007wof.1. mouse.

Organism-specific databases

CTD25828.
MGIMGI:1929468. Txn2.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00530000064086.
HOGENOMHOG000292977.
HOVERGENHBG009243.
InParanoidA2A440.
KOK03671.
OMASFNVQDH.
PhylomeDBP97493.
TreeFamTF314517.

Gene expression databases

BgeeP97493.
CleanExMM_TXN2.
GenevestigatorP97493.

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]
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR01068. thioredoxin. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTXN2. mouse.
NextBio312931.
PROP97493.
SOURCESearch...

Entry information

Entry nameTHIOM_MOUSE
AccessionPrimary (citable) accession number: P97493
Secondary accession number(s): A2A440, Q545D5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 119 of the entry and version 1 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