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Q8VBT0 (TMX1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. 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
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-related transmembrane protein 1
Alternative name(s):
Thioredoxin domain-containing protein 1
Gene names
Name:Tmx1
Synonyms:Txndc, Txndc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length278 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions.

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Endoplasmic reticulum membrane; Single-pass type I membrane protein Potential. Note: Predominantly found in the endoplasmic reticulum By similarity.

Sequence similarities

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 278252Thioredoxin-related transmembrane protein 1
PRO_0000034154

Regions

Topological domain27 – 181155Extracellular Potential
Transmembrane182 – 20221Helical; Potential
Topological domain203 – 27876Cytoplasmic Potential
Domain27 – 132106Thioredoxin

Amino acid modifications

Modified residue2451Phosphoserine Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10
Modified residue2561Phosphoserine Ref.6
Modified residue2781Phosphoserine By similarity
Disulfide bond56 ↔ 59Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VBT0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: EB682243008E3333

FASTA27831,396
        10         20         30         40         50         60 
MAHLGRLMVP LAALVLLLWA VPGAHGRRNN VRVLTDENWT SLLEGEWMIE FYAPWCPACQ 

        70         80         90        100        110        120 
NLQPEWESFA EWGEDLEVKV AKVDVTEQTG LSGRFIITAL PSIYHCKDGE FRRYVGPRTK 

       130        140        150        160        170        180 
KDFINFVSDK EWKNIEPISS WFGPSSVLMT MMSALFQLSV YIRTSHSYFV HDLGIPAWGS 

       190        200        210        220        230        240 
YLVFAFATVL SGLLLGLCMI FVADCLCPSK RRKPQQQYAK KTSPEFSQPL KKVEEEQEAD 

       250        260        270 
EEDVSEEEAE DREGASKATS QSSIRQRCVG LPSATDTS

« Hide

References

[1]"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 NOD.
Tissue: Bone marrow, Embryo, Pancreatic islet and Pituitary.
[2]"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 and FVB/N.
Tissue: Mammary gland and Retina.
[3]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, MASS SPECTROMETRY.
Tissue: Liver.
[4]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, MASS SPECTROMETRY.
Tissue: Brain cortex.
[5]"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, MASS SPECTROMETRY.
Tissue: Liver.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, MASS SPECTROMETRY.
Tissue: Liver.
[7]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, MASS SPECTROMETRY.
Tissue: Liver.
[8]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, MASS SPECTROMETRY.
Tissue: Melanoma.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, MASS SPECTROMETRY.
Tissue: Macrophage.
[10]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK013150 mRNA. Translation: BAB28680.3.
AK030429 mRNA. Translation: BAC26960.1.
AK050567 mRNA. Translation: BAC34326.1.
AK137059 mRNA. Translation: BAE23223.1.
AK150511 mRNA. Translation: BAE29624.1.
AK153027 mRNA. Translation: BAE31660.1.
AK170468 mRNA. Translation: BAE41816.1.
BC017603 mRNA. Translation: AAH17603.1.
BC021533 mRNA. Translation: AAH21533.1.
IPIIPI00121341.
RefSeqNP_082615.1. NM_028339.1.
UniGeneMm.490350.

3D structure databases

ProteinModelPortalQ8VBT0.
SMRQ8VBT0. Positions 23-146.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000021471.

PTM databases

PhosphoSiteQ8VBT0.

Proteomic databases

PaxDbQ8VBT0.
PRIDEQ8VBT0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021471; ENSMUSP00000021471; ENSMUSG00000021072.
GeneID72736.
KEGGmmu:72736.
UCSCuc007ntu.1. mouse.

Organism-specific databases

CTD81542.
MGIMGI:1919986. Tmx1.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00390000011580.
HOGENOMHOG000045750.
InParanoidQ8VBT0.
OMALLWGAPW.
OrthoDBEOG4KSPKM.

Gene expression databases

BgeeQ8VBT0.
CleanExMM_TXNDC1.
GenevestigatorQ8VBT0.
GermOnlineENSMUSG00000021072. Mus musculus.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTMX1. mouse.
NextBio336838.
SOURCESearch...

Entry information

Entry nameTMX1_MOUSE
AccessionPrimary (citable) accession number: Q8VBT0
Secondary accession number(s): Q3UCI8, Q9CSD5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2002
Last modified: April 3, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents