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Protein

Thioredoxin-related transmembrane protein 1

Gene

Tmx1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. disulfide oxidoreductase activity Source: MGI
  2. protein disulfide isomerase activity Source: GO_Central

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. protein folding Source: GO_Central
  3. response to endoplasmic reticulum stress Source: MGI
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-related transmembrane protein 1
Alternative name(s):
Thioredoxin domain-containing protein 1
Gene namesi
Name:Tmx1
Synonyms:Txndc, Txndc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1919986. Tmx1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 181155ExtracellularSequence AnalysisAdd
BLAST
Transmembranei182 – 20221HelicalSequence AnalysisAdd
BLAST
Topological domaini203 – 27876CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. endoplasmic reticulum membrane Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. nucleolus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 278252Thioredoxin-related transmembrane protein 1PRO_0000034154Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 59Redox-activePROSITE-ProRule annotation
Modified residuei245 – 2451Phosphoserine3 Publications
Modified residuei278 – 2781PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ8VBT0.
PaxDbiQ8VBT0.
PRIDEiQ8VBT0.

PTM databases

PhosphoSiteiQ8VBT0.

Expressioni

Gene expression databases

BgeeiQ8VBT0.
CleanExiMM_TXNDC1.
GenevestigatoriQ8VBT0.

Interactioni

Protein-protein interaction databases

IntActiQ8VBT0. 1 interaction.
STRINGi10090.ENSMUSP00000021471.

Structurei

3D structure databases

ProteinModelPortaliQ8VBT0.
SMRiQ8VBT0. Positions 23-146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 132106ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00390000011580.
HOGENOMiHOG000045750.
InParanoidiQ8VBT0.
OMAiAPWTHGR.
OrthoDBiEOG7KM5VC.
PhylomeDBiQ8VBT0.
TreeFamiTF106376.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
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.

Q8VBT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHLGRLMVP LAALVLLLWA VPGAHGRRNN VRVLTDENWT SLLEGEWMIE
60 70 80 90 100
FYAPWCPACQ NLQPEWESFA EWGEDLEVKV AKVDVTEQTG LSGRFIITAL
110 120 130 140 150
PSIYHCKDGE FRRYVGPRTK KDFINFVSDK EWKNIEPISS WFGPSSVLMT
160 170 180 190 200
MMSALFQLSV YIRTSHSYFV HDLGIPAWGS YLVFAFATVL SGLLLGLCMI
210 220 230 240 250
FVADCLCPSK RRKPQQQYAK KTSPEFSQPL KKVEEEQEAD EEDVSEEEAE
260 270
DREGASKATS QSSIRQRCVG LPSATDTS
Length:278
Mass (Da):31,396
Last modified:February 28, 2002 - v1
Checksum:iEB682243008E3333
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25958.1.
RefSeqiNP_082615.1. NM_028339.1.
UniGeneiMm.204670.

Genome annotation databases

EnsembliENSMUST00000021471; ENSMUSP00000021471; ENSMUSG00000021072.
GeneIDi72736.
KEGGimmu:72736.
UCSCiuc007ntu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25958.1.
RefSeqiNP_082615.1. NM_028339.1.
UniGeneiMm.204670.

3D structure databases

ProteinModelPortaliQ8VBT0.
SMRiQ8VBT0. Positions 23-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VBT0. 1 interaction.
STRINGi10090.ENSMUSP00000021471.

PTM databases

PhosphoSiteiQ8VBT0.

Proteomic databases

MaxQBiQ8VBT0.
PaxDbiQ8VBT0.
PRIDEiQ8VBT0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021471; ENSMUSP00000021471; ENSMUSG00000021072.
GeneIDi72736.
KEGGimmu:72736.
UCSCiuc007ntu.1. mouse.

Organism-specific databases

CTDi81542.
MGIiMGI:1919986. Tmx1.

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00390000011580.
HOGENOMiHOG000045750.
InParanoidiQ8VBT0.
OMAiAPWTHGR.
OrthoDBiEOG7KM5VC.
PhylomeDBiQ8VBT0.
TreeFamiTF106376.

Miscellaneous databases

ChiTaRSiTmx1. mouse.
NextBioi336838.
PROiQ8VBT0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VBT0.
CleanExiMM_TXNDC1.
GenevestigatoriQ8VBT0.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and FVB/N.
    Tissue: Mammary gland and Retina.
  3. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTMX1_MOUSE
AccessioniPrimary (citable) accession number: Q8VBT0
Secondary accession number(s): Q3UCI8, Q9CSD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2004
Last sequence update: February 28, 2002
Last modified: March 3, 2015
This is version 123 of the entry and version 1 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.