Tmx1
entrez
72736
canonical
uniprot
Q8VBT0
canonical
ensembl
ENSMUSG00000021072
resolver
ensp
ENSMUSP00000021471
resolver
enst
ENSMUST00000021471
resolver
genesymbol
Tmx1
resolver
genesymbol_syn
Txndc
resolver
genesymbol_syn
Txndc1
resolver
uniprot
Q3UCI8
resolver
uniprot
Q9CSD5
resolver
uniprot_entry
TMX1_MOUSE
resolver
uniprot_sec
Q3UCI8
resolver
uniprot_sec
Q9CSD5
resolver
amino_acid_sequence
MAHLGRLMVPLAALVLLLWAVPGAHGRRNNVRVLTDENWTSLLEGEWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVKVAKVDVTEQTGLSGRFIITALPSIYHCKDGEFRRYVGPRTKKDFINFVSDKEWKNIEPISSWFGPSSVLMTMMSALFQLSVYIRTSHSYFVHDLGIPAWGSYLVFAFATVLSGLLLGLCMIFVADCLCPSKRRKPQQQYAKKTSPEFSQPLKKVEEEQEADEEDVSEEEAEDREGASKATSQSSIRQRCVGLPSATDTS
uniprot
proteins
ec_number
5.3.4.1
uniprot
proteins
function
FUNCTION: Thioredoxin domain-containing protein that participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions (PubMed:26246604). Acts as a key inhibitor of the alternative triglyceride biosynthesis pathway by inhibiting the activity of TMEM68/DIESL at the endoplasmic reticulum, thereby restricting accumulation of triacylglycerol (By similarity). The alternative triglyceride biosynthesis pathway mediates formation of triacylglycerol from diacylglycerol and membrane phospholipids (By similarity). Acts as a protein disulfide isomerase by catalyzing formation or reduction of disulfide bonds (PubMed:26246604). Specifically mediates formation of disulfide bonds of transmembrane proteins at the endoplasmic reticulum membrane (PubMed:26246604). Involved in ER-associated degradation (ERAD) via its protein disulfide isomerase activity by acting on folding-defective polypeptides at the endoplasmic reticulum membrane (By similarity). Acts as a negative regulator of platelet aggregation following secretion in the extracellular space (PubMed:30425049). Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals (By similarity). Regulates endoplasmic reticulum-mitochondria Ca(2+) flux (By similarity). {ECO:0000250|UniProtKB:Q9H3N1, ECO:0000269|PubMed:26246604, ECO:0000269|PubMed:30425049}.
uniprot
proteins
mass_dalton
31396
uniprot
proteins
mutagenesis
MUTAGEN 59; /note="C->A: Abolished protein disulfide isomerase activity."; /evidence="ECO:0000269|PubMed:26246604
uniprot
proteins
post_translational_modification
PTM: Palmitoylated; palmitoylation is required for localization to mitochondria-associated endoplasmic reticulum membrane (MAM). {ECO:0000250|UniProtKB:Q9H3N1}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17114649
uniprot
proteins
pubmed
17208939
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18630941
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
26246604
uniprot
proteins
pubmed
30425049
uniprot
proteins
sequence_length
278
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9H3N1}; Single-pass type I membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9H3N1}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:Q9H3N1}. Note=Predominantly found in the endoplasmic reticulum. Secreted in the extracellular space following thrombin stimulation. Localizes to mitochondria-associated endoplasmic reticulum membrane (MAM); palmitoylation is required for MAM localization. {ECO:0000250|UniProtKB:Q9H3N1}.
uniprot
proteins
transmembrane_region
TRANSMEM 182..202; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins