TMX1
entrez
81542
canonical
uniprot
Q9H3N1
canonical
ensembl
ENSG00000139921
resolver
ensp
ENSP00000393316
resolver
enst
ENST00000457354
resolver
genesymbol
TMX1
resolver
genesymbol_syn
TMX
resolver
genesymbol_syn
TXNDC
resolver
genesymbol_syn
TXNDC1
resolver
hgnc
HGNC:15487
resolver
uniprot
B2R7A4
resolver
uniprot
Q8N487
resolver
uniprot
Q8NBN5
resolver
uniprot
Q9Y4T6
resolver
uniprot_entry
TMX1_HUMAN
resolver
uniprot_sec
B2R7A4
resolver
uniprot_sec
Q8N487
resolver
uniprot_sec
Q8NBN5
resolver
uniprot_sec
Q9Y4T6
resolver
amino_acid_sequence
MAPSGSLAVPLAVLVLLLWGAPWTHGRRSNVRVITDENWRELLEGDWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNIAKVDVTEQPGLSGRFIITALPTIYHCKDGEFRRYQGPRTKKDFINFISDKEWKSIEPVSSWFGPGSVLMSSMSALFQLSMWIRTCHNYFIEDLGLPVWGSYTVFALATLFSGLLLGLCMIFVADCLCPSKRRRPQPYPYPSKKLLSESAQPLKKVEEEQEADEEDVSEEEAESKEGTNKDFPQNAIRQRSLGPSLATDKS
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:11152479, PubMed:37648867). 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 (PubMed:37648867). The alternative triglyceride biosynthesis pathway mediates formation of triacylglycerol from diacylglycerol and membrane phospholipids (PubMed:37648867). Acts as a protein disulfide isomerase by catalyzing formation or reduction of disulfide bonds (PubMed:22228764, PubMed:29932915). Specifically mediates formation of disulfide bonds of transmembrane proteins at the endoplasmic reticulum membrane (PubMed:22228764). Involved in endoplasmic reticulum-associated degradation (ERAD) via its protein disulfide isomerase activity by acting on folding-defective polypeptides at the endoplasmic reticulum membrane (PubMed:29932915). 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 (PubMed:27502484, PubMed:31304984). Regulates endoplasmic reticulum-mitochondria Ca(2+) flux (PubMed:27502484). {ECO:0000269|PubMed:11152479, ECO:0000269|PubMed:22228764, ECO:0000269|PubMed:27502484, ECO:0000269|PubMed:29932915, ECO:0000269|PubMed:30425049, ECO:0000269|PubMed:31304984, ECO:0000269|PubMed:37648867}.
uniprot
proteins
mass_dalton
31791
uniprot
proteins
mutagenesis
MUTAGEN 56; /note="C->S: Loss of reductase activity and ability to inhibit TMEM68/DIESL; when associated with S-59."; /evidence="ECO:0000269|PubMed:11152479, ECO:0000269|PubMed:37648867"; MUTAGEN 59; /note="C->S: Loss of reductase activity and ability to inhibit TMEM68/DIESL; when associated with S-56."; /evidence="ECO:0000269|PubMed:11152479, ECO:0000269|PubMed:37648867"; MUTAGEN 205..207; /note="CLC->ALA: Abolished palmitoylation, leading to decreased localization to mitochondria-associated endoplasmic reticulum membrane (MAM)."; /evidence="ECO:0000269|PubMed:22045338, ECO:0000269|PubMed:27502484
uniprot
proteins
post_translational_modification
PTM: Palmitoylated; palmitoylation is required for localization to mitochondria-associated endoplasmic reticulum membrane (MAM). {ECO:0000269|PubMed:22045338, ECO:0000269|PubMed:27502484}.
uniprot
proteins
pubmed
11152479
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22045338
uniprot
proteins
pubmed
22228764
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27502484
uniprot
proteins
pubmed
29932915
uniprot
proteins
pubmed
30425049
uniprot
proteins
pubmed
31304984
uniprot
proteins
pubmed
37648867
uniprot
proteins
sequence_length
280
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11152479, ECO:0000269|PubMed:22045338, ECO:0000269|PubMed:27502484, ECO:0000269|PubMed:31304984, ECO:0000269|PubMed:37648867}; Single-pass type I membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:22045338, ECO:0000269|PubMed:27502484, ECO:0000269|PubMed:31304984}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000305|PubMed:30425049}. Note=Predominantly found in the endoplasmic reticulum (PubMed:11152479). Secreted in the extracellular space following thrombin stimulation (PubMed:30425049). Localizes to mitochondria-associated endoplasmic reticulum membrane (MAM); palmitoylation is required for MAM localization (PubMed:22045338, PubMed:27502484, PubMed:31304984). {ECO:0000269|PubMed:11152479, ECO:0000269|PubMed:22045338, ECO:0000269|PubMed:27502484, ECO:0000269|PubMed:30425049, ECO:0000269|PubMed:31304984}.
uniprot
proteins
transmembrane_region
TRANSMEM 181..203; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins