TMEM147
entrez
10430
canonical
uniprot
Q9BVK8
canonical
ensembl
ENSG00000105677
resolver
ensp
ENSP00000222284
resolver
ensp
ENSP00000376040
resolver
ensp
ENSP00000598987
resolver
genesymbol
TMEM147
resolver
hgnc
HGNC:30414
resolver
uniprot
A8MWW0
resolver
uniprot
O75790
resolver
uniprot_entry
TM147_HUMAN
resolver
uniprot_sec
A8MWW0
resolver
uniprot_sec
O75790
resolver
amino_acid_sequence
MTLFHFGNCFALAYFPYFITYKCSGLSEYNAFWKCVQAGVTYLFVQLCKMLFLATFFPTWEGGIYDFIGEFMKASVDVADLIGLNLVMSRNAGKGEYKIMVAALGWATAELIMSRCIPLWVGARGIEFDWKYIQMSIDSNISLVHYIVASAQVWMITRYDLYHTFRPAVLLLMFLSVYKAFVMETFVHLCSLGSWAALLARAVVTGLLALSTLALYVAVVNVHS
uniprot
proteins
disease_involvement
DISEASE: Neurodevelopmental disorder with facial dysmorphism, absent language, and pseudo-Pelger-Huet anomaly (NEDFLPH) [MIM:620075]: An autosomal recessive disorder with onset in infancy and characterized by global developmental delay, intellectual disability, dysmorphic facial features, coarse facies, and behavioral problems. Affected individuals may have variable findings on brain imaging, such as cortical atrophy, thin corpus callosum and enlarged ventricles. Laboratory studies show nuclear lobulation defects in a subset of neutrophils, indicating a pseudo-Pelger-Huet anomaly. {ECO:0000269|PubMed:36044892}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (PubMed:32820719, PubMed:36261522). The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions (PubMed:36261522). Also acts as a negative regulator of CHRM3 function, most likely by interfering with its trafficking to the cell membrane (PubMed:21056967). Negatively regulates CHRM3-mediated calcium mobilization and activation of RPS6KA1/p90RSK activity (PubMed:21056967). Regulates LBR localization to the nucleus inner membrane (PubMed:32694168). {ECO:0000269|PubMed:21056967, ECO:0000269|PubMed:32694168, ECO:0000269|PubMed:32820719, ECO:0000269|PubMed:36261522}.
uniprot
proteins
mass_dalton
25261
uniprot
proteins
protein_family
TMEM147 family
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20538592
uniprot
proteins
pubmed
21056967
uniprot
proteins
pubmed
32694168
uniprot
proteins
pubmed
32820719
uniprot
proteins
pubmed
36044892
uniprot
proteins
pubmed
36261522
uniprot
proteins
sequence_length
224
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20538592, ECO:0000269|PubMed:21056967, ECO:0000269|PubMed:32694168, ECO:0000269|PubMed:36044892, ECO:0000269|PubMed:36261522}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:32694168}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:I6VSD2}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 1..21; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0A8I3MKU8"; TRANSMEM 35..58; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0A8I3MKU8"; TRANSMEM 67..88; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0A8I3MKU8"; TRANSMEM 99..124; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0A8I3MKU8"; TRANSMEM 130..155; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0A8I3MKU8"; TRANSMEM 165..187; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0A8I3MKU8"; TRANSMEM 195..216; /note="Helical"; /evidence="ECO:0000250|UniProtKB:A0A8I3MKU8
uniprot
proteins