TM4SF20
entrez
79853
canonical
uniprot
Q53R12
canonical
ensembl
ENSG00000168955
resolver
ensp
ENSP00000303028
resolver
enst
ENST00000304568
resolver
genesymbol
TM4SF20
resolver
hgnc
HGNC:26230
resolver
uniprot
B2RP42
resolver
uniprot
Q5U609
resolver
uniprot
Q6UWS1
resolver
uniprot
Q9H5X9
resolver
uniprot_entry
T4S20_HUMAN
resolver
uniprot_sec
B2RP42
resolver
uniprot_sec
Q5U609
resolver
uniprot_sec
Q6UWS1
resolver
uniprot_sec
Q9H5X9
resolver
amino_acid_sequence
MTCCEGWTSCNGFSLLVLLLLGVVLNAIPLIVSLVEEDQFSQNPISCFEWWFPGIIGAGLMAIPATTMSLTARKRACCNNRTGMFLSSLFSVITVIGALYCMLISIQALLKGPLMCNSPSNSNANCEFSLKNISDIHPESFNLQWFFNDSCAPPTGFNKPTSNDTMASGWRASSFHFDSEENKHRLIHFSVFLGLLLVGILEVLFGLSQIVIGFLGCLCGVSKRRSQIV
uniprot
proteins
disease_involvement
DISEASE: Specific language impairment 5 (SLI5) [MIM:615432]: A disorder characterized by a delay in early speech acquisition. It is usually associated with cerebral white matter abnormalities on brain MRI. Some individuals may show disorders in communication, consistent with autism spectrum disorder, or global developmental delay, although others ultimately show normal cognitive function. Penetrance is incomplete and expressivity is variable. {ECO:0000269|PubMed:23810381}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Polytopic transmembrane protein that inhibits regulated intramembrane proteolysis (RIP) of CREB3L1, inhibiting its activation and the induction of collagen synthesis (PubMed:25310401, PubMed:27499293). In response to ceramide, which alters TM4SF20 membrane topology, stimulates RIP activation of CREB3L1 (PubMed:27499293). Ceramide reverses the direction through which transmembrane helices are translocated into the endoplasmic reticulum membrane during translation of TM4SF20, this mechanism is called 'regulated alternative translocation' (RAT) and regulates the function of the transmembrane protein (PubMed:27499293). {ECO:0000269|PubMed:25310401, ECO:0000269|PubMed:27499293}.
uniprot
proteins
mass_dalton
25075
uniprot
proteins
mutagenesis
MUTAGEN 12; /note="G->P: No effect on cleavage of the first 13 residues."; /evidence="ECO:0000269|PubMed:27499293"; MUTAGEN 13; /note="F->P: No effect on cleavage of the first 13 residues."; /evidence="ECO:0000269|PubMed:27499293"; MUTAGEN 14; /note="S->P: Abolishes cleavage of the first 13 residues."; /evidence="ECO:0000269|PubMed:27499293"; MUTAGEN 15; /note="L->P: No effect on cleavage of the first 13 residues."; /evidence="ECO:0000269|PubMed:27499293"; MUTAGEN 16; /note="L->P: No effect on cleavage of the first 13 residues."; /evidence="ECO:0000269|PubMed:27499293"; MUTAGEN 22; /note="G->L: Inverts transmembrane topology. Induces cleavage of CREB3L1."; /evidence="ECO:0000269|PubMed:27499293"; MUTAGEN 26; /note="N->L: Inverts transmembrane topology."; /evidence="ECO:0000269|PubMed:27499293"; MUTAGEN 80; /note="N->Q: No effect on glycosylation upon ceramide treatment."; /evidence="ECO:0000269|PubMed:27499293"; MUTAGEN 132; /note="N->Q: Reduces glycosylation upon ceramide treatment. Abolishes glycosylation upon ceramide treatment; when associated with Q-132 and Q-163."; /evidence="ECO:0000269|PubMed:27499293"; MUTAGEN 148; /note="N->Q: Reduces glycosylation upon ceramide treatment. Abolishes glycosylation upon ceramide treatment; when associated with Q-132 and Q-163."; /evidence="ECO:0000269|PubMed:27499293"; MUTAGEN 163; /note="N->Q: Reduces glycosylation upon ceramide treatment. Abolishes glycosylation upon ceramide treatment; when associated with Q-132 and Q-148."; /evidence="ECO:0000269|PubMed:27499293
uniprot
proteins
post_translational_modification
PTM: Glycosylated at Asn-132, Asn-148 and Asn-163 in presence of ceramide which inverts the orientation of TM4SF20 in membranes exposing these residues to the endoplasmic reticulum lumen. {ECO:0000269|PubMed:27499293}.; PTM: Cleaved by signal peptidase at Ser-14 but the peptide does not act as a signal peptide. Cleavage is inhibited by ceramide which inverts the orientation of TM4SF20 in membranes exposing the N-terminus to the cytosol and not to the endoplasmic reticulum lumen. {ECO:0000269|PubMed:27499293}.
uniprot
proteins
protein_family
L6 tetraspanin family
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
23810381
uniprot
proteins
pubmed
25310401
uniprot
proteins
pubmed
27499293
uniprot
proteins
sequence_length
229
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:23810381}; Multi-pass membrane protein {ECO:0000269|PubMed:23810381}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25310401}; Multi-pass membrane protein {ECO:0000269|PubMed:25310401}. Note=Ceramide alters the direction through which transmembrane helices are translocated into the endoplasmic reticulum membrane during translation of TM4SF20. {ECO:0000269|PubMed:27499293}.
uniprot
proteins
transmembrane_region
TRANSMEM 15..35; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 45..65; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 84..104; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 186..206; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins