TSPAN12
entrez
23554
canonical
uniprot
O95859
canonical
ensembl
ENSG00000106025
resolver
ensp
ENSP00000222747
resolver
ensp
ENSP00000397699
resolver
ensp
ENSP00000524379
resolver
ensp
ENSP00000524381
resolver
ensp
ENSP00000588729
resolver
genesymbol
TSPAN12
resolver
genesymbol_syn
NET2
resolver
genesymbol_syn
TM4SF12
resolver
hgnc
HGNC:21641
resolver
uniprot
A4D0V8
resolver
uniprot
B4DRG6
resolver
uniprot
Q549U9
resolver
uniprot
Q8N5Y0
resolver
uniprot_entry
TSN12_HUMAN
resolver
uniprot_sec
A4D0V8
resolver
uniprot_sec
B4DRG6
resolver
uniprot_sec
Q549U9
resolver
uniprot_sec
Q8N5Y0
resolver
amino_acid_sequence
MAREDSVKCLRCLLYALNLLFWLMSISVLAVSAWMRDYLNNVLTLTAETRVEEAVILTYFPVVHPVMIAVCCFLIIVGMLGYCGTVKRNLLLLAWYFGSLLVIFCVELACGVWTYEQELMVPVQWSDMVTLKARMTNYGLPRYRWLTHAWNFFQREFKCCGVVYFTDWLEMTEMDWPPDSCCVREFPGCSKQAHQEDLSDLYQEGCGKKMYSFLRGTKQLQVLRFLGISIGVTQILAMILTITLLWALYYDRREPGTDQMMSLKNDNSQHLSCPSVELLKPSLSRIFEHTSMANSFNTHFEMEEL
uniprot
proteins
disease_involvement
DISEASE: Vitreoretinopathy, exudative 5 (EVR5) [MIM:613310]: An autosomal dominant form of exudative vitreoretinopathy, a disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery. {ECO:0000269|PubMed:20159111, ECO:0000269|PubMed:20159112, ECO:0000269|PubMed:22427576}. Note=The disease is caused by variants affecting the gene represented in this entry. TSPAN12 dominant and recessive mutations have been identified in patients with exudative vitreoretinopathy. Patients with mutations in both alleles of TSPAN12 have severe exudative vitreoretinopathy or retinal dysplasia. These mutations appear to result in a milder phenotype in heterozygous mutation carriers (PubMed:22427576). {ECO:0000269|PubMed:22427576}.
uniprot
proteins
function
FUNCTION: Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activates the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1) (By similarity). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity. {ECO:0000250, ECO:0000269|PubMed:19211836, ECO:0000269|PubMed:19587294}.
uniprot
proteins
mass_dalton
35383
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="C->S: Impairs interaction with ADAM10; when associated with S-12 and S-83."; /evidence="ECO:0000269|PubMed:19587294"; MUTAGEN 12; /note="C->S: Impairs interaction with ADAM10; when associated with S-9 and S-83."; /evidence="ECO:0000269|PubMed:19587294"; MUTAGEN 83; /note="C->S: Impairs interaction with ADAM10; when associated with S-9 and S-12."; /evidence="ECO:0000269|PubMed:19587294
uniprot
proteins
post_translational_modification
PTM: Palmitoylated; required for interaction with ADAM10. The precise position of palmitoylated residues is unclear and occurs either on Cys-9, Cys-12 and/or Cys-83. {ECO:0000269|PubMed:19587294}.
uniprot
proteins
protein_family
Tetraspanin (TM4SF) family
uniprot
proteins
pubmed
10719184
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19211836
uniprot
proteins
pubmed
19587294
uniprot
proteins
pubmed
20159111
uniprot
proteins
pubmed
20159112
uniprot
proteins
pubmed
22427576
uniprot
proteins
sequence_length
305
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 13..33; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 60..80; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 90..110; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 225..245; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins