GPC3
entrez
2719
canonical
uniprot
P51654
canonical
ensembl
ENSG00000147257
resolver
ensp
ENSP00000359854
resolver
ensp
ENSP00000377836
resolver
ensp
ENSP00000486325
resolver
ensp
ENSP00000510438
resolver
enst
ENST00000689310
resolver
genesymbol
GPC3
resolver
genesymbol_syn
OCI5
resolver
hgnc
HGNC:4451
resolver
uniprot
A0A8I5KW36
resolver
uniprot
B4DTD8
resolver
uniprot
C9JLE3
resolver
uniprot
G3V1R0
resolver
uniprot
I6QTG3
resolver
uniprot
Q2L880
resolver
uniprot
Q2L882
resolver
uniprot
Q53H15
resolver
uniprot_entry
A0A8I5KW36_HUMAN
resolver
uniprot_entry
B4DTD8_HUMAN
resolver
uniprot_entry
GPC3_HUMAN
resolver
uniprot_entry
I6QTG3_HUMAN
resolver
uniprot_entry
Q53H15_HUMAN
resolver
uniprot_sec
C9JLE3
resolver
uniprot_sec
G3V1R0
resolver
uniprot_sec
Q2L880
resolver
uniprot_sec
Q2L882
resolver
amino_acid_sequence
MAGTVRTACLVVAMLLSLDFPGQAQPPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASMELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQLMNPGLPDSALDINECLRGARRDLKVFGNFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVLLGLFSTIHDSIQYVQKNAGKLTTTIGKLCAHSQQRQYRSAYYPEDLFIDKKVLKVAHVEHEETLSSRRRELIQKLKSFISFYSALPGYICSHSPVAENDTLCWNGQELVERYSQKAARNGMKNQFNLHELKMKGPEPVVSQIIDKLKHINQLLRTMSMPKGRVLDKNLDEEGFESGDCGDDEDECIGGSGDGMIKVKNQLRFLAELAYDLDVDDAPGNSQQATPKDNEISTFHNLGNVHSPLKLLTSMAISVVCFFFLVH
uniprot
proteins
disease_involvement
DISEASE: Simpson-Golabi-Behmel syndrome 1 (SGBS1) [MIM:312870]: A condition characterized by pre- and postnatal overgrowth (gigantism), facial dysmorphism and a variety of inconstant visceral and skeletal malformations. Characteristic dysmorphic features include macrocephaly with coarse, distinctive facies with a large protruding jaw, broad nasal bridge and cleft palate. Cardiac defects are frequent. {ECO:0000269|PubMed:10814714}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Cell surface proteoglycan (PubMed:14610063). Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (By similarity). Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation (By similarity). Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligands (PubMed:16227623, PubMed:24496449). Positively regulates the non-canonical Wnt signaling pathway (By similarity). Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression (By similarity). Inhibits the dipeptidyl peptidase activity of DPP4 (PubMed:17549790). Plays a role in limb patterning and skeletal development by controlling the cellular response to BMP4 (By similarity). Modulates the effects of growth factors BMP2, BMP7 and FGF7 on renal branching morphogenesis (By similarity). Required for coronary vascular development (By similarity). Plays a role in regulating cell movements during gastrulation (By similarity). {ECO:0000250|UniProtKB:Q6V9Y8, ECO:0000250|UniProtKB:Q8CFZ4, ECO:0000269|PubMed:14610063, ECO:0000269|PubMed:16227623, ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:24496449}.
uniprot
proteins
mass_dalton
65563
uniprot
proteins
mutagenesis
MUTAGEN 355..358; /note="RQYR->AQYA: Abolishes proteolytic processing. Abolishes interaction with WNT5A and ability to regulate Wnt signaling. Increases binding of hedgehog protein SHH to the PTC1 receptor and abolishes ability to inhibit hedgehog signaling."; /evidence="ECO:0000269|PubMed:14610063, ECO:0000269|PubMed:16227623, ECO:0000269|PubMed:25653284"; MUTAGEN 355; /note="R->A: No effect on proteolytic processing."; /evidence="ECO:0000269|PubMed:14610063"; MUTAGEN 358; /note="R->A: No effect on proteolytic processing."; /evidence="ECO:0000269|PubMed:14610063"; MUTAGEN 371..374; /note="KVLK->AVLA: No effect on proteolytic processing."; /evidence="ECO:0000269|PubMed:14610063"; MUTAGEN 387..389; /note="RRR->AAA: No effect on proteolytic processing."; /evidence="ECO:0000269|PubMed:14610063"; MUTAGEN 394..396; /note="KLK->ALA: No effect on proteolytic processing."; /evidence="ECO:0000269|PubMed:14610063
uniprot
proteins
post_translational_modification
PTM: O-glycosylated; contains heparan sulfate and/or chondroitin sulfate. {ECO:0000269|PubMed:14610063, ECO:0000269|PubMed:32337544}.; PTM: Cleaved intracellularly by a furin-like convertase to generate 2 subunits, alpha and beta, which remain associated through disulfide bonds and are associated with the cell surface via the GPI-anchor (PubMed:14610063). This processing is essential for its role in inhibition of hedgehog signaling (PubMed:25653284). A second proteolytic event may result in cleavage of the protein on the cell surface, separating it from the GPI-anchor and leading to its shedding from the cell surface (PubMed:14610063). {ECO:0000269|PubMed:14610063, ECO:0000269|PubMed:25653284}.
uniprot
proteins
protein_family
Glypican family
uniprot
proteins
pubmed
10814714
uniprot
proteins
pubmed
12851874
uniprot
proteins
pubmed
14610063
uniprot
proteins
pubmed
15059894
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16024626
uniprot
proteins
pubmed
16227623
uniprot
proteins
pubmed
17549790
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24496449
uniprot
proteins
pubmed
25653284
uniprot
proteins
pubmed
26091039
uniprot
proteins
pubmed
29345911
uniprot
proteins
pubmed
32337544
uniprot
proteins
pubmed
8589713
uniprot
proteins
pubmed
9021160
uniprot
proteins
pubmed
9133586
uniprot
proteins
pubmed
9339360
uniprot
proteins
sequence_length
580
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14610063}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P13265}; Extracellular side {ECO:0000250|UniProtKB:P13265}.
uniprot
proteins