GPC1
entrez
2817
canonical
uniprot
P35052
canonical
ensembl
ENSG00000063660
resolver
ensp
ENSP00000264039
resolver
ensp
ENSP00000415077
resolver
enst
ENST00000420138
resolver
genesymbol
GPC1
resolver
hgnc
HGNC:4449
resolver
uniprot
A0A384NPH9
resolver
uniprot
B3KTD1
resolver
uniprot
H7C410
resolver
uniprot
Q53QM4
resolver
uniprot_entry
A0A384NPH9_HUMAN
resolver
uniprot_entry
GPC1_HUMAN
resolver
uniprot_entry
H7C410_HUMAN
resolver
uniprot_sec
B3KTD1
resolver
uniprot_sec
Q53QM4
resolver
amino_acid_sequence
MELRARGWWLLCAAAALVACARGDPASKSRSCGEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANRSHAELETALRDSSRVLQAMLATQLRSFDDHFQHLLNDSERTLQATFPGAFGELYTQNARAFRDLYSELRLYYRGANLHLEETLAEFWARLLERLFKQLHPQLLLPDDYLDCLGKQAEALRPFGEAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVPLGPECSRAVMKLVYCAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGTSGVESVIGSVHTWLAEAINALQDNRDTLTAKVIQGCGNPKVNPQGPGPEEKRRRGKLAPRERPPSGTLEKLVSEAKAQLRDVQDFWISLPGTLCSEKMALSTASDDRCWNGMARGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRSAYNGNDVDFQDASDDGSGSGSGDGCLDDLCSRKVSRKSSSSRTPLTHALPGLSEQEGQKTSAASCPQPPTFLLPLLLFLALTVARPRWR
uniprot
proteins
disease_involvement
DISEASE: Note=Associates (via the heparan sulfate side chains) with fibrillar APP amyloid-beta peptides in primitive and classic amyloid plaques and may be involved in the deposition of these senile plaques in the Alzheimer disease (AD) brain (PubMed:15084524). {ECO:0000269|PubMed:15084524}.; DISEASE: Note=Misprocessing of GPC1 is found in fibroblasts of patients with Niemann-Pick Type C1 disease. This is due to the defective deaminative degradation of heparan sulfate chains (PubMed:16645004). {ECO:0000269|PubMed:16645004}.
uniprot
proteins
function
FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling. {ECO:0000250, ECO:0000269|PubMed:19936054, ECO:0000269|PubMed:21642435}.
uniprot
proteins
mass_dalton
61680
uniprot
proteins
mutagenesis
MUTAGEN 79; /note="N->Q: Protein yield reduced by half. Protein yield reduced by 90%, abolishes N-glycosylation but no effect on secondary structure; when associated with Q-116."; /evidence="ECO:0000269|PubMed:21932778"; MUTAGEN 116; /note="N->Q: No effect on protein yield. Protein yield reduced by 90%, abolishes N-glycosylation but no effect on secondary structure; when associated with Q-79."; /evidence="ECO:0000269|PubMed:21932778
uniprot
proteins
post_translational_modification
PTM: S-nitrosylated in a Cu(2+)-dependent manner. Nitric acid (NO) is released from the nitrosylated cysteines by ascorbate or by some other reducing agent, in a Cu(2+) or Zn(2+) dependent manner. This free nitric oxide is then capable of cleaving the heparan sulfate side chains.; PTM: N- and O-glycosylated. N-glycosylation is mainly of the complex type containing sialic acid. O-glycosylated with heparan sulfate. The heparan sulfate chains can be cleaved either by the action of heparanase or, degraded by a deaminative process that uses nitric oxide (NO) released from the S-nitrosylated cysteines. This process is triggered by ascorbate, or by some other reducing agent, in a Cu(2+)- or Zn(2+) dependent manner. Cu(2+) ions are provided by ceruloproteins such as APP, PRNP or CP which associate with GCP1 in intracellular compartments or lipid rafts. {ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:16971378, ECO:0000269|PubMed:19479373, ECO:0000269|PubMed:19775117, ECO:0000269|PubMed:2148568, ECO:0000269|PubMed:21642435, ECO:0000269|PubMed:21932778, ECO:0000269|PubMed:22351761}.; PTM: This cell-associated glypican is further processed to give rise to a medium-released species.
uniprot
proteins
protein_family
Glypican family
uniprot
proteins
pubmed
12732622
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15084524
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16645004
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
16971378
uniprot
proteins
pubmed
19479373
uniprot
proteins
pubmed
19775117
uniprot
proteins
pubmed
19936054
uniprot
proteins
pubmed
2148568
uniprot
proteins
pubmed
21642435
uniprot
proteins
pubmed
21932778
uniprot
proteins
pubmed
22351761
uniprot
proteins
sequence_length
558
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Endosome. Note=S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endosomes. Associates with both forms of PRNP in lipid rafts. Colocalizes with APP in perinuclear compartments and with CP in intracellular compartments. Associates with fibrillar APP amyloid-beta peptides in lipid rafts in Alzheimer disease brains.; SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular space.
uniprot
proteins