Gpc1
entrez
14733
canonical
uniprot
Q9QZF2
canonical
ensembl
ENSMUSG00000034220
resolver
ensp
ENSMUSP00000047199
resolver
enst
ENSMUST00000045970
resolver
genesymbol
Gpc1
resolver
uniprot
Q3U379
resolver
uniprot_entry
GPC1_MOUSE
resolver
uniprot_entry
Q3U379_MOUSE
resolver
amino_acid_sequence
MELRTRGWWLLCAAAALVVCARGDPASKSRSCSEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANHSRMELESALHDSSRALQATLATQLHGIDDHFQRLLNDSERTLQEAFPGAFGDLYTQNTRAFRDLYAELRLYYRGANLHLEETLAEFWARLLERLFKQLHPQLLPDDYLDCLGKQAEALRPFGDAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVPLAPECSRAIMKLVYCAHCRGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGPSGAESVIGGVHVWLAEAINALQDNKDTLTAKVIQACGNPKVNPHGSGPEEKRRRGKLALQEKPSTGTLEKLVSEAKAQLRDIQDFWISLPGTLCSEKMAMSPASDDRCWNGISKGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRGAYGGNDVDFQDASDDGSGSGSGGGCPDDTCGRRVSKKSSSSRTPLTHALPGLSEQEGQKTSAATCPEPHSFFLLFLVTLVLAAARPRWR
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. Binds Cu(2+) or Zn(2+) ions. {ECO:0000250, ECO:0000269|PubMed:19732411, ECO:0000269|PubMed:19936054, ECO:0000269|PubMed:20100867, ECO:0000269|PubMed:21996748}.
uniprot
proteins
mass_dalton
61360
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. {ECO:0000269|PubMed:15677459}.; 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:15677459, ECO:0000269|PubMed:16971378, ECO:0000269|PubMed:18717736, ECO:0000269|PubMed:19656770}.; PTM: This cell-associated glypican is further processed to give rise to a medium-released species. {ECO:0000250}.
uniprot
proteins
protein_family
Glypican family
uniprot
proteins
pubmed
11474185
uniprot
proteins
pubmed
12732622
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15677459
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
16923158
uniprot
proteins
pubmed
16971378
uniprot
proteins
pubmed
18717736
uniprot
proteins
pubmed
19656770
uniprot
proteins
pubmed
19732411
uniprot
proteins
pubmed
19936054
uniprot
proteins
pubmed
20100867
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21996748
uniprot
proteins
sequence_length
557
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