Gpc1
entrez
58920
canonical
uniprot
P35053
canonical
ensembl
ENSRNOG00000049437
resolver
ensp
ENSRNOP00000066597
resolver
enst
ENSRNOT00000074395
resolver
genesymbol
Gpc1
resolver
uniprot
M0RAP4
resolver
uniprot
Q6P7Q2
resolver
uniprot_entry
GPC1_RAT
resolver
uniprot_entry
M0RAP4_RAT
resolver
uniprot_entry
Q6P7Q2_RAT
resolver
amino_acid_sequence
MELRARGWWLLCAAAALVACTRGDPASKSRSCSEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANHSRMELETALHDSSRALQATLATQLHGIDDHFQRLLNDSERTLQDAFPGAFGDLYTQNTRAFRDLYAELRLYYRGANLHLEETLAEFWARLLERLFKQLHPQLLLPDDYLDCLGKQAEALRPFGDAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVPLAPECSRAVMKLVYCAHCRGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGPSGAEYVIGSVHMWLAEAINALQDNKDTLTAKVIQGCGNPKVNPHGSGPEEKRRRAKLALQEKSSTGTLEKLVSEAKAQLRDIQDYWISLPGTLCSEKMAMSPASDDRCWNGISKGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRGAYGGNDVDFQDASDDGSGSGSGGGCPDDACGRRVSKKSSSSRTPLIHALPGLSEQEGQKTSAATRPEPHYFFLLFLFTLVLAAARPRWR
uniprot
proteins
function
FUNCTION: Cell surface proteoglycan that bears heparan sulfate. 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 (By similarity). Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination. {ECO:0000250, ECO:0000269|PubMed:15383532, ECO:0000269|PubMed:16407548}.
uniprot
proteins
mass_dalton
61734
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:14707133}.; 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
1417860
uniprot
proteins
pubmed
14707133
uniprot
proteins
pubmed
15383532
uniprot
proteins
pubmed
16407548
uniprot
proteins
pubmed
8207484
uniprot
proteins
sequence_length
558
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Endosome {ECO:0000250}. 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 (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular space {ECO:0000250}.
uniprot
proteins