GPC1_HUMAN
ID GPC1_HUMAN Reviewed; 558 AA.
AC P35052; B3KTD1; Q53QM4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Glypican-1;
DE Contains:
DE RecName: Full=Secreted glypican-1;
DE Flags: Precursor;
GN Name=GPC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-53; 100-118
RP AND 298-317, GPI-ANCHOR AT SER-530, GLYCOSYLATION AT ASN-116, AND VARIANT
RP GLY-500.
RC TISSUE=Lung fibroblast;
RX PubMed=2148568; DOI=10.1083/jcb.111.6.3165;
RA David G., Lories V., Decock B., Marynen P., Cassiman J.-J.,
RA van den Berghe H.;
RT "Molecular cloning of a phosphatidylinositol-anchored membrane heparan
RT sulfate proteoglycan from human lung fibroblasts.";
RL J. Cell Biol. 111:3165-3176(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-500.
RC TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP COPPER-BINDING, S-NITROSYLATION, AND GLYCOSYLATION.
RX PubMed=12732622; DOI=10.1074/jbc.m300394200;
RA Mani K., Cheng F., Havsmark B., Jonsson M., Belting M., Fransson L.A.;
RT "Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-
RT nitroso-dependent autocleavage of glypican-1 heparan sulfate.";
RL J. Biol. Chem. 278:38956-38965(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND POSSIBLE ASSOCIATION WITH ALZHEIMER DISEASE.
RX PubMed=15084524; DOI=10.1096/fj.03-1040fje;
RA Watanabe N., Araki W., Chui D.H., Makifuchi T., Ihara Y., Tabira T.;
RT "Glypican-1 as an Abeta binding HSPG in the human brain: its localization
RT in DIG domains and possible roles in the pathogenesis of Alzheimer's
RT disease.";
RL FASEB J. 18:1013-1015(2004).
RN [8]
RP S-NITROSYLATION, AND ASSOCIATION WITH NIEMANN-PICK TYPE C1 DISEASE.
RX PubMed=16645004; DOI=10.1093/glycob/cwj121;
RA Mani K., Cheng F., Fransson L.A.;
RT "Defective nitric oxide-dependent, deaminative cleavage of glypican-1
RT heparan sulfate in Niemann-Pick C1 fibroblasts.";
RL Glycobiology 16:711-718(2006).
RN [9]
RP SUBCELLULAR LOCATION, S-NITROSYLATION, AND GLYCOSYLATION.
RX PubMed=16971378; DOI=10.1093/glycob/cwl045;
RA Mani K., Cheng F., Fransson L.A.;
RT "Constitutive and vitamin C-induced, NO-catalyzed release of heparan
RT sulfate from recycling glypican-1 in late endosomes.";
RL Glycobiology 16:1251-1261(2006).
RN [10]
RP GLYCOSYLATION, AND LACK OF GLYCOSYLATION AT SER-55.
RX PubMed=19775117; DOI=10.1021/bi901402x;
RA Svensson G., Linse S., Mani K.;
RT "Chemical and thermal unfolding of glypican-1: protective effect of heparan
RT sulfate against heat-induced irreversible aggregation.";
RL Biochemistry 48:9994-10004(2009).
RN [11]
RP S-NITROSYLATION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=19479373; DOI=10.1007/s10719-009-9243-z;
RA Svensson G., Mani K.;
RT "S-Nitrosylation of secreted recombinant human glypican-1.";
RL Glycoconj. J. 26:1247-1257(2009).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19936054; DOI=10.1371/journal.ppat.1000666;
RA Taylor D.R., Whitehouse I.J., Hooper N.M.;
RT "Glypican-1 mediates both prion protein lipid raft association and disease
RT isoform formation.";
RL PLoS Pathog. 5:E1000666-E1000666(2009).
RN [13]
RP GLYCOSYLATION AT ASN-79 AND ASN-116, AND MUTAGENESIS OF ASN-79 AND ASN-116.
RX PubMed=21932778; DOI=10.1021/bi200218s;
RA Svensson G., Hyrenius Wittsten A., Linse S., Mani K.;
RT "The structural role of N-linked glycans on human glypican-1.";
RL Biochemistry 50:9377-9387(2011).
RN [14]
RP S-NITROSYLATION, GLYCOSYLATION, AND FUNCTION.
RX PubMed=21642435; DOI=10.1074/jbc.m111.243345;
RA Cheng F., Cappai R., Ciccotosto G.D., Svensson G., Multhaup G.,
RA Fransson L.A., Mani K.;
RT "Suppression of amyloid beta A11 antibody immunoreactivity by vitamin C:
RT possible role of heparan sulfate oligosaccharides derived from glypican-1
RT by ascorbate-induced, nitric oxide (NO)-catalyzed degradation.";
RL J. Biol. Chem. 286:27559-27572(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), DISULFIDE BONDS, LACK OF
RP GLYCOSYLATION AT SER-55, AND GLYCOSYLATION AT ASN-79 AND ASN-116.
RX PubMed=22351761; DOI=10.1074/jbc.m111.322487;
RA Svensson G., Awad W., Hakansson M., Mani K., Logan D.T.;
RT "Crystal structure of N-glycosylated human glypican-1 core protein:
RT Structure of two loops evolutionarily conserved in vertebrate glypican-1.";
RL J. Biol. Chem. 287:14040-14051(2012).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-337.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate. Binds,
CC via the heparan sulfate side chains, alpha-4 (V) collagen and
CC participates in Schwann cell myelination (By similarity). May act as a
CC catalyst in increasing the rate of conversion of prion protein PRPN(C)
CC to PRNP(Sc) via associating (via the heparan sulfate side chains) with
CC both forms of PRPN, targeting them to lipid rafts and facilitating
CC their interaction. Required for proper skeletal muscle differentiation
CC by sequestering FGF2 in lipid rafts preventing its binding to receptors
CC (FGFRs) and inhibiting the FGF-mediated signaling. {ECO:0000250,
CC ECO:0000269|PubMed:19936054, ECO:0000269|PubMed:21642435}.
CC -!- INTERACTION:
CC P35052; Q6PRD1: GPR179; NbExp=2; IntAct=EBI-8307554, EBI-20895185;
CC P35052; Q8C419: Gpr158; Xeno; NbExp=3; IntAct=EBI-8307554, EBI-776313;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor;
CC Extracellular side. Endosome. Note=S-nitrosylated form recycled in
CC endosomes. Localizes to CAV1-containing vesicles close to the cell
CC surface. Cleavage of heparan sulfate side chains takes place mainly in
CC late endosomes. Associates with both forms of PRNP in lipid rafts.
CC Colocalizes with APP in perinuclear compartments and with CP in
CC intracellular compartments. Associates with fibrillar APP amyloid-beta
CC peptides in lipid rafts in Alzheimer disease brains.
CC -!- SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular
CC space.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35052-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35052-2; Sequence=VSP_055225, VSP_055226, VSP_055227;
CC -!- PTM: S-nitrosylated in a Cu(2+)-dependent manner. Nitric acid (NO) is
CC released from the nitrosylated cysteines by ascorbate or by some other
CC reducing agent, in a Cu(2+) or Zn(2+) dependent manner. This free
CC nitric oxide is then capable of cleaving the heparan sulfate side
CC chains.
CC -!- PTM: N- and O-glycosylated. N-glycosylation is mainly of the complex
CC type containing sialic acid. O-glycosylated with heparan sulfate. The
CC heparan sulfate chains can be cleaved either by the action of
CC heparanase or, degraded by a deaminative process that uses nitric oxide
CC (NO) released from the S-nitrosylated cysteines. This process is
CC triggered by ascorbate, or by some other reducing agent, in a
CC Cu(2+)- or Zn(2+) dependent manner. Cu(2+) ions are provided by
CC ceruloproteins such as APP, PRNP or CP which associate with GCP1 in
CC intracellular compartments or lipid rafts.
CC {ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:16971378,
CC ECO:0000269|PubMed:19479373, ECO:0000269|PubMed:19775117,
CC ECO:0000269|PubMed:2148568, ECO:0000269|PubMed:21642435,
CC ECO:0000269|PubMed:21932778, ECO:0000269|PubMed:22351761}.
CC -!- PTM: This cell-associated glypican is further processed to give rise to
CC a medium-released species.
CC -!- DISEASE: Note=Associates (via the heparan sulfate side chains) with
CC fibrillar APP amyloid-beta peptides in primitive and classic amyloid
CC plaques and may be involved in the deposition of these senile plaques
CC in the Alzheimer disease (AD) brain (PubMed:15084524).
CC {ECO:0000269|PubMed:15084524}.
CC -!- DISEASE: Note=Misprocessing of GPC1 is found in fibroblasts of patients
CC with Niemann-Pick Type C1 disease. This is due to the defective
CC deaminative degradation of heparan sulfate chains (PubMed:16645004).
CC {ECO:0000269|PubMed:16645004}.
CC -!- SIMILARITY: Belongs to the glypican family. {ECO:0000305}.
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DR EMBL; X54232; CAA38139.1; -; mRNA.
DR EMBL; AK095397; BAG53043.1; -; mRNA.
DR EMBL; AK096638; BAG53345.1; -; mRNA.
DR EMBL; AC110619; AAY24160.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71180.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71183.1; -; Genomic_DNA.
DR EMBL; BC051279; AAH51279.1; -; mRNA.
DR CCDS; CCDS2534.1; -. [P35052-1]
DR PIR; A36347; A36347.
DR RefSeq; NP_002072.2; NM_002081.2. [P35052-1]
DR PDB; 4ACR; X-ray; 2.55 A; A/B/C/D=24-479.
DR PDB; 4AD7; X-ray; 2.94 A; A/B/C/D=24-529.
DR PDB; 4BWE; X-ray; 2.46 A; A/B/C/D=24-479.
DR PDB; 4YWT; X-ray; 2.38 A; A/B/C/D=24-527.
DR PDBsum; 4ACR; -.
DR PDBsum; 4AD7; -.
DR PDBsum; 4BWE; -.
DR PDBsum; 4YWT; -.
DR AlphaFoldDB; P35052; -.
DR SMR; P35052; -.
DR BioGRID; 109079; 186.
DR IntAct; P35052; 30.
DR MINT; P35052; -.
DR STRING; 9606.ENSP00000264039; -.
DR GlyConnect; 1279; 2 N-Linked glycans (1 site).
DR GlyGen; P35052; 7 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P35052; -.
DR PhosphoSitePlus; P35052; -.
DR SwissPalm; P35052; -.
DR BioMuta; GPC1; -.
DR DMDM; 292495012; -.
DR EPD; P35052; -.
DR jPOST; P35052; -.
DR MassIVE; P35052; -.
DR MaxQB; P35052; -.
DR PaxDb; P35052; -.
DR PeptideAtlas; P35052; -.
DR PRIDE; P35052; -.
DR ProteomicsDB; 54976; -. [P35052-1]
DR Antibodypedia; 34516; 349 antibodies from 34 providers.
DR DNASU; 2817; -.
DR Ensembl; ENST00000264039.7; ENSP00000264039.2; ENSG00000063660.9. [P35052-1]
DR GeneID; 2817; -.
DR KEGG; hsa:2817; -.
DR MANE-Select; ENST00000264039.7; ENSP00000264039.2; NM_002081.3; NP_002072.2.
DR UCSC; uc002vyw.5; human. [P35052-1]
DR CTD; 2817; -.
DR DisGeNET; 2817; -.
DR GeneCards; GPC1; -.
DR HGNC; HGNC:4449; GPC1.
DR HPA; ENSG00000063660; Tissue enhanced (skin).
DR MalaCards; GPC1; -.
DR MIM; 600395; gene.
DR neXtProt; NX_P35052; -.
DR NIAGADS; ENSG00000063660; -.
DR OpenTargets; ENSG00000063660; -.
DR PharmGKB; PA28830; -.
DR VEuPathDB; HostDB:ENSG00000063660; -.
DR eggNOG; KOG3821; Eukaryota.
DR GeneTree; ENSGT01050000244897; -.
DR HOGENOM; CLU_024658_2_0_1; -.
DR InParanoid; P35052; -.
DR OMA; YCAHCRG; -.
DR OrthoDB; 611422at2759; -.
DR PhylomeDB; P35052; -.
DR TreeFam; TF105317; -.
DR PathwayCommons; P35052; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR Reactome; R-HSA-2024096; HS-GAG degradation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR Reactome; R-HSA-3656237; Defective EXT2 causes exostoses 2.
DR Reactome; R-HSA-3656253; Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
DR Reactome; R-HSA-376176; Signaling by ROBO receptors.
DR Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; P35052; -.
DR SIGNOR; P35052; -.
DR BioGRID-ORCS; 2817; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; GPC1; human.
DR GeneWiki; Glypican_1; -.
DR GenomeRNAi; 2817; -.
DR Pharos; P35052; Tbio.
DR PRO; PR:P35052; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P35052; protein.
DR Bgee; ENSG00000063660; Expressed in ventricular zone and 194 other tissues.
DR ExpressionAtlas; P35052; baseline and differential.
DR Genevisible; P35052; HS.
DR GO; GO:0046658; C:anchored component of plasma membrane; IEA:InterPro.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; TAS:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
DR GO; GO:0043236; F:laminin binding; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; IDA:UniProtKB.
DR GO; GO:0032288; P:myelin assembly; ISS:UniProtKB.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2001016; P:positive regulation of skeletal muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:1905475; P:regulation of protein localization to membrane; IBA:GO_Central.
DR GO; GO:0014037; P:Schwann cell differentiation; ISS:UniProtKB.
DR InterPro; IPR001863; Glypican.
DR InterPro; IPR015502; Glypican-1.
DR InterPro; IPR019803; Glypican_CS.
DR PANTHER; PTHR10822; PTHR10822; 1.
DR PANTHER; PTHR10822:SF8; PTHR10822:SF8; 1.
DR Pfam; PF01153; Glypican; 1.
DR PROSITE; PS01207; GLYPICAN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Copper;
KW Direct protein sequencing; Disulfide bond; Endosome; Glycoprotein;
KW GPI-anchor; Heparan sulfate; Lipoprotein; Membrane; Proteoglycan;
KW Reference proteome; S-nitrosylation; Secreted; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2148568"
FT CHAIN 24..530
FT /note="Glypican-1"
FT /id="PRO_0000012295"
FT CHAIN 24..?
FT /note="Secreted glypican-1"
FT /id="PRO_0000333837"
FT PROPEP 531..558
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000012296"
FT REGION 341..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 530
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000305|PubMed:2148568"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21932778,
FT ECO:0000269|PubMed:22351761"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2148568,
FT ECO:0000269|PubMed:21932778, ECO:0000269|PubMed:22351761"
FT CARBOHYD 486
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000305"
FT CARBOHYD 488
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000305"
FT CARBOHYD 490
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000305"
FT DISULFID 32..68
FT /evidence="ECO:0000269|PubMed:22351761"
FT DISULFID 62..256
FT /evidence="ECO:0000269|PubMed:22351761"
FT DISULFID 69..259
FT /evidence="ECO:0000269|PubMed:22351761"
FT DISULFID 191..343
FT /evidence="ECO:0000269|PubMed:22351761"
FT DISULFID 246..279
FT /evidence="ECO:0000269|PubMed:22351761"
FT DISULFID 268..415
FT /evidence="ECO:0000269|PubMed:22351761"
FT DISULFID 272..401
FT /evidence="ECO:0000269|PubMed:22351761"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055225"
FT VAR_SEQ 295..359
FT /note="DSMVLITDKFWGTSGVESVIGSVHTWLAEAINALQDNRDTLTAKVIQGCGNP
FT KVNPQGPGPEEKR -> GEPPPARAAWNCLGECTTGGPGGRVVPSLELGPRDLIRDALT
FT RARSGWCCRVEGPGCLLNVLSDV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055226"
FT VAR_SEQ 360..558
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055227"
FT VARIANT 337
FT /note="A -> D (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036044"
FT VARIANT 500
FT /note="S -> G (in dbSNP:rs2228331)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2148568"
FT /id="VAR_033977"
FT MUTAGEN 79
FT /note="N->Q: Protein yield reduced by half. Protein yield
FT reduced by 90%, abolishes N-glycosylation but no effect on
FT secondary structure; when associated with Q-116."
FT /evidence="ECO:0000269|PubMed:21932778"
FT MUTAGEN 116
FT /note="N->Q: No effect on protein yield. Protein yield
FT reduced by 90%, abolishes N-glycosylation but no effect on
FT secondary structure; when associated with Q-79."
FT /evidence="ECO:0000269|PubMed:21932778"
FT HELIX 33..40
FT /evidence="ECO:0007829|PDB:4YWT"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:4BWE"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4YWT"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 71..130
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 159..178
FT /evidence="ECO:0007829|PDB:4YWT"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:4YWT"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 205..237
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:4YWT"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 374..388
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 392..403
FT /evidence="ECO:0007829|PDB:4YWT"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:4YWT"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:4YWT"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:4YWT"
FT HELIX 451..472
FT /evidence="ECO:0007829|PDB:4YWT"
SQ SEQUENCE 558 AA; 61680 MW; 16553B56080A83C8 CRC64;
MELRARGWWL LCAAAALVAC ARGDPASKSR SCGEVRQIYG AKGFSLSDVP QAEISGEHLR
ICPQGYTCCT SEMEENLANR SHAELETALR DSSRVLQAML ATQLRSFDDH FQHLLNDSER
TLQATFPGAF GELYTQNARA FRDLYSELRL YYRGANLHLE ETLAEFWARL LERLFKQLHP
QLLLPDDYLD CLGKQAEALR PFGEAPRELR LRATRAFVAA RSFVQGLGVA SDVVRKVAQV
PLGPECSRAV MKLVYCAHCL GVPGARPCPD YCRNVLKGCL ANQADLDAEW RNLLDSMVLI
TDKFWGTSGV ESVIGSVHTW LAEAINALQD NRDTLTAKVI QGCGNPKVNP QGPGPEEKRR
RGKLAPRERP PSGTLEKLVS EAKAQLRDVQ DFWISLPGTL CSEKMALSTA SDDRCWNGMA
RGRYLPEVMG DGLANQINNP EVEVDITKPD MTIRQQIMQL KIMTNRLRSA YNGNDVDFQD
ASDDGSGSGS GDGCLDDLCS RKVSRKSSSS RTPLTHALPG LSEQEGQKTS AASCPQPPTF
LLPLLLFLAL TVARPRWR
