GPC1_BOVIN
ID GPC1_BOVIN Reviewed; 559 AA.
AC G3X745; Q2KJ65;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Glypican-1;
DE Contains:
DE RecName: Full=Secreted glypican-1;
DE Flags: Precursor;
GN Name=GPC1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}; Extracellular side {ECO:0000250}. Endosome
CC {ECO:0000250}. Note=S-nitrosylated form recycled in endosomes.
CC Localizes to CAV1-containing vesicles close to the cell surface.
CC Cleavage of heparan sulfate side chains takes place mainly in late
CC endosomes. Associates with both forms of PRNP in lipid rafts.
CC Colocalizes with APP in perinuclear compartments and with CP in
CC intracellular compartments (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular
CC space {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated (By similarity). N-glycosylation is mainly
CC of the complex type containing sialic acid. O-glycosylated with heparan
CC sulfate. The heparan sulfate chains can be cleaved either by the action
CC of heparanase or, degraded by a deaminative process that uses nitric
CC oxide (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 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Shed from the cell surface probably by further cleavage.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glypican family. {ECO:0000305}.
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DR EMBL; DAAA02009500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02009501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02009502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02009503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02009504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02009505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02009506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC105496; AAI05497.1; -; mRNA.
DR EMBL; BC153219; AAI53220.1; -; mRNA.
DR RefSeq; XP_010802238.1; XM_010803936.1.
DR RefSeq; XP_015318389.1; XM_015462903.1.
DR AlphaFoldDB; G3X745; -.
DR SMR; G3X745; -.
DR STRING; 9913.ENSBTAP00000018329; -.
DR DrugBank; DB06824; Triethylenetetramine.
DR PaxDb; G3X745; -.
DR PRIDE; G3X745; -.
DR GeneID; 518114; -.
DR KEGG; bta:518114; -.
DR CTD; 2817; -.
DR eggNOG; KOG3821; Eukaryota.
DR HOGENOM; CLU_024658_2_0_1; -.
DR InParanoid; G3X745; -.
DR OrthoDB; 611422at2759; -.
DR TreeFam; TF105317; -.
DR Proteomes; UP000009136; Unplaced.
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; IEA:InterPro.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; ISS: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; 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 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 2: Evidence at transcript level;
KW Cell membrane; Copper; Disulfide bond; Endosome; Glycoprotein; GPI-anchor;
KW Heparan sulfate; Lipoprotein; Membrane; Proteoglycan; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..530
FT /note="Glypican-1"
FT /id="PRO_0000417504"
FT CHAIN 24..?
FT /note="Secreted glypican-1"
FT /id="PRO_0000417505"
FT PROPEP 531..559
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000417506"
FT REGION 478..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 530
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT DISULFID 32..68
FT /evidence="ECO:0000250"
FT DISULFID 62..256
FT /evidence="ECO:0000250"
FT DISULFID 69..259
FT /evidence="ECO:0000250"
FT DISULFID 191..343
FT /evidence="ECO:0000250"
FT DISULFID 246..279
FT /evidence="ECO:0000250"
FT DISULFID 268..415
FT /evidence="ECO:0000250"
FT DISULFID 272..401
FT /evidence="ECO:0000250"
FT CONFLICT 554
FT /note="V -> A (in Ref. 2; AAI53220/AAI05497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 61007 MW; 5F84385ADC2EAA22 CRC64;
MELRARGWWL LYAAAVLVAC ARGDPASKSR SCGEVRQIYG AKGFSLSDVP QAEISGEHLR
ICPQGYTCCT SEMEENLANR SRAELETALL EGTRALQATL AAQQRGFDDH FQRLLNDSER
ALQEAFPGAF GELYTQNAKA FRDLYAELRL YYGGANLHLQ ETLAEFWARL LERLFRQLHP
QLLLPDDYLD CLGKQAEPLR PFGEAPRELR LRATRAFVAA RTFVQGLGVA GDVVRKVAKV
PLSPECSRAV MKLVYCAHCL GVPGARPCPD YCRNVLKGCL ANQADLDAEW RNLLDSMVLI
TDKFWGPSGA ESVVGGVHYW LAEAINALQD NSDTLTAKVI QGCGNPKVNP QGPGTEEKWP
RGKLALQERP PAGTLQKLVS EAKAQLRDAQ DFWISLPGTL CSEKLAMSSA SDERCWNGMA
KGRYLPEVMG DGLANQINNP EVEVDITKPD MTIRQQIMQL KIMTNRLRGA YNGNDLDFQD
ASDDGSGSGS GEGCPDEMCG RKVGRKSASS RTPLTHALPG LSEREGQQTS AAAPTPPQAS
PLLLLGLALA LPAVAPRGR
