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Protein

Glypican-1

Gene

Gpc1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Cu2+ or Zn2+ ions (By similarity). Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination.By similarity2 Publications

GO - Molecular functioni

  • collagen V binding Source: RGD
  • copper ion binding Source: UniProtKB
  • fibroblast growth factor binding Source: UniProtKB
  • laminin binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Copper, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Glypican-1
Alternative name(s):
HSPG M12
Cleaved into the following chain:
Gene namesi
Name:Gpc1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61853. Gpc1.

Subcellular locationi

  • Cell membrane; Lipid-anchorGPI-anchor; Extracellular side
  • Endosome By similarity

  • 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 530507Glypican-1PRO_0000012299Add
BLAST
Chaini24 – ?Secreted glypican-1PRO_0000333839
Propeptidei531 – 55828Removed in mature formSequence analysisPRO_0000012300Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 68By similarity
Disulfide bondi62 ↔ 256By similarity
Disulfide bondi69 ↔ 259By similarity
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication
Glycosylationi116 – 1161N-linked (GlcNAc...)1 Publication
Disulfide bondi191 ↔ 343By similarity
Disulfide bondi246 ↔ 279By similarity
Disulfide bondi268 ↔ 415By similarity
Disulfide bondi272 ↔ 401By similarity
Glycosylationi486 – 4861O-linked (Xyl...) (heparan sulfate)Sequence analysis
Glycosylationi488 – 4881O-linked (Xyl...) (heparan sulfate)Sequence analysis
Glycosylationi490 – 4901O-linked (Xyl...) (heparan sulfate)Sequence analysis
Lipidationi530 – 5301GPI-anchor amidated serineSequence analysis

Post-translational modificationi

S-nitrosylated in a Cu2+-dependent manner. Nitric acid (NO) is released from the nitrosylated cysteines by ascorbate or by some other reducing agent, in a Cu2+ or Zn2+ dependent manner. This free nitric oxide is then capable of cleaving the heparan sulfate side chains.
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 Cu2+- or Zn2+ dependent manner. Cu2+ ions are provided by ceruloproteins such as APP, PRNP or CP which associate with GCP1 in intracellular compartments or lipid rafts.1 Publication
This cell-associated glypican is further processed to give rise to a medium-released species.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Heparan sulfate, Lipoprotein, Proteoglycan

Proteomic databases

PaxDbiP35053.
PRIDEiP35053.

PTM databases

UniCarbKBiP35053.

Expressioni

Tissue specificityi

Nervous system.1 Publication

Interactioni

GO - Molecular functioni

  • collagen V binding Source: RGD
  • fibroblast growth factor binding Source: UniProtKB
  • laminin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi248661. 1 interaction.
IntActiP35053. 1 interaction.
STRINGi10116.ENSRNOP00000066597.

Family & Domainsi

Sequence similaritiesi

Belongs to the glypican family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3821. Eukaryota.
ENOG410XST2. LUCA.
HOVERGENiHBG003464.
InParanoidiP35053.
KOiK08107.
PhylomeDBiP35053.

Family and domain databases

InterProiIPR001863. Glypican.
IPR015502. Glypican-1.
IPR019803. Glypican_CS.
[Graphical view]
PANTHERiPTHR10822. PTHR10822. 1 hit.
PTHR10822:SF8. PTHR10822:SF8. 1 hit.
PfamiPF01153. Glypican. 1 hit.
[Graphical view]
PROSITEiPS01207. GLYPICAN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELRARGWWL LCAAAALVAC TRGDPASKSR SCSEVRQIYG AKGFSLSDVP
60 70 80 90 100
QAEISGEHLR ICPQGYTCCT SEMEENLANH SRMELETALH DSSRALQATL
110 120 130 140 150
ATQLHGIDDH FQRLLNDSER TLQDAFPGAF GDLYTQNTRA FRDLYAELRL
160 170 180 190 200
YYRGANLHLE ETLAEFWARL LERLFKQLHP QLLLPDDYLD CLGKQAEALR
210 220 230 240 250
PFGDAPRELR LRATRAFVAA RSFVQGLGVA SDVVRKVAQV PLAPECSRAV
260 270 280 290 300
MKLVYCAHCR GVPGARPCPD YCRNVLKGCL ANQADLDAEW RNLLDSMVLI
310 320 330 340 350
TDKFWGPSGA EYVIGSVHMW LAEAINALQD NKDTLTAKVI QGCGNPKVNP
360 370 380 390 400
HGSGPEEKRR RAKLALQEKS STGTLEKLVS EAKAQLRDIQ DYWISLPGTL
410 420 430 440 450
CSEKMAMSPA SDDRCWNGIS KGRYLPEVMG DGLANQINNP EVEVDITKPD
460 470 480 490 500
MTIRQQIMQL KIMTNRLRGA YGGNDVDFQD ASDDGSGSGS GGGCPDDACG
510 520 530 540 550
RRVSKKSSSS RTPLIHALPG LSEQEGQKTS AATRPEPHYF FLLFLFTLVL

AAARPRWR
Length:558
Mass (Da):61,734
Last modified:February 1, 1994 - v1
Checksum:iE2878A854B9A1D7F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211T → A in AAA41251 (PubMed:8207484).Curated
Sequence conflicti312 – 3121Y → N in AAA41251 (PubMed:8207484).Curated
Sequence conflicti362 – 3621A → G in AAA41251 (PubMed:8207484).Curated
Sequence conflicti437 – 4371I → G AA sequence (PubMed:8207484).Curated
Sequence conflicti443 – 4431E → D AA sequence (PubMed:8207484).Curated
Sequence conflicti515 – 5151I → T in AAA41251 (PubMed:8207484).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02896 mRNA. Translation: AAA86439.1.
L34067 mRNA. Translation: AAA41251.1.
PIRiI56545.
RefSeqiNP_110455.1. NM_030828.1.
UniGeneiRn.7044.

Genome annotation databases

GeneIDi58920.
KEGGirno:58920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02896 mRNA. Translation: AAA86439.1.
L34067 mRNA. Translation: AAA41251.1.
PIRiI56545.
RefSeqiNP_110455.1. NM_030828.1.
UniGeneiRn.7044.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248661. 1 interaction.
IntActiP35053. 1 interaction.
STRINGi10116.ENSRNOP00000066597.

PTM databases

UniCarbKBiP35053.

Proteomic databases

PaxDbiP35053.
PRIDEiP35053.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi58920.
KEGGirno:58920.

Organism-specific databases

CTDi2817.
RGDi61853. Gpc1.

Phylogenomic databases

eggNOGiKOG3821. Eukaryota.
ENOG410XST2. LUCA.
HOVERGENiHBG003464.
InParanoidiP35053.
KOiK08107.
PhylomeDBiP35053.

Miscellaneous databases

PROiP35053.

Family and domain databases

InterProiIPR001863. Glypican.
IPR015502. Glypican-1.
IPR019803. Glypican_CS.
[Graphical view]
PANTHERiPTHR10822. PTHR10822. 1 hit.
PTHR10822:SF8. PTHR10822:SF8. 1 hit.
PfamiPF01153. Glypican. 1 hit.
[Graphical view]
PROSITEiPS01207. GLYPICAN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of a major heparan sulfate proteoglycan from brain and identification as the rat form of glypican."
    Karthikeyan L., Maurel P., Rauch U., Margolis R.K., Margolis R.U.
    Biochem. Biophys. Res. Commun. 188:395-401(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-55 AND 424-445.
    Tissue: Brain.
  2. "Neuronal expression of glypican, a cell-surface glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan, in the adult rat nervous system."
    Litwack E.D., Stipp C.S., Kumbasar A., Lander A.D.
    J. Neurosci. 14:3713-3724(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PROTEIN SEQUENCE OF 83-112; 196-207 AND 422-443.
    Strain: New England Deaconess Hospital.
  3. "Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in the copper/zinc-nitric oxide-dependent degradation of glypican-1 heparan sulfate in rat C6 glioma cells."
    Mani K., Cheng F., Havsmark B., David S., Fransson L.A.
    J. Biol. Chem. 279:12918-12923(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: COPPER-BINDING, GLYCOSYLATION, SUBCELLULAR LOCATION.
  4. "Constitutive release of alpha4 type V collagen N-terminal domain by Schwann cells and binding to cell surface and extracellular matrix heparan sulfate proteoglycans."
    Rothblum K., Stahl R.C., Carey D.J.
    J. Biol. Chem. 279:51282-51288(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Glypican-1 and alpha4(V) collagen are required for Schwann cell myelination."
    Chernousov M.A., Rothblum K., Stahl R.C., Evans A., Prentiss L., Carey D.J.
    J. Neurosci. 26:508-517(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiGPC1_RAT
AccessioniPrimary (citable) accession number: P35053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 8, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.