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Protein

Glypican-1

Gene

Gpc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Cu2+ or Zn2+ ions.By similarity4 Publications

GO - Molecular functioni

  • 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

Enzyme and pathway databases

ReactomeiR-MMU-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
R-MMU-2022928. HS-GAG biosynthesis.
R-MMU-2024096. HS-GAG degradation.
R-MMU-376176. Signaling by Robo receptor.
R-MMU-428890. Role of Abl in Robo-Slit signaling.
R-MMU-975634. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Glypican-1
Cleaved into the following chain:
Gene namesi
Name:Gpc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1194891. Gpc1.

Subcellular locationi

  • Cell membrane; Lipid-anchorGPI-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 Abeta peptides in lipid rafts in Alzheimer disease brains.

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • endosome Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • extracellular space Source: UniProtKB-SubCell
  • Golgi lumen Source: Reactome
  • membrane raft Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Null mice with induced pancreatic ductal adenocarcinomas (PDACs) exhibit attenuated pancreatic tumor growth and invasiveness, decreased cancer cell proliferation and mitogen-activated protein kinase activation. Pancreatic cancer cells isolated from the tumors of GPC1 (-/-) mice were not as invasive in response to fibroblast growth factor-2 (FGF-2) as cancer cells isolated from wild-type mice.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323By similarityAdd
BLAST
Chaini24 – 529506Glypican-1PRO_0000012297Add
BLAST
Chaini24 – ?Secreted glypican-1PRO_0000333838
Propeptidei530 – 55728Removed in mature formSequence analysisPRO_0000012298Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 68By similarity
Disulfide bondi62 ↔ 255By similarity
Disulfide bondi69 ↔ 258By similarity
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication
Glycosylationi116 – 1161N-linked (GlcNAc...)1 Publication
Disulfide bondi190 ↔ 342By similarity
Disulfide bondi245 ↔ 278By similarity
Disulfide bondi267 ↔ 414By similarity
Disulfide bondi271 ↔ 400By similarity
Glycosylationi485 – 4851O-linked (Xyl...) (heparan sulfate)Sequence analysis
Glycosylationi487 – 4871O-linked (Xyl...) (heparan sulfate)Sequence analysis
Glycosylationi489 – 4891O-linked (Xyl...) (heparan sulfate)Sequence analysis
Lipidationi529 – 5291GPI-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.1 Publication
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.5 Publications
This cell-associated glypican is further processed to give rise to a medium-released species.By similarity

Keywords - PTMi

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

Proteomic databases

MaxQBiQ9QZF2.
PaxDbiQ9QZF2.
PRIDEiQ9QZF2.

PTM databases

iPTMnetiQ9QZF2.
PhosphoSiteiQ9QZF2.

Expressioni

Gene expression databases

BgeeiENSMUSG00000034220.
CleanExiMM_GPC1.
ExpressionAtlasiQ9QZF2. baseline and differential.
GenevisibleiQ9QZF2. MM.

Interactioni

GO - Molecular functioni

  • fibroblast growth factor binding Source: UniProtKB
  • laminin binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ9QZF2. 1 interaction.
MINTiMINT-4096508.
STRINGi10090.ENSMUSP00000047199.

Structurei

3D structure databases

ProteinModelPortaliQ9QZF2.
SMRiQ9QZF2. Positions 29-474.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glypican family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3821. Eukaryota.
ENOG410XST2. LUCA.
GeneTreeiENSGT00550000074430.
HOGENOMiHOG000253003.
HOVERGENiHBG003464.
InParanoidiQ9QZF2.
KOiK08107.
OMAiMKLVYCP.
OrthoDBiEOG091G06T6.
PhylomeDBiQ9QZF2.
TreeFamiTF105317.

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.

Q9QZF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELRTRGWWL LCAAAALVVC ARGDPASKSR SCSEVRQIYG AKGFSLSDVP
60 70 80 90 100
QAEISGEHLR ICPQGYTCCT SEMEENLANH SRMELESALH DSSRALQATL
110 120 130 140 150
ATQLHGIDDH FQRLLNDSER TLQEAFPGAF GDLYTQNTRA FRDLYAELRL
160 170 180 190 200
YYRGANLHLE ETLAEFWARL LERLFKQLHP QLLPDDYLDC LGKQAEALRP
210 220 230 240 250
FGDAPRELRL RATRAFVAAR SFVQGLGVAS DVVRKVAQVP LAPECSRAIM
260 270 280 290 300
KLVYCAHCRG VPGARPCPDY CRNVLKGCLA NQADLDAEWR NLLDSMVLIT
310 320 330 340 350
DKFWGPSGAE SVIGGVHVWL AEAINALQDN KDTLTAKVIQ ACGNPKVNPH
360 370 380 390 400
GSGPEEKRRR GKLALQEKPS TGTLEKLVSE AKAQLRDIQD FWISLPGTLC
410 420 430 440 450
SEKMAMSPAS DDRCWNGISK GRYLPEVMGD GLANQINNPE VEVDITKPDM
460 470 480 490 500
TIRQQIMQLK IMTNRLRGAY GGNDVDFQDA SDDGSGSGSG GGCPDDTCGR
510 520 530 540 550
RVSKKSSSSR TPLTHALPGL SEQEGQKTSA ATCPEPHSFF LLFLVTLVLA

AARPRWR
Length:557
Mass (Da):61,360
Last modified:May 1, 2000 - v1
Checksum:i58A9A24955D16A0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF185613 mRNA. Translation: AAD56243.1.
BC062902 mRNA. Translation: AAH62902.1.
CCDSiCCDS15177.1.
RefSeqiNP_057905.1. NM_016696.4.
UniGeneiMm.297976.

Genome annotation databases

EnsembliENSMUST00000045970; ENSMUSP00000047199; ENSMUSG00000034220.
GeneIDi14733.
KEGGimmu:14733.
UCSCiuc007cbs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF185613 mRNA. Translation: AAD56243.1.
BC062902 mRNA. Translation: AAH62902.1.
CCDSiCCDS15177.1.
RefSeqiNP_057905.1. NM_016696.4.
UniGeneiMm.297976.

3D structure databases

ProteinModelPortaliQ9QZF2.
SMRiQ9QZF2. Positions 29-474.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QZF2. 1 interaction.
MINTiMINT-4096508.
STRINGi10090.ENSMUSP00000047199.

PTM databases

iPTMnetiQ9QZF2.
PhosphoSiteiQ9QZF2.

Proteomic databases

MaxQBiQ9QZF2.
PaxDbiQ9QZF2.
PRIDEiQ9QZF2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045970; ENSMUSP00000047199; ENSMUSG00000034220.
GeneIDi14733.
KEGGimmu:14733.
UCSCiuc007cbs.1. mouse.

Organism-specific databases

CTDi2817.
MGIiMGI:1194891. Gpc1.

Phylogenomic databases

eggNOGiKOG3821. Eukaryota.
ENOG410XST2. LUCA.
GeneTreeiENSGT00550000074430.
HOGENOMiHOG000253003.
HOVERGENiHBG003464.
InParanoidiQ9QZF2.
KOiK08107.
OMAiMKLVYCP.
OrthoDBiEOG091G06T6.
PhylomeDBiQ9QZF2.
TreeFamiTF105317.

Enzyme and pathway databases

ReactomeiR-MMU-1971475. A tetrasaccharide linker sequence is required for GAG synthesis.
R-MMU-2022928. HS-GAG biosynthesis.
R-MMU-2024096. HS-GAG degradation.
R-MMU-376176. Signaling by Robo receptor.
R-MMU-428890. Role of Abl in Robo-Slit signaling.
R-MMU-975634. Retinoid metabolism and transport.

Miscellaneous databases

ChiTaRSiGpc1. mouse.
PROiQ9QZF2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000034220.
CleanExiMM_GPC1.
ExpressionAtlasiQ9QZF2. baseline and differential.
GenevisibleiQ9QZF2. MM.

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...

Entry informationi

Entry nameiGPC1_MOUSE
AccessioniPrimary (citable) accession number: Q9QZF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 111 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.