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Glypican-1 (HSPG M12) [Cleaved into: Secreted glypican-1]

 GPC1_RAT                Reviewed;         558 AA.
P35053;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
23-MAY-2018, entry version 113.
RecName: Full=Glypican-1;
AltName: Full=HSPG M12;
Contains:
RecName: Full=Secreted glypican-1;
Flags: Precursor;
Name=Gpc1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-55 AND 424-445.
TISSUE=Brain;
PubMed=1417860; DOI=10.1016/0006-291X(92)92398-H;
Karthikeyan L., Maurel P., Rauch U., Margolis R.K., Margolis R.U.;
"Cloning of a major heparan sulfate proteoglycan from brain and
identification as the rat form of glypican.";
Biochem. Biophys. Res. Commun. 188:395-401(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND PROTEIN SEQUENCE
OF 83-112; 196-207 AND 422-443.
STRAIN=New England Deaconess Hospital;
PubMed=8207484;
Litwack E.D., Stipp C.S., Kumbasar A., Lander A.D.;
"Neuronal expression of glypican, a cell-surface
glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan, in
the adult rat nervous system.";
J. Neurosci. 14:3713-3724(1994).
[3]
COPPER-BINDING, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=14707133; DOI=10.1074/jbc.M313678200;
Mani K., Cheng F., Havsmark B., David S., Fransson L.A.;
"Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in
the copper/zinc-nitric oxide-dependent degradation of glypican-1
heparan sulfate in rat C6 glioma cells.";
J. Biol. Chem. 279:12918-12923(2004).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15383532; DOI=10.1074/jbc.M408837200;
Rothblum K., Stahl R.C., Carey D.J.;
"Constitutive release of alpha4 type V collagen N-terminal domain by
Schwann cells and binding to cell surface and extracellular matrix
heparan sulfate proteoglycans.";
J. Biol. Chem. 279:51282-51288(2004).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16407548; DOI=10.1523/JNEUROSCI.2544-05.2006;
Chernousov M.A., Rothblum K., Stahl R.C., Evans A., Prentiss L.,
Carey D.J.;
"Glypican-1 and alpha4(V) collagen are required for Schwann cell
myelination.";
J. Neurosci. 26:508-517(2006).
-!- 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}.
-!- 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}.
-!- TISSUE SPECIFICITY: Nervous system. {ECO:0000269|PubMed:8207484}.
-!- 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.
-!- SIMILARITY: Belongs to the glypican family. {ECO:0000305}.
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EMBL; L02896; AAA86439.1; -; mRNA.
EMBL; L34067; AAA41251.1; -; mRNA.
PIR; I56545; I56545.
RefSeq; NP_110455.1; NM_030828.1.
UniGene; Rn.7044; -.
SMR; P35053; -.
BioGrid; 248661; 1.
IntAct; P35053; 1.
STRING; 10116.ENSRNOP00000066597; -.
iPTMnet; P35053; -.
UniCarbKB; P35053; -.
PaxDb; P35053; -.
PRIDE; P35053; -.
GeneID; 58920; -.
KEGG; rno:58920; -.
CTD; 2817; -.
RGD; 61853; Gpc1.
eggNOG; KOG3821; Eukaryota.
eggNOG; ENOG410XST2; LUCA.
HOVERGEN; HBG003464; -.
InParanoid; P35053; -.
KO; K08107; -.
PhylomeDB; P35053; -.
PRO; PR:P35053; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0046658; C:anchored component of plasma membrane; IEA:InterPro.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005578; C:proteinaceous extracellular matrix; ISS:UniProtKB.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:InterPro.
GO; GO:0043236; F:laminin binding; ISS:UniProtKB.
GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; ISS:UniProtKB.
GO; GO:0032288; P:myelin assembly; IDA:UniProtKB.
GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:2001016; P:positive regulation of skeletal muscle cell differentiation; ISS:UniProtKB.
GO; GO:0014037; P:Schwann cell differentiation; IDA:UniProtKB.
InterPro; IPR001863; Glypican.
InterPro; IPR015502; Glypican-1.
InterPro; IPR019803; Glypican_CS.
PANTHER; PTHR10822; PTHR10822; 1.
PANTHER; PTHR10822:SF8; PTHR10822:SF8; 1.
Pfam; PF01153; Glypican; 1.
PROSITE; PS01207; GLYPICAN; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Copper; Direct protein sequencing;
Disulfide bond; Endosome; Glycoprotein; GPI-anchor; Heparan sulfate;
Lipoprotein; Membrane; Proteoglycan; Reference proteome; Secreted;
Signal; Zinc.
SIGNAL 1 23 {ECO:0000269|PubMed:1417860}.
CHAIN 24 530 Glypican-1.
/FTId=PRO_0000012299.
CHAIN 24 ? Secreted glypican-1.
/FTId=PRO_0000333839.
PROPEP 531 558 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000012300.
LIPID 530 530 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:14707133}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:14707133}.
CARBOHYD 486 486 O-linked (Xyl...) (heparan sulfate)
serine. {ECO:0000255}.
CARBOHYD 488 488 O-linked (Xyl...) (heparan sulfate)
serine. {ECO:0000255}.
CARBOHYD 490 490 O-linked (Xyl...) (heparan sulfate)
serine. {ECO:0000255}.
DISULFID 32 68 {ECO:0000250}.
DISULFID 62 256 {ECO:0000250}.
DISULFID 69 259 {ECO:0000250}.
DISULFID 191 343 {ECO:0000250}.
DISULFID 246 279 {ECO:0000250}.
DISULFID 268 415 {ECO:0000250}.
DISULFID 272 401 {ECO:0000250}.
CONFLICT 21 21 T -> A (in Ref. 2; AAA41251).
{ECO:0000305}.
CONFLICT 312 312 Y -> N (in Ref. 2; AAA41251).
{ECO:0000305}.
CONFLICT 362 362 A -> G (in Ref. 2; AAA41251).
{ECO:0000305}.
CONFLICT 437 437 I -> G (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 443 443 E -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 515 515 I -> T (in Ref. 2; AAA41251).
{ECO:0000305}.
SEQUENCE 558 AA; 61734 MW; E2878A854B9A1D7F CRC64;
MELRARGWWL LCAAAALVAC TRGDPASKSR SCSEVRQIYG AKGFSLSDVP QAEISGEHLR
ICPQGYTCCT SEMEENLANH SRMELETALH DSSRALQATL ATQLHGIDDH FQRLLNDSER
TLQDAFPGAF GDLYTQNTRA FRDLYAELRL YYRGANLHLE ETLAEFWARL LERLFKQLHP
QLLLPDDYLD CLGKQAEALR PFGDAPRELR LRATRAFVAA RSFVQGLGVA SDVVRKVAQV
PLAPECSRAV MKLVYCAHCR GVPGARPCPD YCRNVLKGCL ANQADLDAEW RNLLDSMVLI
TDKFWGPSGA EYVIGSVHMW LAEAINALQD NKDTLTAKVI QGCGNPKVNP HGSGPEEKRR
RAKLALQEKS STGTLEKLVS EAKAQLRDIQ DYWISLPGTL CSEKMAMSPA SDDRCWNGIS
KGRYLPEVMG DGLANQINNP EVEVDITKPD MTIRQQIMQL KIMTNRLRGA YGGNDVDFQD
ASDDGSGSGS GGGCPDDACG RRVSKKSSSS RTPLIHALPG LSEQEGQKTS AATRPEPHYF
FLLFLFTLVL AAARPRWR


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