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Glypican-3 (GTR2-2) (Intestinal protein OCI-5) (MXR7) [Cleaved into: Secreted glypican-3]

 GPC3_HUMAN              Reviewed;         580 AA.
P51654; C9JLE3; G3V1R0; Q2L880; Q2L882;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
10-OCT-2018, entry version 172.
RecName: Full=Glypican-3;
AltName: Full=GTR2-2;
AltName: Full=Intestinal protein OCI-5;
AltName: Full=MXR7;
Contains:
RecName: Full=Glypican-3 alpha subunit {ECO:0000303|PubMed:14610063};
Contains:
RecName: Full=Glypican-3 beta subunit {ECO:0000303|PubMed:14610063};
Flags: Precursor;
Name=GPC3; Synonyms=OCI5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9021160; DOI=10.1007/s003359900357;
Shen T., Sonoda G., Hamid J., Li M., Filmus J., Buick R.N.,
Testa J.R.;
"Mapping of the Simpson-Golabi-Behmel overgrowth syndrome gene (GPC3)
to chromosome X in human and rat by fluorescence in situ
hybridization.";
Mamm. Genome 8:72-72(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE
SPECIFICITY, AND DISEASE.
TISSUE=Embryo;
PubMed=8589713; DOI=10.1038/ng0396-241;
Pilia G., Hughes-Benzie R.M., Mackenzie A., Baybayan P., Chen E.Y.,
Huber R., Neri G., Cao A., Forabosco A., Schlessinger D.;
"Mutations in GPC3, a glypican gene, cause the Simpson-Golabi-Behmel
overgrowth syndrome.";
Nat. Genet. 12:241-247(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9133586; DOI=10.1016/S0378-1119(96)00689-0;
Lage H., Dietel M.;
"Cloning and characterization of human cDNAs encoding a protein with
high homology to rat intestinal development protein OCI-5.";
Gene 188:151-156(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND VARIANT MET-429.
Grozdanov P.N., Yovchev M.I., Dabeva M.D.;
"Expression of the Glypican-3 protein in hepatoma cells.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
PubMed=9339360; DOI=10.1006/geno.1997.4916;
Huber R., Crisponi L., Mazzarella R., Chen C.N., Su Y., Shizuya H.,
Chen E.Y., Cao A., Pilia G.;
"Analysis of exon/intron structure and 400 kb of genomic sequence
surrounding the 5'-promoter and 3'-terminal ends of the human glypican
3 (GPC3) gene.";
Genomics 45:48-58(1997).
[8]
MARKER FOR HEPATOCELLULAR CARCINOMA.
PubMed=12851874;
Capurro M., Wanless I.R., Sherman M., Deboer G., Shi W., Miyoshi E.,
Filmus J.;
"Glypican-3: a novel serum and histochemical marker for hepatocellular
carcinoma.";
Gastroenterology 125:89-97(2003).
[9]
FUNCTION, SUBUNIT, INTERACTION WITH WNT5A, SUBCELLULAR LOCATION,
GLYCOSYLATION, CLEAVAGE, AND MUTAGENESIS OF 355-ARG--ARG-358;
370-LYS--LYS-374; 387-ARG--ARG-389 AND 394-LYS--LYS-396.
PubMed=14610063; DOI=10.1083/jcb.200302152;
De Cat B., Muyldermans S.Y., Coomans C., Degeest G.,
Vanderschueren B., Creemers J., Biemar F., Peers B., David G.;
"Processing by proprotein convertases is required for glypican-3
modulation of cell survival, Wnt signaling, and gastrulation
movements.";
J. Cell Biol. 163:625-635(2003).
[10]
PROTEIN SEQUENCE OF 359-367.
PubMed=15059894;
Hippo Y., Watanabe K., Watanabe A., Midorikawa Y., Yamamoto S.,
Ihara S., Tokita S., Iwanari H., Ito Y., Nakano K., Nezu J.,
Tsunoda H., Yoshino T., Ohizumi I., Tsuchiya M., Ohnishi S.,
Makuuchi M., Hamakubo T., Kodama T., Aburatani H.;
"Identification of soluble NH2-terminal fragment of glypican-3 as a
serological marker for early-stage hepatocellular carcinoma.";
Cancer Res. 64:2418-2423(2004).
[11]
ROLE IN HEPATOCELLULAR CARCINOMA GROWTH.
PubMed=16024626; DOI=10.1158/0008-5472.CAN-04-4244;
Capurro M.I., Xiang Y.Y., Lobe C., Filmus J.;
"Glypican-3 promotes the growth of hepatocellular carcinoma by
stimulating canonical Wnt signaling.";
Cancer Res. 65:6245-6254(2005).
[12]
FUNCTION, INTERACTION WITH WNT3A AND WNT7B, MUTAGENESIS OF
355-ARG--ARG-358, AND ROLE IN HEPATOCELLULAR CARCINOMA GROWTH.
PubMed=16227623; DOI=10.1074/jbc.M507004200;
Capurro M.I., Shi W., Sandal S., Filmus J.;
"Processing by convertases is not required for glypican-3-induced
stimulation of hepatocellular carcinoma growth.";
J. Biol. Chem. 280:41201-41206(2005).
[13]
FUNCTION, AND INTERACTION WITH DPP4.
PubMed=17549790; DOI=10.1002/pmic.200600654;
Davoodi J., Kelly J., Gendron N.H., MacKenzie A.E.;
"The Simpson-Golabi-Behmel syndrome causative glypican-3, binds to and
inhibits the dipeptidyl peptidase activity of CD26.";
Proteomics 7:2300-2310(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
FUNCTION, AND INTERACTION WITH FZD4; FZD7 AND FZD8.
PubMed=24496449; DOI=10.1242/jcs.140871;
Capurro M., Martin T., Shi W., Filmus J.;
"Glypican-3 binds to Frizzled and plays a direct role in the
stimulation of canonical Wnt signaling.";
J. Cell Sci. 127:1565-1575(2014).
[16]
PHOSPHORYLATION AT SER-352.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[17]
CLEAVAGE, AND MUTAGENESIS OF 355-ARG--ARG-358.
PubMed=25653284; DOI=10.1074/jbc.M114.612705;
Capurro M., Shi W., Izumikawa T., Kitagawa H., Filmus J.;
"Processing by convertases is required for glypican-3-induced
inhibition of Hedgehog signaling.";
J. Biol. Chem. 290:7576-7585(2015).
[18]
GLYCOSYLATION AT ASN-124; ASN-241 AND ASN-418, PYROGLUTAMATE FORMATION
AT GLN-25, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=29345911; DOI=10.1021/acs.biochem.7b01208;
Saad A., Liet B., Joucla G., Santarelli X., Charpentier J.,
Claverol S., Grosset C.F., Trezeguet V.;
"Role of glycanation and convertase maturation of soluble glypican-3
in inhibiting proliferation of hepatocellular carcinoma cells.";
Biochemistry 57:1201-1211(2018).
[19]
VARIANT SGBS1 ARG-296.
PubMed=10814714; DOI=10.1093/hmg/9.9.1321;
Veugelers M., Cat B.D., Muyldermans S.Y., Reekmans G., Delande N.,
Frints S., Legius E., Fryns J.-P., Schrander-Stumpel C., Weidle B.,
Magdalena N., David G.;
"Mutational analysis of the GPC3/GPC4 glypican gene cluster on Xq26 in
patients with Simpson-Golabi-Behmel syndrome: identification of loss-
of-function mutations in the GPC3 gene.";
Hum. Mol. Genet. 9:1321-1328(2000).
-!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate
(PubMed:14610063). Negatively regulates the hedgehog signaling
pathway when attached via the GPI-anchor to the cell surface by
competing with the hedgehog receptor PTC1 for binding to hedgehog
proteins (By similarity). Binding to the hedgehog protein SHH
triggers internalization of the complex by endocytosis and its
subsequent lysosomal degradation (By similarity). Positively
regulates the canonical Wnt signaling pathway by binding to the
Wnt receptor Frizzled and stimulating the binding of the Frizzled
receptor to Wnt ligands (PubMed:16227623, PubMed:24496449).
Positively regulates the non-canonical Wnt signaling pathway (By
similarity). Binds to CD81 which decreases the availability of
free CD81 for binding to the transcriptional repressor HHEX,
resulting in nuclear translocation of HHEX and transcriptional
repression (By similarity). Inhibits the dipeptidyl peptidase
activity of DPP4 (PubMed:17549790). Plays a role in limb
patterning and skeletal development by controlling the cellular
response to BMP4 (By similarity). Modulates the effects of growth
factors BMP2, BMP7 and FGF7 on renal branching morphogenesis (By
similarity). Required for coronary vascular development (By
similarity). Plays a role in regulating cell movements during
gastrulation (By similarity). {ECO:0000250|UniProtKB:Q6V9Y8,
ECO:0000250|UniProtKB:Q8CFZ4, ECO:0000269|PubMed:14610063,
ECO:0000269|PubMed:16227623, ECO:0000269|PubMed:17549790,
ECO:0000269|PubMed:24496449}.
-!- SUBUNIT: Heterodimer; disulfide-linked (PubMed:14610063). Cleavage
by a furin-like convertase results in production of alpha and beta
chains which form a disulfide-linked heterodimer
(PubMed:14610063). Interacts with DPP4 (PubMed:17549790).
Interacts with FGF2 (By similarity). Interacts with WNT5A
(PubMed:14610063). Also interacts with WNT3A and WNT7B
(PubMed:16227623). Interacts with hedgehog protein SHH; the
heparan sulfate chains are not required for the interaction (By
similarity). Also interacts with hedgehog protein IHH (By
similarity). Interacts with CD81 (By similarity). Interacts with
Wnt receptors FZD4, FZD7 and FZD8; the heparan sulfate chains are
required for the interaction (PubMed:24496449).
{ECO:0000250|UniProtKB:P13265, ECO:0000250|UniProtKB:Q8CFZ4,
ECO:0000269|PubMed:14610063, ECO:0000269|PubMed:16227623,
ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:24496449}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14610063};
Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P13265};
Extracellular side {ECO:0000250|UniProtKB:P13265}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P51654-1; Sequence=Displayed;
Name=2; Synonyms=Variant B;
IsoId=P51654-2; Sequence=VSP_046117;
Name=3; Synonyms=Variant C;
IsoId=P51654-3; Sequence=VSP_046703;
-!- TISSUE SPECIFICITY: Highly expressed in lung, liver and kidney.
{ECO:0000269|PubMed:8589713}.
-!- PTM: O-glycosylated; contains heparan sulfate.
{ECO:0000269|PubMed:14610063}.
-!- PTM: Cleaved intracellularly by a furin-like convertase to
generate 2 subunits, alpha and beta, which remain associated
through disulfide bonds and are associated with the cell surface
via the GPI-anchor (PubMed:14610063). This processing is essential
for its role in inhibition of hedgehog signaling
(PubMed:25653284). A second proteolytic event may result in
cleavage of the protein on the cell surface, separating it from
the GPI-anchor and leading to its shedding from the cell surface
(PubMed:14610063). {ECO:0000269|PubMed:14610063,
ECO:0000269|PubMed:25653284}.
-!- DISEASE: Simpson-Golabi-Behmel syndrome 1 (SGBS1) [MIM:312870]: A
condition characterized by pre- and postnatal overgrowth
(gigantism), facial dysmorphism and a variety of inconstant
visceral and skeletal malformations. Characteristic dysmorphic
features include macrocephaly with coarse, distinctive facies with
a large protruding jaw, broad nasal bridge and cleft palate.
Cardiac defects are frequent. {ECO:0000269|PubMed:10814714}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Used as a marker for hepatocellular carcinoma (HCC)
as it is expressed in HCC but is not detectable in hepatocytes
from normal or benign liver diseases (PubMed:12851874). When
attached to the cell surface, stimulates the growth of HCC cells
by increasing canonical Wnt signaling (PubMed:16024626). Cleavage
is not required for stimulation of Wnt signaling or HCC growth
(PubMed:16227623). {ECO:0000269|PubMed:12851874,
ECO:0000269|PubMed:16024626, ECO:0000269|PubMed:16227623}.
-!- SIMILARITY: Belongs to the glypican family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GPC3ID156.html";
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EMBL; U50410; AAA93471.1; -; mRNA.
EMBL; L47124; AAA98131.1; -; Genomic_DNA.
EMBL; L47125; AAA98132.1; -; mRNA.
EMBL; L47176; AAB58806.1; -; mRNA.
EMBL; Z37987; CAA86069.1; -; mRNA.
EMBL; DQ349136; ABC72125.1; -; mRNA.
EMBL; DQ349138; ABC72127.1; -; mRNA.
EMBL; AL008712; CAI43110.1; -; Genomic_DNA.
EMBL; AC002420; CAI43110.1; JOINED; Genomic_DNA.
EMBL; AF003529; CAI43110.1; JOINED; Genomic_DNA.
EMBL; AL009174; CAI43110.1; JOINED; Genomic_DNA.
EMBL; Z99570; CAI43110.1; JOINED; Genomic_DNA.
EMBL; AL009174; CAI42761.1; -; Genomic_DNA.
EMBL; AC002420; CAI42761.1; JOINED; Genomic_DNA.
EMBL; AF003529; CAI42761.1; JOINED; Genomic_DNA.
EMBL; AL008712; CAI42761.1; JOINED; Genomic_DNA.
EMBL; Z99570; CAI42761.1; JOINED; Genomic_DNA.
EMBL; Z99570; CAI42277.1; -; Genomic_DNA.
EMBL; AC002420; CAI42277.1; JOINED; Genomic_DNA.
EMBL; AF003529; CAI42277.1; JOINED; Genomic_DNA.
EMBL; AL008712; CAI42277.1; JOINED; Genomic_DNA.
EMBL; AL009174; CAI42277.1; JOINED; Genomic_DNA.
EMBL; AL034401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z97196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471107; EAX11771.1; -; Genomic_DNA.
EMBL; AF003529; AAB87062.1; -; Genomic_DNA.
CCDS; CCDS14638.1; -. [P51654-1]
CCDS; CCDS55495.1; -. [P51654-2]
CCDS; CCDS55496.1; -. [P51654-3]
RefSeq; NP_001158089.1; NM_001164617.1. [P51654-3]
RefSeq; NP_001158091.1; NM_001164619.1. [P51654-2]
RefSeq; NP_004475.1; NM_004484.3. [P51654-1]
UniGene; Hs.644108; -.
ProteinModelPortal; P51654; -.
SMR; P51654; -.
BioGrid; 108983; 24.
DIP; DIP-61509N; -.
IntAct; P51654; 5.
STRING; 9606.ENSP00000377836; -.
iPTMnet; P51654; -.
PhosphoSitePlus; P51654; -.
BioMuta; GPC3; -.
DMDM; 1708022; -.
MaxQB; P51654; -.
PaxDb; P51654; -.
PeptideAtlas; P51654; -.
PRIDE; P51654; -.
ProteomicsDB; 56359; -.
TopDownProteomics; P51654-1; -. [P51654-1]
DNASU; 2719; -.
Ensembl; ENST00000370818; ENSP00000359854; ENSG00000147257. [P51654-1]
Ensembl; ENST00000394299; ENSP00000377836; ENSG00000147257. [P51654-3]
Ensembl; ENST00000631057; ENSP00000486325; ENSG00000147257. [P51654-2]
GeneID; 2719; -.
KEGG; hsa:2719; -.
UCSC; uc004exe.4; human. [P51654-1]
CTD; 2719; -.
DisGeNET; 2719; -.
EuPathDB; HostDB:ENSG00000147257.13; -.
GeneCards; GPC3; -.
GeneReviews; GPC3; -.
HGNC; HGNC:4451; GPC3.
HPA; HPA006316; -.
MalaCards; GPC3; -.
MIM; 300037; gene.
MIM; 312870; phenotype.
neXtProt; NX_P51654; -.
OpenTargets; ENSG00000147257; -.
Orphanet; 373; Simpson-Golabi-Behmel syndrome.
PharmGKB; PA28832; -.
eggNOG; KOG3821; Eukaryota.
eggNOG; ENOG410XST2; LUCA.
GeneTree; ENSGT00550000074430; -.
HOGENOM; HOG000049177; -.
HOVERGEN; HBG005896; -.
InParanoid; P51654; -.
KO; K08109; -.
OMA; MNPGLPE; -.
OrthoDB; EOG091G06T6; -.
PhylomeDB; P51654; -.
TreeFam; TF105317; -.
Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
Reactome; R-HSA-2022928; HS-GAG biosynthesis.
Reactome; R-HSA-2024096; HS-GAG degradation.
Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
Reactome; R-HSA-3656237; Defective EXT2 causes exostoses 2.
Reactome; R-HSA-3656253; Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SignaLink; P51654; -.
SIGNOR; P51654; -.
ChiTaRS; GPC3; human.
GeneWiki; Glypican_3; -.
GenomeRNAi; 2719; -.
PRO; PR:P51654; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000147257; Expressed in 172 organ(s), highest expression level in kidney.
CleanEx; HS_GPC3; -.
ExpressionAtlas; P51654; baseline and differential.
Genevisible; P51654; HS.
GO; GO:0046658; C:anchored component of plasma membrane; ISS:UniProtKB.
GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0031226; C:intrinsic component of plasma membrane; TAS:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0060422; F:peptidyl-dipeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
GO; GO:0010171; P:body morphogenesis; IEA:Ensembl.
GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0042074; P:cell migration involved in gastrulation; ISS:UniProtKB.
GO; GO:0072111; P:cell proliferation involved in kidney development; ISS:UniProtKB.
GO; GO:0072203; P:cell proliferation involved in metanephros development; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0060976; P:coronary vasculature development; ISS:UniProtKB.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome.
GO; GO:0006027; P:glycosaminoglycan catabolic process; TAS:Reactome.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0072138; P:mesenchymal cell proliferation involved in ureteric bud development; ISS:UniProtKB.
GO; GO:0072180; P:mesonephric duct morphogenesis; ISS:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0045926; P:negative regulation of growth; IEA:Ensembl.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0045807; P:positive regulation of endocytosis; ISS:UniProtKB.
GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
GO; GO:2000050; P:regulation of non-canonical Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
InterPro; IPR001863; Glypican.
InterPro; IPR015501; Glypican-3.
InterPro; IPR019803; Glypican_CS.
PANTHER; PTHR10822; PTHR10822; 1.
PANTHER; PTHR10822:SF4; PTHR10822:SF4; 1.
Pfam; PF01153; Glypican; 1.
PROSITE; PS01207; GLYPICAN; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; GPI-anchor; Heparan sulfate; Lipoprotein; Membrane;
Phosphoprotein; Protease inhibitor; Proteoglycan;
Pyrrolidone carboxylic acid; Reference proteome; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:29345911}.
CHAIN 25 358 Glypican-3 alpha subunit.
{ECO:0000305|PubMed:14610063}.
/FTId=PRO_0000445410.
CHAIN 359 554 Glypican-3 beta subunit.
{ECO:0000305|PubMed:14610063}.
/FTId=PRO_0000445411.
PROPEP 555 580 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000012310.
SITE 358 359 Cleavage. {ECO:0000269|PubMed:14610063,
ECO:0000269|PubMed:15059894}.
MOD_RES 25 25 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:29345911}.
MOD_RES 352 352 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
LIPID 554 554 GPI-anchor amidated asparagine.
{ECO:0000255}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:29345911}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:29345911}.
CARBOHYD 418 418 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:29345911}.
CARBOHYD 495 495 O-linked (Xyl...) (heparan sulfate)
serine. {ECO:0000255}.
CARBOHYD 509 509 O-linked (Xyl...) (heparan sulfate)
serine. {ECO:0000255}.
DISULFID 35 72 {ECO:0000250|UniProtKB:P35052}.
DISULFID 65 262 {ECO:0000250|UniProtKB:P35052}.
DISULFID 73 265 {ECO:0000250|UniProtKB:P35052}.
DISULFID 197 349 {ECO:0000250|UniProtKB:P35052}.
DISULFID 252 285 {ECO:0000250|UniProtKB:P35052}.
DISULFID 274 422 Interchain (between alpha and beta
chains). {ECO:0000250|UniProtKB:P35052}.
DISULFID 278 410 Interchain (between alpha and beta
chains). {ECO:0000250|UniProtKB:P35052}.
VAR_SEQ 59 112 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_046117.
VAR_SEQ 344 344 T -> TETEKKIWHFKYPIFFLCIGLDLQ (in isoform
3). {ECO:0000303|Ref.4}.
/FTId=VSP_046703.
VARIANT 296 296 W -> R (in SGBS1; dbSNP:rs104894854).
{ECO:0000269|PubMed:10814714}.
/FTId=VAR_021385.
VARIANT 429 429 V -> M (in dbSNP:rs11539789).
{ECO:0000269|Ref.4}.
/FTId=VAR_069139.
MUTAGEN 355 358 RQYR->AQYA: Abolishes proteolytic
processing. Abolishes interaction with
WNT5A and ability to regulate Wnt
signaling. Increases binding of hedgehog
protein SHH to the PTC1 receptor and
abolishes ability to inhibit hedgehog
signaling. {ECO:0000269|PubMed:14610063,
ECO:0000269|PubMed:16227623,
ECO:0000269|PubMed:25653284}.
MUTAGEN 355 355 R->A: No effect on proteolytic
processing.
{ECO:0000269|PubMed:14610063}.
MUTAGEN 358 358 R->A: No effect on proteolytic
processing.
{ECO:0000269|PubMed:14610063}.
MUTAGEN 371 374 KVLK->AVLA: No effect on proteolytic
processing.
{ECO:0000269|PubMed:14610063}.
MUTAGEN 387 389 RRR->AAA: No effect on proteolytic
processing.
{ECO:0000269|PubMed:14610063}.
MUTAGEN 394 396 KLK->ALA: No effect on proteolytic
processing.
{ECO:0000269|PubMed:14610063}.
SEQUENCE 580 AA; 65563 MW; 19485B76D3CE15FC CRC64;
MAGTVRTACL VVAMLLSLDF PGQAQPPPPP PDATCHQVRS FFQRLQPGLK WVPETPVPGS
DLQVCLPKGP TCCSRKMEEK YQLTARLNME QLLQSASMEL KFLIIQNAAV FQEAFEIVVR
HAKNYTNAMF KNNYPSLTPQ AFEFVGEFFT DVSLYILGSD INVDDMVNEL FDSLFPVIYT
QLMNPGLPDS ALDINECLRG ARRDLKVFGN FPKLIMTQVS KSLQVTRIFL QALNLGIEVI
NTTDHLKFSK DCGRMLTRMW YCSYCQGLMM VKPCGGYCNV VMQGCMAGVV EIDKYWREYI
LSLEELVNGM YRIYDMENVL LGLFSTIHDS IQYVQKNAGK LTTTIGKLCA HSQQRQYRSA
YYPEDLFIDK KVLKVAHVEH EETLSSRRRE LIQKLKSFIS FYSALPGYIC SHSPVAENDT
LCWNGQELVE RYSQKAARNG MKNQFNLHEL KMKGPEPVVS QIIDKLKHIN QLLRTMSMPK
GRVLDKNLDE EGFESGDCGD DEDECIGGSG DGMIKVKNQL RFLAELAYDL DVDDAPGNSQ
QATPKDNEIS TFHNLGNVHS PLKLLTSMAI SVVCFFFLVH


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