GPC1_XENTR
ID GPC1_XENTR Reviewed; 554 AA.
AC Q0V9W0;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Glypican-1;
DE Contains:
DE RecName: Full=Secreted glypican-1;
DE Flags: Precursor;
GN Name=gpc1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Secreted glypican-1]: Secreted, extracellular
CC space {ECO:0000250}.
CC -!- PTM: O-glycosylated with heparan sulfate side chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glypican family. {ECO:0000305}.
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DR EMBL; AAMC01022256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAMC01022257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC121374; AAI21375.1; -; mRNA.
DR RefSeq; NP_001072316.1; NM_001078848.1.
DR AlphaFoldDB; Q0V9W0; -.
DR SMR; Q0V9W0; -.
DR STRING; 8364.ENSXETP00000006591; -.
DR PaxDb; Q0V9W0; -.
DR DNASU; 779769; -.
DR Ensembl; ENSXETT00000104077; ENSXETP00000088342; ENSXETG00000003037.
DR GeneID; 779769; -.
DR KEGG; xtr:779769; -.
DR CTD; 2817; -.
DR Xenbase; XB-GENE-964661; gpc1.
DR eggNOG; KOG3821; Eukaryota.
DR HOGENOM; CLU_024658_2_0_1; -.
DR InParanoid; Q0V9W0; -.
DR OMA; YCAHCRG; -.
DR OrthoDB; 611422at2759; -.
DR PhylomeDB; Q0V9W0; -.
DR TreeFam; TF105317; -.
DR Reactome; R-XTR-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-XTR-2022928; HS-GAG biosynthesis.
DR Reactome; R-XTR-2024096; HS-GAG degradation.
DR Reactome; R-XTR-376176; Signaling by ROBO receptors.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000003037; Expressed in testis and 9 other tissues.
DR ExpressionAtlas; Q0V9W0; baseline.
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:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0017134; F:fibroblast growth factor binding; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1905475; P:regulation of protein localization to membrane; IBA:GO_Central.
DR InterPro; IPR001863; Glypican.
DR InterPro; IPR015502; Glypican-1.
DR PANTHER; PTHR10822; PTHR10822; 1.
DR PANTHER; PTHR10822:SF8; PTHR10822:SF8; 1.
DR Pfam; PF01153; Glypican; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Heparan sulfate;
KW Lipoprotein; Membrane; Proteoglycan; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..?
FT /note="Glypican-1"
FT /id="PRO_0000417510"
FT CHAIN 22..?
FT /note="Secreted glypican-1"
FT /id="PRO_0000417511"
FT PROPEP ?..554
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000417512"
FT REGION 346..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 554 AA; 62450 MW; A975B9DF433DAE07 CRC64;
MERLCWGWWW HLGILCLMHW AAGDTGSKTK SCSEVKQVYL AKGFSLNGAP QSEISGEHLR
ICPQGYTCCT SEMEENFANI SRVEFEAKLR ESSASIQRLL TTQHRNFDSY FQDLLNTSER
VLQERFPSQY GDLYSQNSKI FRDLYSELRQ YYRGSGINLE EALIEFWSRL LERVFKAQHT
QYSFSEEYMD CLVKQYEQLK PFGDTPREVK LKAARAFIAA RSFVQGLNAA ADVVRKANQV
PMSTECARAV MKLVYCPHCR GHSSIKLCSN YCWNVMRGCL ANQADLDSEW RNLIESLLLV
ADKFNGASNV ENIVGAIHTK ISEAITHMQE NKELLTNKVF KICGTPKKTN KGSKSEERRR
KGKATQEDKS AVATMDNLIS DVKGILSDIQ DYWVSLPSLF CTEKVTAGPG NEDKCWNGIT
KGRYMPEPMG SGLANQINNP EVDVDITKPD MTIRQQIMQL KIMTSRLRNA YNGNDVDFQD
TSDDMSGSGS GDGCNEDLCG SGRKLSRETV IIQPATHAVP RQPNPGETGK GTRLSSWDLL
ICLVALLVAQ CTRW
