GPC1_DANRE
ID GPC1_DANRE Reviewed; 554 AA.
AC F1QCC6; Q32LV9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Glypican-1;
DE Contains:
DE RecName: Full=Secreted glypican-1;
DE Flags: Precursor;
GN Name=gpc1; ORFNames=zgc:122977;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate.
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; BX322595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109411; AAI09412.1; -; mRNA.
DR RefSeq; NP_001032450.1; NM_001037373.1.
DR AlphaFoldDB; F1QCC6; -.
DR SMR; F1QCC6; -.
DR STRING; 7955.ENSDARP00000106138; -.
DR PaxDb; F1QCC6; -.
DR GeneID; 553367; -.
DR KEGG; dre:553367; -.
DR CTD; 553367; -.
DR ZFIN; ZDB-GENE-051120-147; gpc1a.
DR eggNOG; KOG3821; Eukaryota.
DR InParanoid; F1QCC6; -.
DR OrthoDB; 611422at2759; -.
DR Reactome; R-DRE-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-DRE-2022928; HS-GAG biosynthesis.
DR Reactome; R-DRE-2024096; HS-GAG degradation.
DR Reactome; R-DRE-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-DRE-376176; Signaling by ROBO receptors.
DR Reactome; R-DRE-975634; Retinoid metabolism and transport.
DR PRO; PR:F1QCC6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0061009; P:common bile duct development; IMP:ZFIN.
DR GO; GO:0035622; P:intrahepatic bile duct development; IMP:ZFIN.
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 InterPro; IPR019803; Glypican_CS.
DR PANTHER; PTHR10822; PTHR10822; 1.
DR PANTHER; PTHR10822:SF8; PTHR10822:SF8; 1.
DR Pfam; PF01153; Glypican; 1.
DR PROSITE; PS01207; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..?
FT /note="Glypican-1"
FT /id="PRO_0000417507"
FT CHAIN 19..?
FT /note="Secreted glypican-1"
FT /id="PRO_0000417508"
FT PROPEP ?..554
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000417509"
FT CARBOHYD 490
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT DISULFID 29..65
FT /evidence="ECO:0000250"
FT DISULFID 59..255
FT /evidence="ECO:0000250"
FT DISULFID 66..258
FT /evidence="ECO:0000250"
FT DISULFID 190..342
FT /evidence="ECO:0000250"
FT DISULFID 245..278
FT /evidence="ECO:0000250"
FT DISULFID 267..419
FT /evidence="ECO:0000250"
FT DISULFID 271..406
FT /evidence="ECO:0000250"
FT CONFLICT 113
FT /note="N -> D (in Ref. 2; AAI09412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 61296 MW; 348F22E35472AED4 CRC64;
MDLTAVALLV SLVSVSLSAE NAGGKARSCT DVRQFYSGKG FTLNGVPQSE ISGEHLRICP
QGYTCCTSAM EETLSNLSRR EFEGLVREAG RSIQALLNAQ YRTFDTYFLE LLNGSERWLE
EAFVAALGEL YRLNAGVFRD LYAELHRYYS GASLNLEEAL DEFWMKLLER LLKASDPETA
SLLSDDFLDC ASKQTETLRP FGDAPRELKA KLVRAFIAAR AFVQGLNAAG EIVRKVSQVP
LSPECNRAIM KLVYCPHCRG LGSVKPCINY CKNVMKGCLA NQADLDTEWQ SLIETMLQVA
SSFGAEPSMD TVIYSIPVRI SEAVLAMQEN MEIYTSKVFK ACGDRGEEGT PSSISEEPKK
KERTVTALEY KPSPKSAARL EVQVTDVYSK LKEMQLYWIQ LPSALCSGKT ASSTTGDKCW
NGITKASYLP EVMGDGLANQ INNPEVEIDI TKPDRTIRQQ IMLLKIMSNR LKNALEGNDV
DFQDTSDDFS GSGSGMCADH LCVRGRPPVF GPKTDRPKLY ATGPENKRVK GSGNQIQPSF
ILLIVFFVSL LLRR
