GPC2_HUMAN
ID GPC2_HUMAN Reviewed; 579 AA.
AC Q8N158; A4D2A7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Glypican-2;
DE Contains:
DE RecName: Full=Secreted glypican-2;
DE Flags: Precursor;
GN Name=GPC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-200.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate. May
CC fulfill a function related to the motile behaviors of developing
CC neurons (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via heparan sulfate) with PTN; this interaction
CC promotes neurite outgrowth through binding of PTN with chondroitin
CC sulfate of proteoglycans, thereby releasing PTPRS of chondroitin
CC sulfate proteoglycans (CSPGs) and leading to binding with heparan
CC sulfate of GPC2. Interacts (heparan sulfate chain) with MDK; this
CC interaction is inhibited by heparin followed by chondroitin sulfate E;
CC this interaction induces GPC2 clustering through heparan sulfate chain;
CC this interaction induces neuronal cell adhesion and neurite outgrowth
CC (By similarity). {ECO:0000250|UniProtKB:P51653}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}; Extracellular side {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Secreted glypican-2]: Secreted, extracellular
CC space {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glypican family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK096281; BAC04745.1; -; mRNA.
DR EMBL; AL834418; CAD39080.1; -; mRNA.
DR EMBL; CH236956; EAL23846.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76578.1; -; Genomic_DNA.
DR EMBL; BC027972; AAH27972.1; -; mRNA.
DR CCDS; CCDS5689.1; -.
DR RefSeq; NP_689955.1; NM_152742.2.
DR PDB; 6WJL; X-ray; 3.30 A; E/G=23-493.
DR PDB; 7T62; EM; 21.00 A; A=19-579.
DR PDBsum; 6WJL; -.
DR PDBsum; 7T62; -.
DR AlphaFoldDB; Q8N158; -.
DR SMR; Q8N158; -.
DR BioGRID; 128766; 6.
DR IntAct; Q8N158; 1.
DR STRING; 9606.ENSP00000292377; -.
DR GlyGen; Q8N158; 5 sites.
DR iPTMnet; Q8N158; -.
DR PhosphoSitePlus; Q8N158; -.
DR BioMuta; GPC2; -.
DR DMDM; 60390116; -.
DR EPD; Q8N158; -.
DR jPOST; Q8N158; -.
DR MassIVE; Q8N158; -.
DR PaxDb; Q8N158; -.
DR PeptideAtlas; Q8N158; -.
DR PRIDE; Q8N158; -.
DR ProteomicsDB; 71563; -.
DR Antibodypedia; 61583; 125 antibodies from 22 providers.
DR DNASU; 221914; -.
DR Ensembl; ENST00000292377.4; ENSP00000292377.2; ENSG00000213420.8.
DR GeneID; 221914; -.
DR KEGG; hsa:221914; -.
DR MANE-Select; ENST00000292377.4; ENSP00000292377.2; NM_152742.3; NP_689955.1.
DR UCSC; uc003utv.3; human.
DR CTD; 221914; -.
DR DisGeNET; 221914; -.
DR GeneCards; GPC2; -.
DR HGNC; HGNC:4450; GPC2.
DR HPA; ENSG00000213420; Tissue enhanced (lymphoid tissue, skin, testis).
DR MIM; 618446; gene.
DR neXtProt; NX_Q8N158; -.
DR OpenTargets; ENSG00000213420; -.
DR PharmGKB; PA28831; -.
DR VEuPathDB; HostDB:ENSG00000213420; -.
DR eggNOG; KOG3821; Eukaryota.
DR GeneTree; ENSGT01050000244897; -.
DR HOGENOM; CLU_024658_2_1_1; -.
DR InParanoid; Q8N158; -.
DR OMA; GFHTQPI; -.
DR OrthoDB; 611422at2759; -.
DR PhylomeDB; Q8N158; -.
DR TreeFam; TF105317; -.
DR PathwayCommons; Q8N158; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR Reactome; R-HSA-2024096; HS-GAG degradation.
DR Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR Reactome; R-HSA-3656237; Defective EXT2 causes exostoses 2.
DR Reactome; R-HSA-3656253; Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
DR Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 221914; 15 hits in 1076 CRISPR screens.
DR GeneWiki; Glypican_2; -.
DR GenomeRNAi; 221914; -.
DR Pharos; Q8N158; Tbio.
DR PRO; PR:Q8N158; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8N158; protein.
DR Bgee; ENSG00000213420; Expressed in ganglionic eminence and 148 other tissues.
DR ExpressionAtlas; Q8N158; baseline and differential.
DR Genevisible; Q8N158; HS.
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:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:1905475; P:regulation of protein localization to membrane; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR GO; GO:0007224; P:smoothened signaling pathway; IBA:GO_Central.
DR InterPro; IPR001863; Glypican.
DR InterPro; IPR031181; Glypican-2.
DR InterPro; IPR019803; Glypican_CS.
DR PANTHER; PTHR10822; PTHR10822; 1.
DR PANTHER; PTHR10822:SF24; PTHR10822:SF24; 1.
DR Pfam; PF01153; Glypican; 1.
DR PROSITE; PS01207; GLYPICAN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; GPI-anchor; Heparan sulfate;
KW Lipoprotein; Membrane; Proteoglycan; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..554
FT /note="Glypican-2"
FT /id="PRO_0000012303"
FT CHAIN 24..?
FT /note="Secreted glypican-2"
FT /id="PRO_0000333841"
FT PROPEP 555..579
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012304"
FT REGION 444..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 554
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000255"
FT VARIANT 200
FT /note="D -> N (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1333017606)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036045"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:6WJL"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 71..92
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 94..129
FT /evidence="ECO:0007829|PDB:6WJL"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 160..174
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:6WJL"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6WJL"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 209..241
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:6WJL"
FT TURN 252..258
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 290..308
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 314..340
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:6WJL"
FT TURN 400..407
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 408..412
FT /evidence="ECO:0007829|PDB:6WJL"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:6WJL"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:6WJL"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:6WJL"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:6WJL"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:6WJL"
FT HELIX 476..486
FT /evidence="ECO:0007829|PDB:6WJL"
SQ SEQUENCE 579 AA; 62830 MW; 1630E3A22BB83DFA CRC64;
MSALRPLLLL LLPLCPGPGP GPGSEAKVTR SCAETRQVLG ARGYSLNLIP PALISGEHLR
VCPQEYTCCS SETEQRLIRE TEATFRGLVE DSGSFLVHTL AARHRKFDEF FLEMLSVAQH
SLTQLFSHSY GRLYAQHALI FNGLFSRLRD FYGESGEGLD DTLADFWAQL LERVFPLLHP
QYSFPPDYLL CLSRLASSTD GSLQPFGDSP RRLRLQITRT LVAARAFVQG LETGRNVVSE
ALKVPVSEGC SQALMRLIGC PLCRGVPSLM PCQGFCLNVV RGCLSSRGLE PDWGNYLDGL
LILADKLQGP FSFELTAESI GVKISEGLMY LQENSAKVSA QVFQECGPPD PVPARNRRAP
PPREEAGRLW SMVTEEERPT TAAGTNLHRL VWELRERLAR MRGFWARLSL TVCGDSRMAA
DASLEAAPCW TGAGRGRYLP PVVGGSPAEQ VNNPELKVDA SGPDVPTRRR RLQLRAATAR
MKTAALGHDL DGQDADEDAS GSGGGQQYAD DWMAGAVAPP ARPPRPPYPP RRDGSGGKGG
GGSARYNQGR SRSGGASIGF HTQTILILSL SALALLGPR
