GPC2_RAT
ID GPC2_RAT Reviewed; 579 AA.
AC P51653;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glypican-2;
DE AltName: Full=Cerebroglycan;
DE AltName: Full=HSPG M13;
DE Contains:
DE RecName: Full=Secreted glypican-2;
DE Flags: Precursor;
GN Name=Gpc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8294498; DOI=10.1083/jcb.124.1.149;
RA Stipp C.S., Litwack E.D., Lander A.D.;
RT "Cerebroglycan: an integral membrane heparan sulfate proteoglycan that is
RT unique to the developing nervous system and expressed specifically during
RT neuronal differentiation.";
RL J. Cell Biol. 124:149-160(1994).
RN [2]
RP INTERACTION WITH MDK.
RX PubMed=12084985; DOI=10.1023/a:1016042303253;
RA Kurosawa N., Chen G.Y., Kadomatsu K., Ikematsu S., Sakuma S., Muramatsu T.;
RT "Glypican-2 binds to midkine: the role of glypican-2 in neuronal cell
RT adhesion and neurite outgrowth.";
RL Glycoconj. J. 18:499-507(2001).
RN [3]
RP INTERACTION WITH PTN.
RX PubMed=27671118; DOI=10.1038/srep33916;
RA Paveliev M., Fenrich K.K., Kislin M., Kuja-Panula J., Kulesskiy E.,
RA Varjosalo M., Kajander T., Mugantseva E., Ahonen-Bishopp A., Khiroug L.,
RA Kulesskaya N., Rougon G., Rauvala H.;
RT "HB-GAM (pleiotrophin) reverses inhibition of neural regeneration by the
RT CNS extracellular matrix.";
RL Sci. Rep. 6:33916-33916(2016).
CC -!- FUNCTION: Cell surface proteoglycan that bears heparan sulfate. May
CC fulfill a function related to the motile behaviors of developing
CC neurons.
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 (PubMed:12084985). {ECO:0000269|PubMed:12084985,
CC ECO:0000269|PubMed:27671118}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor;
CC Extracellular side.
CC -!- SUBCELLULAR LOCATION: [Secreted glypican-2]: Secreted, extracellular
CC space {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Nervous system.
CC -!- DEVELOPMENTAL STAGE: Widely and transiently expressed by immature
CC neurons, appearing around the time of final mitosis and disappearing
CC after cell migration and axon outgrowth have been completed.
CC -!- SIMILARITY: Belongs to the glypican family. {ECO:0000305}.
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DR EMBL; L20468; AAA40961.1; -; mRNA.
DR PIR; A49649; A49649.
DR RefSeq; NP_612520.1; NM_138511.1.
DR AlphaFoldDB; P51653; -.
DR SMR; P51653; -.
DR STRING; 10116.ENSRNOP00000001849; -.
DR GlyGen; P51653; 5 sites.
DR PaxDb; P51653; -.
DR PRIDE; P51653; -.
DR Ensembl; ENSRNOT00000001849; ENSRNOP00000001849; ENSRNOG00000001367.
DR GeneID; 171517; -.
DR KEGG; rno:171517; -.
DR UCSC; RGD:621363; rat.
DR CTD; 221914; -.
DR RGD; 621363; Gpc2.
DR eggNOG; KOG3821; Eukaryota.
DR GeneTree; ENSGT01050000244897; -.
DR HOGENOM; CLU_024658_2_1_1; -.
DR InParanoid; P51653; -.
DR OMA; GFHTQPI; -.
DR OrthoDB; 611422at2759; -.
DR PhylomeDB; P51653; -.
DR TreeFam; TF105317; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022928; HS-GAG biosynthesis.
DR Reactome; R-RNO-2024096; HS-GAG degradation.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:P51653; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001367; Expressed in testis and 18 other tissues.
DR Genevisible; P51653; RN.
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; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; TAS:RGD.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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; IDA:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA: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; IMP:RGD.
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 Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Heparan sulfate; Lipoprotein; Membrane; Proteoglycan; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..556
FT /note="Glypican-2"
FT /id="PRO_0000012307"
FT CHAIN 22..?
FT /note="Secreted glypican-2"
FT /id="PRO_0000333843"
FT PROPEP 557..579
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012308"
FT REGION 347..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 556
FT /note="GPI-anchor amidated serine"
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 498
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 CONFLICT 377
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="P -> PP (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 63354 MW; 7C324001311D36A5 CRC64;
MSAVRPLLLL LLPLCPGPGP GHGSEAKVVR SCAETRQVLG ARGYSLNLIP PSLISGEHLQ
ICPQEYTCCS SETEQKLIRD AEVTFRGLVE DSGSFLIHTL AARHRKFNEF FREMLSISQH
SLAQLFSHSY GRLYSQHAVI FNSLFSGLRD YYEKSGEGLD DTLADFWAQL LERAFPLLHP
QYSFPPDFLL CLTRLTSTAD GSLQPFGDSP RRLRLQITRA LVAARALVQG LETGRNVVSE
ALKVPMLEGC RQALMRLIGC PLCRGVPSLM PCRGFCLNVA HGCLSSRGLE PEWGGYLDGL
LLLAEKLQGP FSFELAAESI GVKISEGLMH LQENSVKVSA KVFQECGTPH PVQSRNRRAP
APREETSRSW RSSAEEERPT TAAGTNLHRL VWELRERLSR VRGFWAGLPV TVCGDSRMAA
DLSQEAAPCW TGVGRGRYMS PVVVGSLNEQ LHNPELDTSS PDVPTRRRRL HLRAATARMK
AAALGQDLDM HDADEDASGS GGGQQYADDW KAGAAPVVPP ARPPRPPRPP RRDGLGVRGG
SGSARYNQGR SRNLGSSVGL HAPRVFILLP SALTLLGLR
