GPC2_MOUSE
ID GPC2_MOUSE Reviewed; 579 AA.
AC Q8BKV1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glypican-2;
DE Contains:
DE RecName: Full=Secreted glypican-2;
DE Flags: Precursor;
GN Name=Gpc2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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).
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}.
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DR EMBL; AK049639; BAC33852.1; -; mRNA.
DR EMBL; BC083180; AAH83180.1; -; mRNA.
DR CCDS; CCDS19799.1; -.
DR RefSeq; NP_766000.1; NM_172412.2.
DR AlphaFoldDB; Q8BKV1; -.
DR SMR; Q8BKV1; -.
DR STRING; 10090.ENSMUSP00000124459; -.
DR GlyGen; Q8BKV1; 5 sites.
DR iPTMnet; Q8BKV1; -.
DR PhosphoSitePlus; Q8BKV1; -.
DR MaxQB; Q8BKV1; -.
DR PaxDb; Q8BKV1; -.
DR PRIDE; Q8BKV1; -.
DR ProteomicsDB; 271428; -.
DR DNASU; 71951; -.
DR Ensembl; ENSMUST00000161827; ENSMUSP00000124459; ENSMUSG00000029510.
DR GeneID; 71951; -.
DR KEGG; mmu:71951; -.
DR UCSC; uc009afj.1; mouse.
DR CTD; 221914; -.
DR MGI; MGI:1919201; Gpc2.
DR VEuPathDB; HostDB:ENSMUSG00000029510; -.
DR eggNOG; KOG3821; Eukaryota.
DR GeneTree; ENSGT01050000244897; -.
DR InParanoid; Q8BKV1; -.
DR OMA; GFHTQPI; -.
DR PhylomeDB; Q8BKV1; -.
DR TreeFam; TF105317; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR Reactome; R-MMU-2024096; HS-GAG degradation.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 71951; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Gpc2; mouse.
DR PRO; PR:Q8BKV1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BKV1; protein.
DR Bgee; ENSMUSG00000029510; Expressed in cortical plate and 92 other tissues.
DR ExpressionAtlas; Q8BKV1; baseline and differential.
DR Genevisible; Q8BKV1; MM.
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; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005796; C:Golgi lumen; 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; ISO:MGI.
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; ISO:MGI.
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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; GPI-anchor; Heparan sulfate; Lipoprotein;
KW Membrane; Proteoglycan; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..556
FT /note="Glypican-2"
FT /id="PRO_0000012305"
FT CHAIN 22..?
FT /note="Secreted glypican-2"
FT /id="PRO_0000333842"
FT PROPEP 557..579
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012306"
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"
SQ SEQUENCE 579 AA; 63344 MW; BB2A604283F17CB0 CRC64;
MSALRPLLLL LLHLCPGLGP GHGSEAKVVR SCAETRQVLG ARGYSLNLIP PSLISGEHLQ
VCPQEYTCCS SETEQKLIRD AEVTFRGLVE DSGSFLIHTL AARHRKFNEF FREMLSISQH
SLAQLFSHSY GRLYSQHAVI FNSLFSGLRD YYEKSGEGLD DTLADFWAQL LERAFPLLHP
QYSFPPDFLL CLTRLTSTAD GSLQPFGDSP RRLRLQISRA LVAARALVQG LETGRNVVSE
ALKVPVLEGC RQALMRLIGC PLCRGVPSLM PCRGFCLNVA HGCLSSRGLE PEWGGYLDGL
LLLAEKLQGP FSFELAAESI GVKISEGLMH LQENSVKVSA KVFQECGTPH PVQSRSRRAP
APREEASRSW RASAEEERPT TAAGTNLHRL VWELRERLSR VRGFWAGLPV TVCGDSRMAA
DLSQETAPCW TGVGRGRYMS PVVVGSLNEQ LHNPELDTSS PDVPTRRRRL HLRAATARMK
AAALGQDLDM HDADEDASGS GGGQQYADDW KAGAVPVVPP ARPPRPPRPP RRDGLGVRGG
SGSARYNQGR SRNLGSSVGL HTPLVLLLLP SALTLLVLR