ID CSPG5_HUMAN Reviewed; 566 AA. AC O95196; Q71M39; Q71M40; DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 3. DT 13-FEB-2019, entry version 153. DE RecName: Full=Chondroitin sulfate proteoglycan 5; DE AltName: Full=Acidic leucine-rich EGF-like domain-containing brain protein; DE AltName: Full=Neuroglycan C; DE Flags: Precursor; GN Name=CSPG5; Synonyms=CALEB, NGC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND VARIANT VAL-188. RC TISSUE=Brain; RX PubMed=9950058; DOI=10.1016/S0168-0102(98)00098-4; RA Yasuda Y., Tokita Y., Aono S., Matsui F., Ono T., Sonta S., RA Watanabe E., Nakanishi Y., Oohira A.; RT "Cloning and chromosomal mapping of the human gene of neuroglycan C RT (NGC), a neural transmembrane chondroitin sulfate proteoglycan with an RT EGF module."; RL Neurosci. Res. 32:313-322(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT VAL-188. RA Aono S., Tokita Y., Yamauchi S., Shuo T., Matsui F., Yasuda Y., RA Keino H., Shimada A., Kishikawa M., Asai M., Oohira A.; RT "Expression of neuroglycan C (NGC), a transmembrane chondroitin RT sulfate proteoglycan with an EGF module, in the human brain."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] RP INTERACTION WITH GOPC. RX PubMed=12885772; DOI=10.1074/jbc.M305577200; RA Hassel B., Schreff M., Stuebe E.-M., Blaich U., Schumacher S.; RT "CALEB/NGC interacts with the Golgi-associated protein PIST."; RL J. Biol. Chem. 278:40136-40143(2003). RN [5] RP INTERACTION WITH ERBB3, AND FUNCTION. RX PubMed=15358134; DOI=10.1016/j.bbrc.2004.07.066; RA Kinugasa Y., Ishiguro H., Tokita Y., Oohira A., Ohmoto H., RA Higashiyama S.; RT "Neuroglycan C, a novel member of the neuregulin family."; RL Biochem. Biophys. Res. Commun. 321:1045-1049(2004). RN [6] RP GLYCOSYLATION AT SER-165, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=23234360; DOI=10.1021/pr300963h; RA Halim A., Ruetschi U., Larson G., Nilsson J.; RT "LC-MS/MS characterization of O-glycosylation sites and glycan RT structures of human cerebrospinal fluid glycoproteins."; RL J. Proteome Res. 12:573-584(2013). CC -!- FUNCTION: May function as a growth and differentiation factor CC involved in neuritogenesis. May induce ERBB3 activation. CC {ECO:0000269|PubMed:15358134}. CC -!- SUBUNIT: Binds TNR and probably TNC (By similarity). Interacts CC with ERBB3 and GOPC. {ECO:0000250, ECO:0000269|PubMed:12885772, CC ECO:0000269|PubMed:15358134}. CC -!- INTERACTION: CC Q8BH60:Gopc (xeno); NbExp=3; IntAct=EBI-296349, EBI-296357; CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000250|UniProtKB:Q9ERQ6}; Single-pass type I membrane CC protein {ECO:0000250|UniProtKB:Q9ERQ6}. Endoplasmic reticulum CC membrane {ECO:0000250|UniProtKB:Q71M36}; Single-pass type I CC membrane protein {ECO:0000250|UniProtKB:Q71M36}. Golgi apparatus CC membrane {ECO:0000250|UniProtKB:Q71M36}; Single-pass type I CC membrane protein {ECO:0000250|UniProtKB:Q71M36}. Cell surface CC {ECO:0000250|UniProtKB:Q71M36}. Note=In neurons, localizes to CC synaptic junctions. Also detected in the endoplasmic reticulum and CC the Golgi. Partially enriched in lipid rafts. CC {ECO:0000250|UniProtKB:Q71M36, ECO:0000250|UniProtKB:Q9ERQ6}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O95196-1; Sequence=Displayed; CC Name=2; Synonyms=CSPG5-I; CC IsoId=O95196-2; Sequence=VSP_015761; CC Name=3; Synonyms=CSPG5-II; CC IsoId=O95196-3; Sequence=VSP_015760, VSP_015761; CC -!- TISSUE SPECIFICITY: Restricted to brain (at protein level). CC {ECO:0000269|PubMed:9950058}. CC -!- DEVELOPMENTAL STAGE: Expressed in brain of 3 months, 5 and 10- CC year-old individuals. {ECO:0000269|PubMed:9950058}. CC -!- PTM: N-glycosylated. {ECO:0000250}. CC -!- PTM: O-glycosylated; contains chondroitin sulfate glycans. Part- CC time proteoglycan, expressed in part as a proteoglycan exhibiting CC chondroitin sulfate glycans and in part as a non-proteoglycan CC form. The relative amount of both forms depends on tissues and CC tissues maturation (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylated; in intracellular and extracellular parts. CC {ECO:0000250}. CC -!- MISCELLANEOUS: Different forms of various molecular weight have CC been observed. Such forms are possibly due to different levels of CC glycosylation, phosphorylation and/or protein cleavage (By CC similarity). {ECO:0000250}. 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; AF059274; AAC69612.1; -; mRNA. DR EMBL; AF461087; AAQ04774.1; -; mRNA. DR EMBL; AF461088; AAQ04775.1; -; mRNA. DR EMBL; AF461089; AAQ04776.1; -; mRNA. DR EMBL; AC099778; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS2757.1; -. [O95196-2] DR CCDS; CCDS56252.1; -. [O95196-3] DR CCDS; CCDS56253.1; -. [O95196-1] DR RefSeq; NP_001193872.1; NM_001206943.1. [O95196-1] DR RefSeq; NP_001193873.1; NM_001206944.1. DR RefSeq; NP_006565.2; NM_006574.3. [O95196-2] DR UniGene; Hs.45127; -. DR ProteinModelPortal; O95196; -. DR SMR; O95196; -. DR BioGrid; 115917; 7. DR IntAct; O95196; 3. DR STRING; 9606.ENSP00000373244; -. DR GlyConnect; 657; -. DR iPTMnet; O95196; -. DR PhosphoSitePlus; O95196; -. DR UniCarbKB; O95196; -. DR BioMuta; CSPG5; -. DR PaxDb; O95196; -. DR PeptideAtlas; O95196; -. DR PRIDE; O95196; -. DR ProteomicsDB; 50697; -. DR ProteomicsDB; 50698; -. [O95196-2] DR ProteomicsDB; 50699; -. [O95196-3] DR DNASU; 10675; -. DR Ensembl; ENST00000264723; ENSP00000264723; ENSG00000114646. [O95196-2] DR Ensembl; ENST00000383738; ENSP00000373244; ENSG00000114646. [O95196-1] DR Ensembl; ENST00000456150; ENSP00000392096; ENSG00000114646. [O95196-3] DR GeneID; 10675; -. DR KEGG; hsa:10675; -. DR UCSC; uc003crn.4; human. [O95196-1] DR CTD; 10675; -. DR DisGeNET; 10675; -. DR EuPathDB; HostDB:ENSG00000114646.9; -. DR GeneCards; CSPG5; -. DR H-InvDB; HIX0003276; -. DR HGNC; HGNC:2467; CSPG5. DR HPA; HPA049529; -. DR HPA; HPA067818; -. DR HPA; HPA071779; -. DR MIM; 606775; gene. DR neXtProt; NX_O95196; -. DR OpenTargets; ENSG00000114646; -. DR PharmGKB; PA26965; -. DR eggNOG; ENOG410IJTR; Eukaryota. DR eggNOG; ENOG410YF9F; LUCA. DR GeneTree; ENSGT00440000034270; -. DR HOGENOM; HOG000112020; -. DR HOVERGEN; HBG081361; -. DR InParanoid; O95196; -. DR KO; K08116; -. DR OMA; EPTYPFQ; -. DR OrthoDB; 433725at2759; -. DR PhylomeDB; O95196; -. DR TreeFam; TF338636; -. DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis. DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis. DR Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis. DR Reactome; R-HSA-2024101; CS/DS 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-3595172; Defective CHST3 causes SEDCJD. DR Reactome; R-HSA-3595174; Defective CHST14 causes EDS, musculocontractural type. DR Reactome; R-HSA-3595177; Defective CHSY1 causes TPBS. DR Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1. DR ChiTaRS; CSPG5; human. DR GenomeRNAi; 10675; -. DR PRO; PR:O95196; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000114646; Expressed in 147 organ(s), highest expression level in endothelial cell. DR ExpressionAtlas; O95196; baseline and differential. DR Genevisible; O95196; HS. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030660; C:Golgi-associated vesicle membrane; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0008083; F:growth factor activity; TAS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; TAS:Reactome. DR GO; GO:0030207; P:chondroitin sulfate catabolic process; TAS:Reactome. DR GO; GO:0030208; P:dermatan sulfate biosynthetic process; TAS:Reactome. DR GO; GO:0046907; P:intracellular transport; TAS:UniProtKB. DR GO; GO:0007399; P:nervous system development; TAS:UniProtKB. DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl. DR GO; GO:0099550; P:trans-synaptic signaling, modulating synaptic transmission; IEA:Ensembl. DR InterPro; IPR010555; CSPG5_S_attach_dom. DR InterPro; IPR009505; Neural_ProG_Cyt. DR Pfam; PF06566; Chon_Sulph_att; 1. DR Pfam; PF06567; Neural_ProG_Cyt; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Complete proteome; KW Developmental protein; Differentiation; Disulfide bond; KW EGF-like domain; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; KW Growth regulation; Membrane; Neurogenesis; Phosphoprotein; KW Polymorphism; Proteoglycan; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 30 {ECO:0000255}. FT CHAIN 31 566 Chondroitin sulfate proteoglycan 5. FT /FTId=PRO_0000042151. FT TOPO_DOM 31 423 Extracellular. {ECO:0000255}. FT TRANSMEM 424 444 Helical. {ECO:0000255}. FT TOPO_DOM 445 566 Cytoplasmic. {ECO:0000255}. FT DOMAIN 371 413 EGF-like. FT REGION 264 301 Interaction with TNC and TNR. FT {ECO:0000250}. FT REGION 442 460 Interaction with GOPC. FT {ECO:0000269|PubMed:12885772}. FT MOD_RES 467 467 Phosphoserine. FT {ECO:0000250|UniProtKB:Q71M36}. FT MOD_RES 475 475 Phosphoserine. FT {ECO:0000250|UniProtKB:Q71M36}. FT MOD_RES 483 483 Phosphoserine. FT {ECO:0000250|UniProtKB:Q71M36}. FT MOD_RES 543 543 Phosphoserine. FT {ECO:0000250|UniProtKB:Q71M36}. FT CARBOHYD 57 57 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 117 117 O-linked (Xyl...) (chondroitin sulfate) FT serine. {ECO:0000250}. FT CARBOHYD 165 165 O-linked (GalNAc...) serine. FT {ECO:0000269|PubMed:23234360}. FT DISULFID 374 387 {ECO:0000250}. FT DISULFID 381 397 {ECO:0000250}. FT DISULFID 399 412 {ECO:0000250}. FT VAR_SEQ 1 138 Missing (in isoform 3). FT {ECO:0000303|Ref.2}. FT /FTId=VSP_015760. FT VAR_SEQ 487 513 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:9950058, FT ECO:0000303|Ref.2}. FT /FTId=VSP_015761. FT VARIANT 188 188 G -> V (in dbSNP:rs3732530). FT {ECO:0000269|PubMed:9950058, FT ECO:0000269|Ref.2}. FT /FTId=VAR_055089. FT VARIANT 417 417 T -> P (in dbSNP:rs34016925). FT /FTId=VAR_055090. SQ SEQUENCE 566 AA; 60016 MW; DD8DA045C1BE31E5 CRC64; MGRAGGGGPG RGPPPLLLFL GAALVLASGA VPAREAGSAV EAEELVKGSP AWEPPANDTR EEAGPPAAGE DEASWTAPGG ELAGPEEVLQ ESAAVTGTAW LEADSPGLGG VTAEAGSGDA QALPATLQAP HEVLGQSIMP PAIPEATEAS GPPSPTPGDK LSPASELPKE SPLEVWLNLG GSTPDPQGPE LTYPFQGTLE PQPASDIIDI DYFEGLDGEG RGADLGSFPG SPGTSENHPD TEGETPSWSL LDLYDDFTPF DESDFYPTTS FYDDLDEEEE EEEDDKDAVG GGDLEDENEL LVPTGKPGLG PGTGQPTSRW HAVPPQHTLG SVPGSSIALR PRPGEPGRDL ASSENGTECR SGFVRHNGSC RSVCDLFPSY CHNGGQCYLV ENIGAFCRCN TQDYIWHKGM RCESIITDFQ VMCVAVGSAA LVLLLLFMMT VFFAKKLYLL KTENTKLRRT NKFRTPSELH NDNFSLSTIA EGSHPNVRKL CNTPRTSSPH ARALAHYDNV ICQDDPSAPH KIQEVLKSCL KEEESFNIQN SMSPKLEGGK GDQADLDVNC LQNNLT //