GenomeNet

Database: UniProt
Entry: O95196
LinkDB: O95196
Original site: O95196 
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}.
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
//
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