GenomeNet

Database: UniProt
Entry: Q9ERQ6
LinkDB: Q9ERQ6
Original site: Q9ERQ6 
ID   CSPG5_RAT               Reviewed;         571 AA.
AC   Q9ERQ6; Q62831;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   16-JAN-2019, entry version 109.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 31-45;
RP   232-238 AND 337-356, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   GLYCOSYLATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=7592931; DOI=10.1074/jbc.270.45.26876;
RA   Watanabe E., Maeda N., Matsui F., Kushima Y., Noda M., Oohira A.;
RT   "Neuroglycan C, a novel membrane-spanning chondroitin sulfate
RT   proteoglycan that is restricted to the brain.";
RL   J. Biol. Chem. 270:26876-26882(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=11069908; DOI=10.1074/jbc.M007234200;
RA   Schumacher S., Jung M., Noerenberg U., Dorner A.,
RA   Chiquet-Ehrismann R., Stuermer C.A.O., Rathjen F.G.;
RT   "CALEB binds via its acidic stretch to the fibrinogen-like domain of
RT   tenascin-C or tenascin-R and its expression is dynamically regulated
RT   after optic nerve lesion.";
RL   J. Biol. Chem. 276:7337-7345(2001).
RN   [3]
RP   TISSUE SPECIFICITY, AND GLYCOSYLATION.
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   [4]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=11095636;
RA   Inatani M., Tanihara H., Oohira A., Otori Y., Nishida A., Honjo M.,
RA   Kido N., Honda Y.;
RT   "Neuroglycan C, a neural tissue-specific transmembrane chondroitin
RT   sulfate proteoglycan, in retinal neural network formation.";
RL   Invest. Ophthalmol. Vis. Sci. 41:4338-4346(2000).
RN   [5]
RP   PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=11929867; DOI=10.1074/jbc.M200909200;
RA   Yamauchi S., Tokita Y., Aono S., Matsui F., Shuo T., Ito H., Kato K.,
RA   Kasahara K., Oohira A.;
RT   "Phosphorylation of neuroglycan C, a brain-specific transmembrane
RT   chondroitin sulfate proteoglycan, and its localization in the lipid
RT   rafts.";
RL   J. Biol. Chem. 277:20583-20590(2002).
RN   [6]
RP   INDUCTION.
RX   PubMed=12358776; DOI=10.1046/j.1471-4159.2002.01083.x;
RA   Toda S., McGinty J.F., Kalivas P.W.;
RT   "Repeated cocaine administration alters the expression of genes in
RT   corticolimbic circuitry after a 3-week withdrawal: a DNA macroarray
RT   study.";
RL   J. Neurochem. 82:1290-1299(2002).
CC   -!- FUNCTION: May function as a growth and differentiation factor
CC       involved in neuritogenesis. May induce ERBB3 activation.
CC   -!- SUBUNIT: Interacts with ERBB3 and GOPC. Binds TNR and probably TNC
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11929867};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:11929867}.
CC       Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q71M36};
CC       Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q71M36}. Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q71M36}; Single-pass type I membrane
CC       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 (By similarity). Partially enriched in lipid rafts
CC       (PubMed:11929867). {ECO:0000250|UniProtKB:Q71M36,
CC       ECO:0000269|PubMed:11929867}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ERQ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ERQ6-2; Sequence=VSP_015765;
CC   -!- TISSUE SPECIFICITY: Expressed in cerebral cortex and cerebellum.
CC       Expressed in retina (at protein level).
CC       {ECO:0000269|PubMed:11069908, ECO:0000269|PubMed:11095636,
CC       ECO:0000269|PubMed:7592931, ECO:0000269|PubMed:9950058}.
CC   -!- DEVELOPMENTAL STAGE: Expression starts at E16 in the cerebral
CC       cortex and increases to reach a maximum 20 days after birth. Then
CC       it decreases till adulthood to be expressed half of the peak
CC       level. In the retina, expression reaches a maximum at postnatal
CC       day 14 (P14). It starts weakly at E16 in the retinal pigment
CC       epithelium (RPE). At P0 it is detected in nerve fiber layer (NFL),
CC       ganglion cell layer (GCL), inner plexiform layer (IPL) and RPE. At
CC       P7, it becomes intense in the NFL and IPL. At P14, expression
CC       becomes intense in the area of outer segments (OS) of the
CC       photoreceptor cells as well as in RPE, whereas in the inner layers
CC       it becomes gradually fainter. From P21 to P42, it decreases in
CC       inner retinal layers. OS and RPE still express, whereas expression
CC       in the NFL and IPL decreases (at protein level).
CC       {ECO:0000269|PubMed:11095636, ECO:0000269|PubMed:7592931}.
CC   -!- INDUCTION: Up-regulated in nucleus accumbens shell by cocaine
CC       administration. {ECO:0000269|PubMed:12358776}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:7592931,
CC       ECO:0000269|PubMed:9950058}.
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:0000269|PubMed:11929867}.
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; U33553; AAC98537.1; -; mRNA.
DR   EMBL; AF292102; AAG29500.1; -; mRNA.
DR   PIR; I55454; I55454.
DR   RefSeq; NP_062157.1; NM_019284.1.
DR   RefSeq; NP_598413.1; NM_133652.1. [Q9ERQ6-1]
DR   UniGene; Rn.10146; -.
DR   SMR; Q9ERQ6; -.
DR   BioGrid; 248393; 1.
DR   STRING; 10116.ENSRNOP00000028278; -.
DR   iPTMnet; Q9ERQ6; -.
DR   PhosphoSitePlus; Q9ERQ6; -.
DR   PaxDb; Q9ERQ6; -.
DR   PRIDE; Q9ERQ6; -.
DR   GeneID; 50568; -.
DR   KEGG; rno:50568; -.
DR   UCSC; RGD:2431; rat. [Q9ERQ6-1]
DR   CTD; 10675; -.
DR   RGD; 2431; Cspg5.
DR   eggNOG; ENOG410IJTR; Eukaryota.
DR   eggNOG; ENOG410YF9F; LUCA.
DR   HOVERGEN; HBG081361; -.
DR   InParanoid; Q9ERQ6; -.
DR   KO; K08116; -.
DR   OrthoDB; 433725at2759; -.
DR   PhylomeDB; Q9ERQ6; -.
DR   PRO; PR:Q9ERQ6; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030660; C:Golgi-associated vesicle membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031103; P:axon regeneration; IEP:RGD.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Endoplasmic reticulum; Glycoprotein;
KW   Golgi apparatus; Growth regulation; Membrane; Neurogenesis;
KW   Phosphoprotein; Proteoglycan; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     30       {ECO:0000269|PubMed:7592931}.
FT   CHAIN        31    571       Chondroitin sulfate proteoglycan 5.
FT                                /FTId=PRO_0000042153.
FT   TOPO_DOM     31    428       Extracellular. {ECO:0000255}.
FT   TRANSMEM    429    449       Helical. {ECO:0000255}.
FT   TOPO_DOM    450    571       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      376    418       EGF-like.
FT   REGION      270    306       Interaction with TNC and TNR.
FT                                {ECO:0000250}.
FT   REGION      447    465       Interaction with GOPC. {ECO:0000250}.
FT   COMPBIAS    146    200       Pro-rich.
FT   COMPBIAS    282    289       Poly-Glu.
FT   MOD_RES     472    472       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q71M36}.
FT   MOD_RES     480    480       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q71M36}.
FT   MOD_RES     488    488       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q71M36}.
FT   MOD_RES     548    548       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q71M36}.
FT   CARBOHYD     57     57       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     76     76       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    123    123       O-linked (Xyl...) (chondroitin sulfate)
FT                                serine. {ECO:0000250}.
FT   CARBOHYD    132    132       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    143    143       O-linked (GalNAc...) serine.
FT                                {ECO:0000255}.
FT   CARBOHYD    144    144       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    153    153       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    156    156       O-linked (GalNAc...) serine.
FT                                {ECO:0000255}.
FT   CARBOHYD    160    160       O-linked (GalNAc...) serine.
FT                                {ECO:0000255}.
FT   CARBOHYD    162    162       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    198    198       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    240    240       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    318    318       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    322    322       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    372    372       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    379    392       {ECO:0000250}.
FT   DISULFID    386    402       {ECO:0000250}.
FT   DISULFID    404    417       {ECO:0000250}.
FT   VAR_SEQ     492    518       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:7592931}.
FT                                /FTId=VSP_015765.
FT   CONFLICT    565    565       C -> F (in Ref. 1; AAC98537).
FT                                {ECO:0000305}.
SQ   SEQUENCE   571 AA;  60959 MW;  CF42A0115F0CD11E CRC64;
     MGRAGGGGPG WGPPPVLLLL GVTLVLTAGA VPAREAGSAI EAEELVRSGL AWESRANDTR
     EEAGLPAAGE DETSWTERGS ELAAVGPGVG PEETLEASAA VTGTAWLEAD GTGLGGVTAE
     AGSGDAQTLP ATLQAPDEAL GSSTMPPAIP EATEASGPPS PTLRDKPSLV PELPKEIPLE
     VWLNLGGSTP DPQRPEPTFP LQGTLETQPA SDIIDIDYFE GLDSEGRGTD MGRFPGSPGT
     SENHPDTEGE TPSWSLLDLY DDFTPFDESD FYPTTSFYDD LEEEEEEEED KDAVGGGDLE
     DESDLLLPSQ KPGVGPGTGQ PTSRWHAVPP QHTLGMVPGG SISLRPRPGD PGKDLATSEN
     GTECRVGFVR HNGSCRSVCD LFPSYCHNGG QCYLVENIGA FCRCNTQDYI WHKGMRCESI
     ITDFQVMCVA VGSAALVLLL LFMMTVFFAK KLYLLKTENT KLRRTNKFRT PSELHNDNFS
     LSTIAEGSHP NVRKLCDTPC VSSPHARALA HCDNIVCQDD PSAPHKIQEA LKSRLKEEES
     FNIQNSMSPK LEGGKGDQDD LEVNCLQNNL T
//
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