CSPG5_RAT
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 03-AUG-2022, entry version 123.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 31-45; 232-238
RP AND 337-356, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND 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 proteoglycan
RT 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., Chiquet-Ehrismann R.,
RA 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 after
RT 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., Watanabe E.,
RA Nakanishi Y., Oohira A.;
RT "Cloning and chromosomal mapping of the human gene of neuroglycan C (NGC),
RT a neural transmembrane chondroitin sulfate proteoglycan with an EGF
RT 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 sulfate
RT 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).
RN [7]
RP INTERACTION WITH MDK.
RX PubMed=16901907; DOI=10.1074/jbc.m602228200;
RA Ichihara-Tanaka K., Oohira A., Rumsby M., Muramatsu T.;
RT "Neuroglycan C is a novel midkine receptor involved in process elongation
RT of oligodendroglial precursor-like cells.";
RL J. Biol. Chem. 281:30857-30864(2006).
CC -!- FUNCTION: May function as a growth and differentiation factor involved
CC in neuritogenesis. May induce ERBB3 activation.
CC -!- SUBUNIT: Interacts with ERBB3 and GOPC. Binds TNR and probably TNC (By
CC similarity). Interacts with MDK; this interaction is independent of the
CC presence of chondroitin sulfate chains and promotes elongation of
CC oligodendroglial precursor-like cells (PubMed:16901907). {ECO:0000250,
CC ECO:0000269|PubMed:16901907}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11929867};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:11929867}.
CC Synaptic cell membrane {ECO:0000250|UniProtKB:Q71M36}; Single-pass type
CC I membrane protein {ECO:0000250|UniProtKB:Q71M36}. Endoplasmic
CC reticulum 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 membrane
CC protein {ECO:0000250|UniProtKB:Q71M36}. Cell surface
CC {ECO:0000250|UniProtKB:Q71M36}. Note=In neurons, localizes to synaptic
CC junctions. Also detected in the endoplasmic reticulum and the Golgi (By
CC similarity). Partially enriched in lipid rafts (PubMed:11929867).
CC {ECO:0000250|UniProtKB:Q71M36, 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). {ECO:0000269|PubMed:11069908,
CC ECO:0000269|PubMed:11095636, ECO:0000269|PubMed:7592931,
CC ECO:0000269|PubMed:9950058}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at E16 in the cerebral cortex
CC and increases to reach a maximum 20 days after birth. Then it decreases
CC till adulthood to be expressed half of the peak level. In the retina,
CC expression reaches a maximum at postnatal day 14 (P14). It starts
CC weakly at E16 in the retinal pigment epithelium (RPE). At P0 it is
CC detected in nerve fiber layer (NFL), ganglion cell layer (GCL), inner
CC plexiform layer (IPL) and RPE. At P7, it becomes intense in the NFL and
CC IPL. At P14, expression becomes intense in the area of outer segments
CC (OS) of the photoreceptor cells as well as in RPE, whereas in the inner
CC layers it becomes gradually fainter. From P21 to P42, it decreases in
CC inner retinal layers. OS and RPE still express, whereas expression in
CC 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-time
CC proteoglycan, expressed in part as a proteoglycan exhibiting
CC chondroitin sulfate glycans and in part as a non-proteoglycan form. The
CC relative amount of both forms depends on tissues and tissues maturation
CC (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 been
CC observed. Such forms are possibly due to different levels of
CC glycosylation, phosphorylation and/or protein cleavage (By similarity).
CC {ECO:0000250}.
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DR EMBL; U33553; AAC98537.1; -; mRNA.
DR EMBL; AF292102; AAG29500.1; -; mRNA.
DR PIR; I55454; I55454.
DR RefSeq; NP_062157.1; NM_019284.1. [Q9ERQ6-2]
DR RefSeq; NP_598413.1; NM_133652.1. [Q9ERQ6-1]
DR AlphaFoldDB; Q9ERQ6; -.
DR BioGRID; 248393; 1.
DR STRING; 10116.ENSRNOP00000028278; -.
DR GlyGen; Q9ERQ6; 15 sites.
DR iPTMnet; Q9ERQ6; -.
DR PhosphoSitePlus; Q9ERQ6; -.
DR PaxDb; Q9ERQ6; -.
DR PRIDE; Q9ERQ6; -.
DR Ensembl; ENSRNOT00000028278; ENSRNOP00000028278; ENSRNOG00000020833. [Q9ERQ6-1]
DR GeneID; 50568; -.
DR KEGG; rno:50568; -.
DR UCSC; RGD:2431; rat. [Q9ERQ6-1]
DR CTD; 10675; -.
DR RGD; 2431; Cspg5.
DR eggNOG; ENOG502QXSB; Eukaryota.
DR GeneTree; ENSGT00440000034270; -.
DR InParanoid; Q9ERQ6; -.
DR OrthoDB; 433725at2759; -.
DR PhylomeDB; Q9ERQ6; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-RNO-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-RNO-2024101; CS/DS degradation.
DR PRO; PR:Q9ERQ6; -.
DR Proteomes; UP000002494; Chromosome 8.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
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:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0031103; P:axon regeneration; IEP:RGD.
DR GO; GO:0048858; P:cell projection morphogenesis; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0106091; P:glial cell projection elongation; IDA:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0099550; P:trans-synaptic signaling, modulating synaptic transmission; ISO:RGD.
DR InterPro; IPR042382; CSPG5.
DR InterPro; IPR010555; CSPG5_S_attach_dom.
DR InterPro; IPR009505; Neural_ProG_Cyt.
DR PANTHER; PTHR15381; PTHR15381; 1.
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; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Growth regulation; Membrane; Neurogenesis; Phosphoprotein; Proteoglycan;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:7592931"
FT CHAIN 31..571
FT /note="Chondroitin sulfate proteoglycan 5"
FT /id="PRO_0000042153"
FT TOPO_DOM 31..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 376..418
FT /note="EGF-like"
FT REGION 57..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..306
FT /note="Interaction with TNC and TNR"
FT /evidence="ECO:0000250"
FT REGION 279..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..465
FT /note="Interaction with GOPC"
FT /evidence="ECO:0000250"
FT REGION 538..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..299
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71M36"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71M36"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71M36"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71M36"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 132
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 379..392
FT /evidence="ECO:0000250"
FT DISULFID 386..402
FT /evidence="ECO:0000250"
FT DISULFID 404..417
FT /evidence="ECO:0000250"
FT VAR_SEQ 492..518
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7592931"
FT /id="VSP_015765"
FT CONFLICT 565
FT /note="C -> F (in Ref. 1; AAC98537)"
FT /evidence="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
