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Protein

Chondroitin sulfate proteoglycan 5

Gene

Cspg5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation.

GO - Biological processi

  • axon regeneration Source: RGD
  • regulation of growth Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Growth regulation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Chondroitin sulfate proteoglycan 5
Alternative name(s):
Acidic leucine-rich EGF-like domain-containing brain protein
Neuroglycan C
Gene namesi
Name:Cspg5
Synonyms:Caleb, Ngc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2431. Cspg5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 428398ExtracellularSequence analysisAdd
BLAST
Transmembranei429 – 44921HelicalSequence analysisAdd
BLAST
Topological domaini450 – 571122CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30301 PublicationAdd
BLAST
Chaini31 – 571541Chondroitin sulfate proteoglycan 5PRO_0000042153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence analysis
Glycosylationi76 – 761O-linked (GalNAc...)Sequence analysis
Glycosylationi123 – 1231O-linked (Xyl...) (chondroitin sulfate)By similarity
Glycosylationi132 – 1321O-linked (GalNAc...)Sequence analysis
Glycosylationi143 – 1431O-linked (GalNAc...)Sequence analysis
Glycosylationi144 – 1441O-linked (GalNAc...)Sequence analysis
Glycosylationi153 – 1531O-linked (GalNAc...)Sequence analysis
Glycosylationi156 – 1561O-linked (GalNAc...)Sequence analysis
Glycosylationi160 – 1601O-linked (GalNAc...)Sequence analysis
Glycosylationi162 – 1621O-linked (GalNAc...)Sequence analysis
Glycosylationi198 – 1981O-linked (GalNAc...)Sequence analysis
Glycosylationi240 – 2401O-linked (GalNAc...)Sequence analysis
Glycosylationi318 – 3181O-linked (GalNAc...)Sequence analysis
Glycosylationi322 – 3221O-linked (GalNAc...)Sequence analysis
Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence analysis
Disulfide bondi379 ↔ 392By similarity
Disulfide bondi386 ↔ 402By similarity
Disulfide bondi404 ↔ 417By similarity
Modified residuei472 – 4721PhosphoserineBy similarity
Modified residuei480 – 4801PhosphoserineBy similarity
Modified residuei488 – 4881PhosphoserineBy similarity
Modified residuei548 – 5481PhosphoserineBy similarity

Post-translational modificationi

N-glycosylated.2 Publications
O-glycosylated; contains chondroitin sulfate glycans. Part-time proteoglycan, expressed in part as a proteoglycan exhibiting chondroitin sulfate glycans and in part as a non-proteoglycan form. The relative amount of both forms depends on tissues and tissues maturation (By similarity).By similarity
Phosphorylated; in intracellular and extracellular parts.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan

Proteomic databases

PaxDbiQ9ERQ6.
PRIDEiQ9ERQ6.

PTM databases

iPTMnetiQ9ERQ6.
PhosphoSiteiQ9ERQ6.

Expressioni

Tissue specificityi

Expressed in cerebral cortex and cerebellum. Expressed in retina (at protein level).4 Publications

Developmental stagei

Expression starts at E16 in the cerebral cortex and increases to reach a maximum 20 days after birth. Then it decreases till adulthood to be expressed half of the peak level. In the retina, expression reaches a maximum at postnatal day 14 (P14). It starts weakly at E16 in the retinal pigment epithelium (RPE). At P0 it is detected in nerve fiber layer (NFL), ganglion cell layer (GCL), inner plexiform layer (IPL) and RPE. At P7, it becomes intense in the NFL and IPL. At P14, expression becomes intense in the area of outer segments (OS) of the photoreceptor cells as well as in RPE, whereas in the inner layers it becomes gradually fainter. From P21 to P42, it decreases in inner retinal layers. OS and RPE still express, whereas expression in the NFL and IPL decreases (at protein level).2 Publications

Inductioni

Up-regulated in nucleus accumbens shell by cocaine administration.1 Publication

Interactioni

Subunit structurei

Interacts with ERBB3 and GOPC. Binds TNR and probably TNC (By similarity).By similarity

Protein-protein interaction databases

BioGridi248393. 1 interaction.
STRINGi10116.ENSRNOP00000028278.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini376 – 41843EGF-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni270 – 30637Interaction with TNC and TNRBy similarityAdd
BLAST
Regioni447 – 46519Interaction with GOPCBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi146 – 20055Pro-richAdd
BLAST
Compositional biasi282 – 2898Poly-Glu

Sequence similaritiesi

Contains 1 EGF-like domain.Curated

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJTR. Eukaryota.
ENOG410YF9F. LUCA.
HOVERGENiHBG081361.
InParanoidiQ9ERQ6.
KOiK08116.
PhylomeDBiQ9ERQ6.

Family and domain databases

InterProiIPR010555. Chon_Sulph_att.
IPR009505. Neural_ProG_Cyt.
[Graphical view]
PfamiPF06566. Chon_Sulph_att. 1 hit.
PF06567. Neural_ProG_Cyt. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ERQ6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGRAGGGGPG WGPPPVLLLL GVTLVLTAGA VPAREAGSAI EAEELVRSGL
60 70 80 90 100
AWESRANDTR EEAGLPAAGE DETSWTERGS ELAAVGPGVG PEETLEASAA
110 120 130 140 150
VTGTAWLEAD GTGLGGVTAE AGSGDAQTLP ATLQAPDEAL GSSTMPPAIP
160 170 180 190 200
EATEASGPPS PTLRDKPSLV PELPKEIPLE VWLNLGGSTP DPQRPEPTFP
210 220 230 240 250
LQGTLETQPA SDIIDIDYFE GLDSEGRGTD MGRFPGSPGT SENHPDTEGE
260 270 280 290 300
TPSWSLLDLY DDFTPFDESD FYPTTSFYDD LEEEEEEEED KDAVGGGDLE
310 320 330 340 350
DESDLLLPSQ KPGVGPGTGQ PTSRWHAVPP QHTLGMVPGG SISLRPRPGD
360 370 380 390 400
PGKDLATSEN GTECRVGFVR HNGSCRSVCD LFPSYCHNGG QCYLVENIGA
410 420 430 440 450
FCRCNTQDYI WHKGMRCESI ITDFQVMCVA VGSAALVLLL LFMMTVFFAK
460 470 480 490 500
KLYLLKTENT KLRRTNKFRT PSELHNDNFS LSTIAEGSHP NVRKLCDTPC
510 520 530 540 550
VSSPHARALA HCDNIVCQDD PSAPHKIQEA LKSRLKEEES FNIQNSMSPK
560 570
LEGGKGDQDD LEVNCLQNNL T
Length:571
Mass (Da):60,959
Last modified:March 1, 2001 - v1
Checksum:iCF42A0115F0CD11E
GO
Isoform 2 (identifier: Q9ERQ6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     492-518: Missing.

Show »
Length:544
Mass (Da):58,039
Checksum:i51C364613203A21E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti565 – 5651C → F in AAC98537 (PubMed:7592931).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei492 – 51827Missing in isoform 2. 1 PublicationVSP_015765Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33553 mRNA. Translation: AAC98537.1.
AF292102 mRNA. Translation: AAG29500.1.
PIRiI55454.
RefSeqiNP_062157.1. NM_019284.1.
NP_598413.1. NM_133652.1. [Q9ERQ6-1]
UniGeneiRn.10146.

Genome annotation databases

GeneIDi50568.
KEGGirno:50568.
UCSCiRGD:2431. rat. [Q9ERQ6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33553 mRNA. Translation: AAC98537.1.
AF292102 mRNA. Translation: AAG29500.1.
PIRiI55454.
RefSeqiNP_062157.1. NM_019284.1.
NP_598413.1. NM_133652.1. [Q9ERQ6-1]
UniGeneiRn.10146.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248393. 1 interaction.
STRINGi10116.ENSRNOP00000028278.

PTM databases

iPTMnetiQ9ERQ6.
PhosphoSiteiQ9ERQ6.

Proteomic databases

PaxDbiQ9ERQ6.
PRIDEiQ9ERQ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi50568.
KEGGirno:50568.
UCSCiRGD:2431. rat. [Q9ERQ6-1]

Organism-specific databases

CTDi10675.
RGDi2431. Cspg5.

Phylogenomic databases

eggNOGiENOG410IJTR. Eukaryota.
ENOG410YF9F. LUCA.
HOVERGENiHBG081361.
InParanoidiQ9ERQ6.
KOiK08116.
PhylomeDBiQ9ERQ6.

Miscellaneous databases

PROiQ9ERQ6.

Family and domain databases

InterProiIPR010555. Chon_Sulph_att.
IPR009505. Neural_ProG_Cyt.
[Graphical view]
PfamiPF06566. Chon_Sulph_att. 1 hit.
PF06567. Neural_ProG_Cyt. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Neuroglycan C, a novel membrane-spanning chondroitin sulfate proteoglycan that is restricted to the brain."
    Watanabe E., Maeda N., Matsui F., Kushima Y., Noda M., Oohira A.
    J. Biol. Chem. 270:26876-26882(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 31-45; 232-238 AND 337-356, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "CALEB binds via its acidic stretch to the fibrinogen-like domain of tenascin-C or tenascin-R and its expression is dynamically regulated after optic nerve lesion."
    Schumacher S., Jung M., Noerenberg U., Dorner A., Chiquet-Ehrismann R., Stuermer C.A.O., Rathjen F.G.
    J. Biol. Chem. 276:7337-7345(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
  3. "Cloning and chromosomal mapping of the human gene of neuroglycan C (NGC), a neural transmembrane chondroitin sulfate proteoglycan with an EGF module."
    Yasuda Y., Tokita Y., Aono S., Matsui F., Ono T., Sonta S., Watanabe E., Nakanishi Y., Oohira A.
    Neurosci. Res. 32:313-322(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, GLYCOSYLATION.
    Tissue: Brain.
  4. "Neuroglycan C, a neural tissue-specific transmembrane chondroitin sulfate proteoglycan, in retinal neural network formation."
    Inatani M., Tanihara H., Oohira A., Otori Y., Nishida A., Honjo M., Kido N., Honda Y.
    Invest. Ophthalmol. Vis. Sci. 41:4338-4346(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  5. "Phosphorylation of neuroglycan C, a brain-specific transmembrane chondroitin sulfate proteoglycan, and its localization in the lipid rafts."
    Yamauchi S., Tokita Y., Aono S., Matsui F., Shuo T., Ito H., Kato K., Kasahara K., Oohira A.
    J. Biol. Chem. 277:20583-20590(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
  6. "Repeated cocaine administration alters the expression of genes in corticolimbic circuitry after a 3-week withdrawal: a DNA macroarray study."
    Toda S., McGinty J.F., Kalivas P.W.
    J. Neurochem. 82:1290-1299(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiCSPG5_RAT
AccessioniPrimary (citable) accession number: Q9ERQ6
Secondary accession number(s): Q62831
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Different forms of various molecular weight have been observed. Such forms are possibly due to different levels of glycosylation, phosphorylation and/or protein cleavage (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.