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Q71M36 (CSPG5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chondroitin sulfate proteoglycan 5
Alternative name(s):
Acidic leucine-rich EGF-like domain-containing brain protein
Neuroglycan C
Gene names
Name:Cspg5
Synonyms:Caleb, Ngc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function as a growth and differentiation factor involved in neuritogenesis. May induce ERBB3 activation. Ref.9

Subunit structure

Binds TNR and probably TNC By similarity. Interacts with ERBB3 and GOPC. Ref.6

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Note: Partially enriched in lipid rafts By similarity. In neurons, localizes to synaptic junctions. Also detected in the endoplasmic reticulum and the Golgi. Ref.1 Ref.7 Ref.8

Tissue specificity

Expressed in olfactory bulb, hippocampus, brain stem, spinal cord, cerebrum and cerebellum. Expressed by Purkinje cells in the cerebellum (at protein level). Expressed in immature and mature cerebellum (isoform 1, isoform 2 and isoform 3) Ref.1 Ref.5 Ref.8

Developmental stage

The proteoglycan form decreases from birth to adulthood in the cerebellum concomitant with non-proteoglycan form increase. In the cerebrum the maximum of expression of the proteoglycan is detected 15 days after birth and then decreases gradually to reach half-level at adulthood (at protein level). Ref.1

Post-translational modification

N-glycosylated By similarity. Ref.1 Ref.8

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. In the cerebellum the 2 forms coexist while in the cerebrum the proteoglycan form is predominant. Ref.1 Ref.8

Phosphorylated; in intracellular and extracellular parts By similarity.

Disruption phenotype

Altered synaptic transmission at early developmental stages. Ref.9

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.

Sequence similarities

Contains 1 EGF-like domain.

Sequence caution

The sequence AAQ04778.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC35578.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q71M36-1)

Also known as: NGC-III;

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.
Isoform 2 (identifier: Q71M36-2)

Also known as: NGC-I;

The sequence of this isoform differs from the canonical sequence as follows:
     487-513: Missing.
Note: Major isoform.
Isoform 3 (identifier: Q71M36-3)

Also known as: NGC-II;

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
     487-513: Missing.
Isoform 4 (identifier: Q71M36-4)

The sequence of this isoform differs from the canonical sequence as follows:
     514-566: DDPSAPHKIQ...GVNCLQNNLT → VTYLPHISPF...RERCIDSLTV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 566536Chondroitin sulfate proteoglycan 5
PRO_0000042152

Regions

Topological domain31 – 423393Extracellular Potential
Transmembrane424 – 44421Helical; Potential
Topological domain445 – 566122Cytoplasmic Potential
Domain371 – 41343EGF-like
Region265 – 30137Interaction with TNC and TNR
Region442 – 46019Interaction with GOPC By similarity

Amino acid modifications

Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation761O-linked (GalNAc...) Potential
Glycosylation1231O-linked (Xyl...) (chondroitin sulfate) Ref.8
Glycosylation1321O-linked (GalNAc...) Potential
Glycosylation1431O-linked (GalNAc...) Potential
Glycosylation1441O-linked (GalNAc...) Potential
Glycosylation1531O-linked (GalNAc...) Potential
Glycosylation1551O-linked (GalNAc...) Potential
Glycosylation1561O-linked (GalNAc...) Potential
Glycosylation1601O-linked (GalNAc...) Potential
Glycosylation2351O-linked (GalNAc...) Potential
Glycosylation3551N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Disulfide bond374 ↔ 387 By similarity
Disulfide bond381 ↔ 397 By similarity
Disulfide bond399 ↔ 412 By similarity

Natural variations

Alternative sequence1 – 8181Missing in isoform 3.
VSP_015762
Alternative sequence487 – 51327Missing in isoform 2 and isoform 3.
VSP_015763
Alternative sequence514 – 56653DDPSA…QNNLT → VTYLPHISPFACLCPCLPLP PCPLALSQSRQSPNSFEDQL RATQWCRERCIDSLTV in isoform 4.
VSP_015764

Experimental info

Mutagenesis381S → A: No effect on chondroitin sulfate attachment. Ref.8
Mutagenesis1231S → A: No chondroitin sulfate attachment. no effect on transport to the cell surface. Ref.8
Sequence conflict3171T → N in AAF23362. Ref.1
Sequence conflict3171T → N in AAQ04777. Ref.1
Sequence conflict3171T → N in AAQ04778. Ref.1
Sequence conflict3171T → N in AAQ04779. Ref.1
Sequence conflict3181N → H in AAH55736. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NGC-III) [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 8AB75BA1ACB11BDE

FASTA56660,406
        10         20         30         40         50         60 
MGRAGGGGPD WGPPPVLLLL GVTLVLTAGA VPARETGSAI EAEELVRSSL AWESRANDTR 

        70         80         90        100        110        120 
EEAGLPAAGE DETSWTERGS EMAAVGPGVG PEEALEASAA VTGTAWLEAD GPGLGGVTAE 

       130        140        150        160        170        180 
AGSGDAQTLP ATLQAPDEAL GSSTMPPAIP EATETSGPPS PAVHDKPSVG PELPKEIPLE 

       190        200        210        220        230        240 
VRLNLGGSTP EPTFPLQGTL ETQPASDIID IDYFEGLDSE GRGADMGSFP GSPGTSENHP 

       250        260        270        280        290        300 
DTEGETPSWS LLDLYDDFTP FDESDFYPTT SFYDDLEEEE EEEEDKDTVG GGDLEDENDL 

       310        320        330        340        350        360 
LLPSQKPGVG PGTGQPTNRW HAVPPQHTLG MVPGSSISLR PRPGDPGKDL ASGENGTECR 

       370        380        390        400        410        420 
VGFVRHNGSC RSVCDLFPSY CHNGGQCYLV ENIGAFCRCN TQDYIWHKGM RCESIITDFQ 

       430        440        450        460        470        480 
VMCVAVGSAA LVLLLLFMMT VFFAKKLYLL KTENTKLRRT NKFRTPSELH NDNFSLSTIA 

       490        500        510        520        530        540 
EGSHPNVRKF CDTPRVSSPH ARALAHYDNI VCQDDPSAPH KIQDPLKSRL KEEESFNIQN 

       550        560 
SMSPKLEGGK GDQDDLGVNC LQNNLT 

« Hide

Isoform 2 (NGC-I) [UniParc].

Checksum: 81B105D7803930A3
Show »

FASTA53957,339
Isoform 3 (NGC-II) [UniParc].

Checksum: 87CE103CCD23205E
Show »

FASTA45849,027
Isoform 4 [UniParc].

Checksum: 62DADBBC033BF0E0
Show »

FASTA56960,857

References

« Hide 'large scale' references
[1]"Genomic organization and expression pattern of mouse neuroglycan C in the cerebellar development."
Aono S., Keino H., Ono T., Yasuda Y., Tokita Y., Matsui F., Taniguchi M., Sonta S., Oohira A.
J. Biol. Chem. 275:337-342(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
Strain: C57BL/6.
Tissue: Brain.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6.
Tissue: Brain.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-566 (ISOFORM 4).
Strain: C57BL/6J.
Tissue: Eye.
[5]"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.
[6]"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: INTERACTION WITH TNR.
[7]"CALEB/NGC interacts with the Golgi-associated protein PIST."
Hassel B., Schreff M., Stuebe E.-M., Blaich U., Schumacher S.
J. Biol. Chem. 278:40136-40143(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Glycosylation site for chondroitin sulfate on the neural part-time proteoglycan, neuroglycan C."
Aono S., Tokita Y., Shuo T., Yamauchi S., Matsui F., Nakanishi K., Hirano K., Sano M., Oohira A.
J. Biol. Chem. 279:46536-46541(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF SER-38 AND SER-123, GLYCOSYLATION AT SER-123, SUBCELLULAR LOCATION.
[9]"Impaired synapse function during postnatal development in the absence of CALEB, an EGF-like protein processed by neuronal activity."
Juettner R., More M.I., Das D., Babich A., Meier J., Henning M., Erdmann B., Mueller E.-C., Otto A., Grantyn R., Rathjen F.G.
Neuron 46:233-245(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF133700 mRNA. Translation: AAF23362.1.
AF461090 mRNA. Translation: AAQ04777.1.
AF461091 mRNA. Translation: AAQ04778.1. Different initiation.
AF461092 mRNA. Translation: AAQ04779.1.
AC159372 Genomic DNA. No translation available.
AC160104 Genomic DNA. No translation available.
BC055736 mRNA. Translation: AAH55736.1.
AK053891 mRNA. Translation: BAC35578.1. Different initiation.
CCDSCCDS52936.1. [Q71M36-1]
RefSeqNP_001159745.1. NM_001166273.1. [Q71M36-1]
NP_038912.3. NM_013884.3. [Q71M36-2]
UniGeneMm.38496.

3D structure databases

ProteinModelPortalQ71M36.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ71M36. 1 interaction.

PTM databases

PhosphoSiteQ71M36.

Proteomic databases

PaxDbQ71M36.
PRIDEQ71M36.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035058; ENSMUSP00000035058; ENSMUSG00000032482. [Q71M36-1]
GeneID29873.
KEGGmmu:29873.
UCSCuc009rtq.2. mouse. [Q71M36-1]
uc009rtr.2. mouse. [Q71M36-2]
uc009rtt.1. mouse. [Q71M36-3]
uc009rtu.1. mouse. [Q71M36-4]

Organism-specific databases

CTD10675.
MGIMGI:1352747. Cspg5.

Phylogenomic databases

eggNOGNOG39505.
GeneTreeENSGT00440000034270.
HOGENOMHOG000112020.
HOVERGENHBG081361.
InParanoidQ71M36.
KOK08116.
OMALEVNCLQ.
OrthoDBEOG7VX8WW.
TreeFamTF338636.

Gene expression databases

BgeeQ71M36.
CleanExMM_CSPG5.
GenevestigatorQ71M36.

Family and domain databases

InterProIPR010555. Chon_Sulph_att.
IPR000742. EG-like_dom.
IPR009505. Neural_ProG_Cyt.
[Graphical view]
PfamPF06566. Chon_Sulph_att. 1 hit.
PF06567. Neural_ProG_Cyt. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCSPG5. mouse.
NextBio307106.
PROQ71M36.
SOURCESearch...

Entry information

Entry nameCSPG5_MOUSE
AccessionPrimary (citable) accession number: Q71M36
Secondary accession number(s): E9QN54 expand/collapse secondary AC list , Q71M37, Q7TNT8, Q8BPJ5, Q9QY32
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot