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Q17802 (CPG1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 81. 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 proteoglycan 1
Alternative name(s):
Cell junction protein 1
Cytokinesis protein cej-1
Gene names
Name:cpg-1
Synonyms:cej-1
ORF Names:C07G2.1
OrganismCaenorhabditis elegans
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length584 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for polar body extrusion during cytokinesis in embryo development. Affects cortical granule size. Has roles in meiotic chromosome segregation, osmotic barrier function and polarization in conjunction with cpg-2. Binds chitin. Ref.1 Ref.4 Ref.5 Ref.6

Tissue specificity

Expressed in the germline. Ref.3

Developmental stage

Expressed throughout development but appears to be up-regulated in adults. Ref.3

Disruption phenotype

Worms lacking cpg-1 and cpg-2 exhibit defects in cytokinesis during embryo development, more specifically meiotic chromosome segregation, polar-body extrusion, osmotic barrier function and polarization. Embryos lacking cpg-1 and cpg-2 proteins have multiple nuclei lacking plasma membranes and may also have weak egg shells. Oocytes lacking cpg-1 and cpg-2 show cortical granules that are reduced in size. Ref.1

Sequence similarities

Contains 3 chitin-binding type-2 domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform a (identifier: Q17802-1)

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 b (identifier: Q17802-2)

The sequence of this isoform differs from the canonical sequence as follows:
     124-547: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 584567Chondroitin proteoglycan 1
PRO_0000023616

Regions

Domain58 – 11558Chitin-binding type-2 1
Domain211 – 26858Chitin-binding type-2 2
Domain524 – 57855Chitin-binding type-2 3

Amino acid modifications

Glycosylation501O-linked (Xyl...) (chondroitin sulfate) Ref.1
Glycosylation2681N-linked (GlcNAc...) Potential
Disulfide bond91 ↔ 104 By similarity
Disulfide bond244 ↔ 257 By similarity
Disulfide bond554 ↔ 567 By similarity

Natural variations

Alternative sequence124 – 547424Missing in isoform b.
VSP_050569

Sequences

Sequence LengthMass (Da)Tools
Isoform a [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 76F8F613E239DD53

FASTA58461,805
        10         20         30         40         50         60 
MTLKPVLLAF LVASAYAQYG VAGMYENLPL ETTTLDGSGD GSGADNGFVS GADAVAIDTD 

        70         80         90        100        110        120 
CSTKEDGLYA IGGCSPQFLT CSGGISRIMD CPADLIYDPR IVACEYSYNV PQCGGVPQDV 

       130        140        150        160        170        180 
TSTQEAYPSE ETTVNPYAPV EEATTTPAED VTVPEETTTE AYAPVDDYST TTPAEDVPVP 

       190        200        210        220        230        240 
VETTASPYAP IVPYTTGAPA ADEPVTRSAV TKSCVGKADG FYSFGECSDH YTACSNGYLI 

       250        260        270        280        290        300 
PMQCPARLAF DEARVICDYV MNVPECTNGS GNDEGSADET TPESSGEMPY SNGYGYEETT 

       310        320        330        340        350        360 
TVAEDVPSTK DYAEPIAAAY VARYPSEKTT AENVPTTTIG YEPEVVETTA PYVEETTTTV 

       370        380        390        400        410        420 
GYKPEVEETT TEAEVPTTTV GYEPEIVETT APYVEETTTA ADVPSTTAVY EPEVVETTTE 

       430        440        450        460        470        480 
AEVPTTTTVG YEPEVVETTV PYVEETTTAA DVPTTTVGYE PEVEETTTEA EVPTTTVGYE 

       490        500        510        520        530        540 
SEVVETTAAD IPTTTIGYAP IVVESTTAAD VPTTTVPAET TTEVPACVEG ATAIEPCSQH 

       550        560        570        580 
YKNCVNGQEA IFICENGLFF SPEQARCAPA DQIAECHQTT VQYY 

« Hide

Isoform b [UniParc].

Checksum: 0C6F93A63073925C
Show »

FASTA16016,897

References

« Hide 'large scale' references
[1]"Identification of novel chondroitin proteoglycans in Caenorhabditis elegans: embryonic cell division depends on CPG-1 and CPG-2."
Olson S.K., Bishop J.R., Yates J.R., Oegema K., Esko J.D.
J. Cell Biol. 173:985-994(2006) [PubMed: 16785326] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT SER-50, FUNCTION, DISRUPTION PHENOTYPE.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
Strain: Bristol N2.
[3]"A global profile of germline gene expression in C. elegans."
Reinke V., Smith H.E., Nance J., Wang J., Van Doren C., Begley R., Jones S.J.M., Davis E.B., Scherer S., Ward S., Kim S.K.
Mol. Cell 6:605-616(2000) [PubMed: 11030340] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[4]"Identification of in vivo mRNA targets of GLD-1, a maxi-KH motif containing protein required for C. elegans germ cell development."
Lee M.-H., Schedl T.
Genes Dev. 15:2408-2420(2001) [PubMed: 11562350] [Abstract]
Cited for: FUNCTION.
[5]"The eggshell is required for meiotic fidelity, polar-body extrusion and polarization of the C. elegans embryo."
Johnston W.L., Krizus A., Dennis J.W.
BMC Biol. 4:35-35(2006) [PubMed: 17042944] [Abstract]
Cited for: FUNCTION.
[6]"Cortical granule exocytosis in C. elegans is regulated by cell cycle components including separase."
Bembenek J.N., Richie C.T., Squirrell J.M., Campbell J.M., Eliceiri K.W., Poteryaev D., Spang A., Golden A., White J.G.
Development 134:3837-3848(2007) [PubMed: 17913784] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ340623 mRNA. Translation: ABC65811.1.
Z32840 Genomic DNA. Translation: CAA83679.1.
Z32840 Genomic DNA. Translation: CAD91625.1.
PIRT19061.
RefSeqNP_001021159.1. NM_001025988.4.
NP_001021160.1. NM_001025989.2.
UniGeneCel.23350.

3D structure databases

ProteinModelPortalQ17802.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-27081N.
MINTMINT-1045469.
STRINGQ17802.

Protein family/group databases

CAZyCBM14. Carbohydrate-Binding Module Family 14.

Proteomic databases

PRIDEQ17802.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC07G2.1a.1; C07G2.1a.1; C07G2.1.
C07G2.1a.2; C07G2.1a.2; C07G2.1.
GeneID175586.
KEGGcel:C07G2.1.
UCSCC07G2.1a.1. c. elegans.

Organism-specific databases

CTD175586.
WormBaseC07G2.1a; CE00665; WBGene00000465; cpg-1.
C07G2.1b; CE33971; WBGene00000465; cpg-1.

Phylogenomic databases

GeneTreeEMGT00050000000345.
InParanoidQ17802.
OMATTVGYEP.

Gene expression databases

ArrayExpressQ17802.

Family and domain databases

InterProIPR002557. Chitin-bd_dom.
[Graphical view]
Gene3DG3DSA:2.170.140.10. Chitin-bd_dom. 3 hits.
PfamPF01607. CBM_14. 3 hits.
[Graphical view]
SMARTSM00494. ChtBD2. 3 hits.
[Graphical view]
SUPFAMSSF57625. Chitin_bind_PerA. 3 hits.
PROSITEPS50940. CHIT_BIND_II. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio888782.

Entry information

Entry nameCPG1_CAEEL
AccessionPrimary (citable) accession number: Q17802
Secondary accession number(s): Q1A3T6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 1, 1996
Last modified: September 21, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families