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P41996 (CPG2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 96. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chondroitin proteoglycan-2
Alternative name(s):
Cytokinesis protein B0280.5
Gene names
Name:cpg-2
ORF Names:B0280.5
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length524 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-2 and cpg-1 exhibit defects in cytokinesis during embryo development more specifically meiotic chromosome segregation, polar-body extrusion, osmotic barrier function and polarization. Embryos lacking cpg-2 and cpg-1 proteins have multiple nuclei lacking plasma membranes and may also have weak egg shells. Oocytes lacking cpg-2 and cpg-1 show cortical granules that are reduced in size. Ref.1

Sequence similarities

Contains 6 chitin-binding type-2 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 524506Chondroitin proteoglycan-2
PRO_0000023617

Regions

Domain21 – 7858Chitin-binding type-2 1
Domain135 – 19258Chitin-binding type-2 2
Domain244 – 30158Chitin-binding type-2 3
Domain306 – 36156Chitin-binding type-2 4
Domain400 – 45657Chitin-binding type-2 5
Domain469 – 52456Chitin-binding type-2 6
Compositional bias75 – 258184Gly-rich

Amino acid modifications

Glycosylation1031O-linked (Xyl...) (chondroitin sulfate) Ref.1
Glycosylation1191O-linked (Xyl...) (chondroitin sulfate) Ref.1
Glycosylation2081O-linked (Xyl...) (chondroitin sulfate) Ref.1
Glycosylation2121O-linked (Xyl...) (chondroitin sulfate) Ref.1
Glycosylation3551N-linked (GlcNAc...) Potential
Glycosylation4971N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 67 By similarity
Disulfide bond168 ↔ 181 By similarity
Disulfide bond277 ↔ 290 By similarity
Disulfide bond337 ↔ 350 By similarity
Disulfide bond432 ↔ 445 By similarity
Disulfide bond500 ↔ 514 By similarity

Sequences

Sequence LengthMass (Da)Tools
P41996 [UniParc].

Last modified August 15, 2003. Version 3.
Checksum: FFCB9A750385FB34

FASTA52453,652
        10         20         30         40         50         60 
MKTVAALTLL AFATAANGQF LQDCTNALDG LYALGECEPQ FLTCSGGIAR IMDCPADLIY 

        70         80         90        100        110        120 
NEPLLICDWR HNVIGCEGSG ESSGETSGEG SGESSGEASG EGSGEASGEG SGEASGEGSG 

       130        140        150        160        170        180 
EASGEGSGSG EETVENVCEN LEDGAYSSGG CTTYYFFCTT NTARFLSCPT PLFYDADSQK 

       190        200        210        220        230        240 
CIWKSLVEEC KEDLTITDGS GETSGEGSGE ASGEASGEGS GEASGESSGQ GSGEASGEGS 

       250        260        270        280        290        300 
GELEPTCEGK ADGIHPNGVC STNFLTCSGG IARIMDCPAS LVFNPTILVC DWPRDVAECA 

       310        320        330        340        350        360 
GLPTPQPTCE EDGYFSFGQC SSSFTACTNG RAIVMFCPAG LKFSESTVRC DYESNVSECQ 

       370        380        390        400        410        420 
ETSGEESGEA SGEQSGEGSG EASGEASGES SGEGSGVEEQ NQCVGLDNGL HAIGCSPRVL 

       430        440        450        460        470        480 
SCQNGHVDIF ECPSSLVFND QSLICDYPQT SLKCLIEDTI LIDETPIAAF DCSTDGLFSD 

       490        500        510        520 
GLCSATYHQC TAGQLINFTC AASNAVFSAA NTECVDSSTL LQCH 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT SER-103; SER-119; SER-208 AND SER-212, 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ340624 mRNA. Translation: ABC65812.1.
FO080148 Genomic DNA. Translation: CCD61602.1.
PIRT15299.
RefSeqNP_498551.3. NM_066150.10.
UniGeneCel.17405.

3D structure databases

ProteinModelPortalP41996.
SMRP41996. Positions 27-80, 138-192, 251-295, 309-358, 415-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid41203. 1 interaction.
MINTMINT-1061878.
STRING6239.B0280.5.

Protein family/group databases

CAZyCBM14. Carbohydrate-Binding Module Family 14.

Proteomic databases

PaxDbP41996.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaB0280.5; B0280.5; WBGene00015102.
GeneID175991.
KEGGcel:CELE_B0280.5.
UCSCB0280.5. c. elegans.

Organism-specific databases

CTD175991.
WormBaseB0280.5; CE31868; WBGene00015102; cpg-2.

Phylogenomic databases

eggNOGNOG241358.
GeneTreeENSGT00650000093766.
HOGENOMHOG000017714.
InParanoidP41996.
OMAFDCSTDG.
PhylomeDBP41996.

Family and domain databases

Gene3D2.170.140.10. 5 hits.
InterProIPR002557. Chitin-bd_dom.
[Graphical view]
PfamPF01607. CBM_14. 6 hits.
[Graphical view]
SMARTSM00494. ChtBD2. 6 hits.
[Graphical view]
SUPFAMSSF57625. SSF57625. 6 hits.
PROSITEPS50940. CHIT_BIND_II. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio890638.

Entry information

Entry nameCPG2_CAEEL
AccessionPrimary (citable) accession number: P41996
Secondary accession number(s): Q1A3T5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 15, 2003
Last modified: June 11, 2014
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

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