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Protein

Chondroitin proteoglycan-2

Gene

cpg-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  • chitin binding Source: UniProtKB

GO - Biological processi

  • chitin metabolic process Source: InterPro
  • eggshell formation Source: UniProtKB
  • embryo development Source: UniProtKB
  • mitotic cytokinesis Source: UniProtKB
  • regulation of cytokinesis Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiCBM14. Carbohydrate-Binding Module Family 14.

Names & Taxonomyi

Protein namesi
Recommended name:
Chondroitin proteoglycan-2
Alternative name(s):
Cytokinesis protein B0280.5
Gene namesi
Name:cpg-2
ORF Names:B0280.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiB0280.5; CE31868; WBGene00015102; cpg-2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 524506Chondroitin proteoglycan-2PRO_0000023617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 67PROSITE-ProRule annotation
Glycosylationi103 – 1031O-linked (Xyl...) (chondroitin sulfate)1 Publication
Glycosylationi119 – 1191O-linked (Xyl...) (chondroitin sulfate)1 Publication
Disulfide bondi168 ↔ 181PROSITE-ProRule annotation
Glycosylationi208 – 2081O-linked (Xyl...) (chondroitin sulfate)1 Publication
Glycosylationi212 – 2121O-linked (Xyl...) (chondroitin sulfate)1 Publication
Disulfide bondi277 ↔ 290PROSITE-ProRule annotation
Disulfide bondi337 ↔ 350PROSITE-ProRule annotation
Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi432 ↔ 445PROSITE-ProRule annotation
Glycosylationi497 – 4971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi500 ↔ 514PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

PaxDbiP41996.

Expressioni

Tissue specificityi

Expressed in the germline.1 Publication

Developmental stagei

Expressed throughout development but appears to be up-regulated in adults.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi41203. 1 interaction.
MINTiMINT-1061878.
STRINGi6239.B0280.5.

Structurei

3D structure databases

ProteinModelPortaliP41996.
SMRiP41996. Positions 27-80, 138-192, 251-295, 309-358, 415-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 7858Chitin-binding type-2 1PROSITE-ProRule annotationAdd
BLAST
Domaini135 – 19258Chitin-binding type-2 2PROSITE-ProRule annotationAdd
BLAST
Domaini244 – 30158Chitin-binding type-2 3PROSITE-ProRule annotationAdd
BLAST
Domaini306 – 36156Chitin-binding type-2 4PROSITE-ProRule annotationAdd
BLAST
Domaini400 – 45657Chitin-binding type-2 5PROSITE-ProRule annotationAdd
BLAST
Domaini469 – 52456Chitin-binding type-2 6PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi75 – 258184Gly-richAdd
BLAST

Sequence similaritiesi

Contains 6 chitin-binding type-2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG241358.
GeneTreeiENSGT00650000093766.
HOGENOMiHOG000017714.
InParanoidiP41996.
OMAiFDCSTDG.
PhylomeDBiP41996.

Family and domain databases

Gene3Di2.170.140.10. 5 hits.
InterProiIPR002557. Chitin-bd_dom.
[Graphical view]
PfamiPF01607. CBM_14. 6 hits.
[Graphical view]
SMARTiSM00494. ChtBD2. 6 hits.
[Graphical view]
SUPFAMiSSF57625. SSF57625. 6 hits.
PROSITEiPS50940. CHIT_BIND_II. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P41996-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTVAALTLL AFATAANGQF LQDCTNALDG LYALGECEPQ FLTCSGGIAR
60 70 80 90 100
IMDCPADLIY NEPLLICDWR HNVIGCEGSG ESSGETSGEG SGESSGEASG
110 120 130 140 150
EGSGEASGEG SGEASGEGSG EASGEGSGSG EETVENVCEN LEDGAYSSGG
160 170 180 190 200
CTTYYFFCTT NTARFLSCPT PLFYDADSQK CIWKSLVEEC KEDLTITDGS
210 220 230 240 250
GETSGEGSGE ASGEASGEGS GEASGESSGQ GSGEASGEGS GELEPTCEGK
260 270 280 290 300
ADGIHPNGVC STNFLTCSGG IARIMDCPAS LVFNPTILVC DWPRDVAECA
310 320 330 340 350
GLPTPQPTCE EDGYFSFGQC SSSFTACTNG RAIVMFCPAG LKFSESTVRC
360 370 380 390 400
DYESNVSECQ ETSGEESGEA SGEQSGEGSG EASGEASGES SGEGSGVEEQ
410 420 430 440 450
NQCVGLDNGL HAIGCSPRVL SCQNGHVDIF ECPSSLVFND QSLICDYPQT
460 470 480 490 500
SLKCLIEDTI LIDETPIAAF DCSTDGLFSD GLCSATYHQC TAGQLINFTC
510 520
AASNAVFSAA NTECVDSSTL LQCH
Length:524
Mass (Da):53,652
Last modified:August 15, 2003 - v3
Checksum:iFFCB9A750385FB34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ340624 mRNA. Translation: ABC65812.1.
FO080148 Genomic DNA. Translation: CCD61602.1.
PIRiT15299.
RefSeqiNP_498551.3. NM_066150.10.
UniGeneiCel.17405.

Genome annotation databases

EnsemblMetazoaiB0280.5; B0280.5; WBGene00015102.
GeneIDi175991.
KEGGicel:CELE_B0280.5.
UCSCiB0280.5. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ340624 mRNA. Translation: ABC65812.1.
FO080148 Genomic DNA. Translation: CCD61602.1.
PIRiT15299.
RefSeqiNP_498551.3. NM_066150.10.
UniGeneiCel.17405.

3D structure databases

ProteinModelPortaliP41996.
SMRiP41996. Positions 27-80, 138-192, 251-295, 309-358, 415-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi41203. 1 interaction.
MINTiMINT-1061878.
STRINGi6239.B0280.5.

Protein family/group databases

CAZyiCBM14. Carbohydrate-Binding Module Family 14.

Proteomic databases

PaxDbiP41996.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiB0280.5; B0280.5; WBGene00015102.
GeneIDi175991.
KEGGicel:CELE_B0280.5.
UCSCiB0280.5. c. elegans.

Organism-specific databases

CTDi175991.
WormBaseiB0280.5; CE31868; WBGene00015102; cpg-2.

Phylogenomic databases

eggNOGiNOG241358.
GeneTreeiENSGT00650000093766.
HOGENOMiHOG000017714.
InParanoidiP41996.
OMAiFDCSTDG.
PhylomeDBiP41996.

Miscellaneous databases

NextBioi890638.
PROiP41996.

Family and domain databases

Gene3Di2.170.140.10. 5 hits.
InterProiIPR002557. Chitin-bd_dom.
[Graphical view]
PfamiPF01607. CBM_14. 6 hits.
[Graphical view]
SMARTiSM00494. ChtBD2. 6 hits.
[Graphical view]
SUPFAMiSSF57625. SSF57625. 6 hits.
PROSITEiPS50940. CHIT_BIND_II. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCPG2_CAEEL
AccessioniPrimary (citable) accession number: P41996
Secondary accession number(s): Q1A3T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 15, 2003
Last modified: April 29, 2015
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.