ID CPG2_CAEEL Reviewed; 524 AA.
AC P41996; Q1A3T5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 3.
DT 01-MAY-2013, entry version 90.
DE RecName: Full=Chondroitin proteoglycan-2;
DE AltName: Full=Cytokinesis protein B0280.5;
DE Flags: Precursor;
GN Name=cpg-2; ORFNames=B0280.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP GLYCOSYLATION AT SER-103; SER-119; SER-208 AND SER-212, FUNCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16785326; DOI=10.1083/jcb.200603003;
RA Olson S.K., Bishop J.R., Yates J.R., Oegema K., Esko J.D.;
RT "Identification of novel chondroitin proteoglycans in Caenorhabditis
RT elegans: embryonic cell division depends on CPG-1 and CPG-2.";
RL J. Cell Biol. 173:985-994(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for
RT investigating biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11030340; DOI=10.1016/S1097-2765(00)00059-9;
RA Reinke V., Smith H.E., Nance J., Wang J., Van Doren C., Begley R.,
RA Jones S.J.M., Davis E.B., Scherer S., Ward S., Kim S.K.;
RT "A global profile of germline gene expression in C. elegans.";
RL Mol. Cell 6:605-616(2000).
RN [4]
RP FUNCTION.
RX PubMed=11562350; DOI=10.1101/gad.915901;
RA Lee M.-H., Schedl T.;
RT "Identification of in vivo mRNA targets of GLD-1, a maxi-KH motif
RT containing protein required for C. elegans germ cell development.";
RL Genes Dev. 15:2408-2420(2001).
RN [5]
RP FUNCTION.
RX PubMed=17042944; DOI=10.1186/1741-7007-4-35;
RA Johnston W.L., Krizus A., Dennis J.W.;
RT "The eggshell is required for meiotic fidelity, polar-body extrusion
RT and polarization of the C. elegans embryo.";
RL BMC Biol. 4:35-35(2006).
RN [6]
RP FUNCTION.
RX PubMed=17913784; DOI=10.1242/dev.011361;
RA Bembenek J.N., Richie C.T., Squirrell J.M., Campbell J.M.,
RA Eliceiri K.W., Poteryaev D., Spang A., Golden A., White J.G.;
RT "Cortical granule exocytosis in C. elegans is regulated by cell cycle
RT components including separase.";
RL Development 134:3837-3848(2007).
CC -!- FUNCTION: Required for polar body extrusion during cytokinesis in
CC embryo development. Affects cortical granule size. Has roles in
CC meiotic chromosome segregation, osmotic barrier function and
CC polarization in conjunction with cpg-2. Binds chitin.
CC -!- TISSUE SPECIFICITY: Expressed in the germline.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development but appears
CC to be up-regulated in adults.
CC -!- DISRUPTION PHENOTYPE: Worms lacking cpg-2 and cpg-1 exhibit
CC defects in cytokinesis during embryo development more specifically
CC meiotic chromosome segregation, polar-body extrusion, osmotic
CC barrier function and polarization. Embryos lacking cpg-2 and cpg-1
CC proteins have multiple nuclei lacking plasma membranes and may
CC also have weak egg shells. Oocytes lacking cpg-2 and cpg-1 show
CC cortical granules that are reduced in size.
CC -!- SIMILARITY: Contains 6 chitin-binding type-2 domains.
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DR EMBL; DQ340624; ABC65812.1; -; mRNA.
DR EMBL; FO080148; CCD61602.1; -; Genomic_DNA.
DR PIR; T15299; T15299.
DR RefSeq; NP_498551.3; NM_066150.10.
DR UniGene; Cel.17405; -.
DR ProteinModelPortal; P41996; -.
DR SMR; P41996; 26-78, 137-194, 246-300, 307-358, 406-455.
DR MINT; MINT-1061878; -.
DR STRING; 6239.B0280.5; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR PaxDb; P41996; -.
DR EnsemblMetazoa; B0280.5.1; B0280.5.1; B0280.5.
DR EnsemblMetazoa; B0280.5.2; B0280.5.2; B0280.5.
DR GeneID; 175991; -.
DR KEGG; cel:CELE_B0280.5; -.
DR UCSC; B0280.5; c. elegans.
DR CTD; 175991; -.
DR WormBase; B0280.5; CE31868; WBGene00015102; cpg-2.
DR eggNOG; NOG241358; -.
DR GeneTree; ENSGT00650000093766; -.
DR HOGENOM; HOG000017714; -.
DR InParanoid; P41996; -.
DR OMA; FDCSTDG; -.
DR NextBio; 890638; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0006030; P:chitin metabolic process; IEA:InterPro.
DR GO; GO:0000281; P:cytokinesis after mitosis; IMP:UniProtKB.
DR GO; GO:0030703; P:eggshell formation; NAS:UniProtKB.
DR GO; GO:0009790; P:embryo development; IMP:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IGI:WormBase.
DR Gene3D; 2.170.140.10; -; 5.
DR InterPro; IPR002557; Chitin-bd_dom.
DR Pfam; PF01607; CBM_14; 6.
DR SMART; SM00494; ChtBD2; 6.
DR SUPFAM; SSF57625; Chitin_bind_PerA; 6.
DR PROSITE; PS50940; CHIT_BIND_II; 6.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chitin-binding; Complete proteome;
KW Developmental protein; Disulfide bond; Glycoprotein; Proteoglycan;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1 18 Potential.
FT CHAIN 19 524 Chondroitin proteoglycan-2.
FT /FTId=PRO_0000023617.
FT DOMAIN 21 78 Chitin-binding type-2 1.
FT DOMAIN 135 192 Chitin-binding type-2 2.
FT DOMAIN 244 301 Chitin-binding type-2 3.
FT DOMAIN 306 361 Chitin-binding type-2 4.
FT DOMAIN 400 456 Chitin-binding type-2 5.
FT DOMAIN 469 524 Chitin-binding type-2 6.
FT COMPBIAS 75 258 Gly-rich.
FT CARBOHYD 103 103 O-linked (Xyl...) (chondroitin sulfate).
FT CARBOHYD 119 119 O-linked (Xyl...) (chondroitin sulfate).
FT CARBOHYD 208 208 O-linked (Xyl...) (chondroitin sulfate).
FT CARBOHYD 212 212 O-linked (Xyl...) (chondroitin sulfate).
FT CARBOHYD 355 355 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 497 497 N-linked (GlcNAc...) (Potential).
FT DISULFID 54 67 By similarity.
FT DISULFID 168 181 By similarity.
FT DISULFID 277 290 By similarity.
FT DISULFID 337 350 By similarity.
FT DISULFID 432 445 By similarity.
FT DISULFID 500 514 By similarity.
SQ SEQUENCE 524 AA; 53652 MW; FFCB9A750385FB34 CRC64;
MKTVAALTLL AFATAANGQF LQDCTNALDG LYALGECEPQ FLTCSGGIAR IMDCPADLIY
NEPLLICDWR HNVIGCEGSG ESSGETSGEG SGESSGEASG EGSGEASGEG SGEASGEGSG
EASGEGSGSG EETVENVCEN LEDGAYSSGG CTTYYFFCTT NTARFLSCPT PLFYDADSQK
CIWKSLVEEC KEDLTITDGS GETSGEGSGE ASGEASGEGS GEASGESSGQ GSGEASGEGS
GELEPTCEGK ADGIHPNGVC STNFLTCSGG IARIMDCPAS LVFNPTILVC DWPRDVAECA
GLPTPQPTCE EDGYFSFGQC SSSFTACTNG RAIVMFCPAG LKFSESTVRC DYESNVSECQ
ETSGEESGEA SGEQSGEGSG EASGEASGES SGEGSGVEEQ NQCVGLDNGL HAIGCSPRVL
SCQNGHVDIF ECPSSLVFND QSLICDYPQT SLKCLIEDTI LIDETPIAAF DCSTDGLFSD
GLCSATYHQC TAGQLINFTC AASNAVFSAA NTECVDSSTL LQCH
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