CPG2_CAEEL
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 03-AUG-2022, entry version 138.
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 Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC 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 investigating
RT 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 and
RT 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., Eliceiri K.W.,
RA 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 meiotic
CC chromosome segregation, osmotic barrier function and polarization in
CC conjunction with cpg-2. Binds chitin. {ECO:0000269|PubMed:11562350,
CC ECO:0000269|PubMed:16785326, ECO:0000269|PubMed:17042944,
CC ECO:0000269|PubMed:17913784}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline.
CC {ECO:0000269|PubMed:11030340}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development but appears to be
CC up-regulated in adults. {ECO:0000269|PubMed:11030340}.
CC -!- DISRUPTION PHENOTYPE: Worms lacking cpg-2 and cpg-1 exhibit defects in
CC cytokinesis during embryo development more specifically meiotic
CC chromosome segregation, polar-body extrusion, osmotic barrier function
CC and polarization. Embryos lacking cpg-2 and cpg-1 proteins have
CC multiple nuclei lacking plasma membranes and may also have weak egg
CC shells. Oocytes lacking cpg-2 and cpg-1 show cortical granules that are
CC reduced in size. {ECO:0000269|PubMed:16785326}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; P41996; -.
DR SMR; P41996; -.
DR BioGRID; 41203; 8.
DR STRING; 6239.B0280.5; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR iPTMnet; P41996; -.
DR EPD; P41996; -.
DR PaxDb; P41996; -.
DR PeptideAtlas; P41996; -.
DR EnsemblMetazoa; B0280.5.1; B0280.5.1; WBGene00015102.
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; ENOG502RXZX; Eukaryota.
DR GeneTree; ENSGT00970000196129; -.
DR HOGENOM; CLU_041716_0_0_1; -.
DR InParanoid; P41996; -.
DR OMA; VEQYCPN; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; P41996; -.
DR PRO; PR:P41996; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015102; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0030312; C:external encapsulating structure; IDA:WormBase.
DR GO; GO:0098595; C:perivitelline space; IDA:WormBase.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0030703; P:eggshell formation; IGI:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IGI:WormBase.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR Pfam; PF01607; CBM_14; 6.
DR SMART; SM00494; ChtBD2; 6.
DR SUPFAM; SSF57625; SSF57625; 6.
DR PROSITE; PS50940; CHIT_BIND_II; 6.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chitin-binding; Developmental protein;
KW Disulfide bond; Glycoprotein; Proteoglycan; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..524
FT /note="Chondroitin proteoglycan-2"
FT /id="PRO_0000023617"
FT DOMAIN 21..78
FT /note="Chitin-binding type-2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 135..192
FT /note="Chitin-binding type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 244..301
FT /note="Chitin-binding type-2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 306..361
FT /note="Chitin-binding type-2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 400..456
FT /note="Chitin-binding type-2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 469..524
FT /note="Chitin-binding type-2 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT REGION 78..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 103
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:16785326"
FT CARBOHYD 119
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:16785326"
FT CARBOHYD 208
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:16785326"
FT CARBOHYD 212
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:16785326"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 168..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 277..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 337..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 432..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 500..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
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
