CPG1_CAEEL
ID CPG1_CAEEL Reviewed; 584 AA.
AC Q17802; Q1A3T6;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Chondroitin proteoglycan 1;
DE AltName: Full=Cell junction protein 1;
DE AltName: Full=Cytokinesis protein cej-1;
DE Flags: Precursor;
GN Name=cpg-1; Synonyms=cej-1; ORFNames=C07G2.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:CAA83679.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), IDENTIFICATION BY MASS
RP SPECTROMETRY, GLYCOSYLATION AT SER-50, FUNCTION, AND 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], AND ALTERNATIVE SPLICING.
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] {ECO:0000305}
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000305};
CC IsoId=Q17802-1; Sequence=Displayed;
CC Name=b {ECO:0000305};
CC IsoId=Q17802-2; Sequence=VSP_050569;
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-1 and cpg-2 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-1 and cpg-2 proteins have
CC multiple nuclei lacking plasma membranes and may also have weak egg
CC shells. Oocytes lacking cpg-1 and cpg-2 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; DQ340623; ABC65811.1; -; mRNA.
DR EMBL; Z32840; CAA83679.1; -; Genomic_DNA.
DR EMBL; Z32840; CAD91625.1; -; Genomic_DNA.
DR PIR; T19061; T19061.
DR RefSeq; NP_001021159.1; NM_001025988.5. [Q17802-1]
DR RefSeq; NP_001021160.1; NM_001025989.3. [Q17802-2]
DR AlphaFoldDB; Q17802; -.
DR BioGRID; 40822; 4.
DR DIP; DIP-27081N; -.
DR STRING; 6239.C07G2.1a; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR iPTMnet; Q17802; -.
DR EPD; Q17802; -.
DR PaxDb; Q17802; -.
DR PeptideAtlas; Q17802; -.
DR EnsemblMetazoa; C07G2.1a.1; C07G2.1a.1; WBGene00000465. [Q17802-1]
DR EnsemblMetazoa; C07G2.1b.1; C07G2.1b.1; WBGene00000465. [Q17802-2]
DR GeneID; 175586; -.
DR KEGG; cel:CELE_C07G2.1; -.
DR UCSC; C07G2.1a.1; c. elegans. [Q17802-1]
DR CTD; 175586; -.
DR WormBase; C07G2.1a; CE00665; WBGene00000465; cpg-1. [Q17802-1]
DR WormBase; C07G2.1b; CE33971; WBGene00000465; cpg-1. [Q17802-2]
DR eggNOG; ENOG502RXTR; Eukaryota.
DR GeneTree; ENSGT00970000196129; -.
DR HOGENOM; CLU_033369_0_0_1; -.
DR InParanoid; Q17802; -.
DR OMA; TTVGYEP; -.
DR OrthoDB; 1610313at2759; -.
DR PRO; PR:Q17802; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000465; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0030312; C:external encapsulating structure; IDA:WormBase.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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; 3.
DR SMART; SM00494; ChtBD2; 3.
DR SUPFAM; SSF57625; SSF57625; 3.
DR PROSITE; PS50940; CHIT_BIND_II; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Chitin-binding;
KW Developmental protein; Disulfide bond; Glycoprotein; Proteoglycan;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..584
FT /note="Chondroitin proteoglycan 1"
FT /id="PRO_0000023616"
FT DOMAIN 58..115
FT /note="Chitin-binding type-2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 211..268
FT /note="Chitin-binding type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 524..578
FT /note="Chitin-binding type-2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT REGION 267..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 50
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:16785326"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 244..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 554..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT VAR_SEQ 124..547
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_050569"
SQ SEQUENCE 584 AA; 61805 MW; 76F8F613E239DD53 CRC64;
MTLKPVLLAF LVASAYAQYG VAGMYENLPL ETTTLDGSGD GSGADNGFVS GADAVAIDTD
CSTKEDGLYA IGGCSPQFLT CSGGISRIMD CPADLIYDPR IVACEYSYNV PQCGGVPQDV
TSTQEAYPSE ETTVNPYAPV EEATTTPAED VTVPEETTTE AYAPVDDYST TTPAEDVPVP
VETTASPYAP IVPYTTGAPA ADEPVTRSAV TKSCVGKADG FYSFGECSDH YTACSNGYLI
PMQCPARLAF DEARVICDYV MNVPECTNGS GNDEGSADET TPESSGEMPY SNGYGYEETT
TVAEDVPSTK DYAEPIAAAY VARYPSEKTT AENVPTTTIG YEPEVVETTA PYVEETTTTV
GYKPEVEETT TEAEVPTTTV GYEPEIVETT APYVEETTTA ADVPSTTAVY EPEVVETTTE
AEVPTTTTVG YEPEVVETTV PYVEETTTAA DVPTTTVGYE PEVEETTTEA EVPTTTVGYE
SEVVETTAAD IPTTTIGYAP IVVESTTAAD VPTTTVPAET TTEVPACVEG ATAIEPCSQH
YKNCVNGQEA IFICENGLFF SPEQARCAPA DQIAECHQTT VQYY
