ID   CPG1_CAEBR              Reviewed;         686 AA.
AC   A8WVU7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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; ORFNames=CBG03957;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAP24760.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP24760.1};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Required for polar body extrusion during cytokinesis in
CC       embryo development. Affects cortical granule size. Shown to have roles
CC       in meiotic chromosome segregation, osmotic barrier function and
CC       polarization in conjunction with cpg-2. Binds chitin (By similarity).
CC       {ECO:0000250|UniProtKB:Q17802}.
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DR   EMBL; HE600906; CAP24760.1; -; Genomic_DNA.
DR   RefSeq; XP_002639373.1; XM_002639327.1.
DR   AlphaFoldDB; A8WVU7; -.
DR   GeneID; 8581366; -.
DR   KEGG; cbr:CBG_03957; -.
DR   CTD; 8581366; -.
DR   WormBase; CBG03957a; CBP41672; WBGene00026714; Cbr-cpg-1.
DR   eggNOG; ENOG502S9IS; Eukaryota.
DR   HOGENOM; CLU_033369_0_0_1; -.
DR   InParanoid; A8WVU7; -.
DR   OMA; TTVGYEP; -.
DR   OrthoDB; 1174178at2759; -.
DR   Proteomes; UP000008549; Chromosome I.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; ISS:UniProtKB.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   Pfam; PF01607; CBM_14; 2.
DR   SMART; SM00494; ChtBD2; 2.
DR   SUPFAM; SSF57625; SSF57625; 2.
DR   PROSITE; PS50940; CHIT_BIND_II; 2.
PE   3: Inferred from homology;
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..686
FT                   /note="Chondroitin proteoglycan 1"
FT                   /id="PRO_0000320219"
FT   DOMAIN          63..120
FT                   /note="Chitin-binding type-2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          228..285
FT                   /note="Chitin-binding type-2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   REGION          284..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        635
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        664
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        96..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        261..274
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ   SEQUENCE   686 AA;  73321 MW;  6C43466951D120A8 CRC64;
     MLPKSVLIVA FLVASSSAQY GVTGMYENLP LESTTVEASG EGSGYNESND DGFVTGADAV
     AIDTDCSTKE DGLYAIGGCS PQFLTCSGGI ARIMDCPANL IYDQRIIACE YSYNVPECSG
     VPQDVSSTQA YYPATEETTP AENVTVPAET TVDPYAPVEV ATTAAPSEDV PVETTASPYA
     PVEVETTTAP AEDVTVPEET TVAPYAPVEV YTTAAPANDE PVTRTLLDKT CNGKADGFYS
     FGQCSDHYIA CSNGYTIPMQ CPARLSFDEA RVICDYTMNV PECQNGSGNY EGSAEETTTE
     ASGELPYSNG YGYEETTTAA ADVPSTEGYA PETTAEAWVA PYRLESTTAA DVPTTTVGYA
     PEVIEETTTS EYVEETTTAA DVSTTTTVEY VPEVTETTTA PYVEETTTAE YVEETTTAAD
     VPTTTTVAYA PEVTETTTVP YIEETTTVEE ATTAADVPTT TGYVPEVIET TTTPYVEETT
     TAEYVEETST AADVPTTTTV AYAPEVTETT TVPYIEETTT VEEATTAADV PTTTGYVPEV
     IETTTTPYVE ETTTVEETTT TTVAYAPEVV ETTTTPYVEE STTTPYVEET TTALMFHPPQ
     SKATKLPQIH HPASKEHLLS SHAHKTIETV SMDMNLSSSA SRDSSSLQSK DDAQLLTKLR
     SATNRTSTKE ATTRTQNMHA HYHRNH