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 27-MAR-2024, entry version 72. 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}. 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; HE600906; CAP24760.1; -; Genomic_DNA. DR RefSeq; XP_002639373.1; XM_002639327.1. DR AlphaFoldDB; A8WVU7; -. DR STRING; 6238.A8WVU7; -. DR GlyCosmos; A8WVU7; 5 sites, No reported glycans. 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; LRHEDCN; -. DR OrthoDB; 3616561at2759; -. 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 Gene3D; 2.170.140.10; Chitin binding domain; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. 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; Invertebrate chitin-binding proteins; 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 //