ID   CPG2_CAEBR              Reviewed;         491 AA.
AC   A8XWX5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Chondroitin proteoglycan 2;
DE   Flags: Precursor;
GN   Name=cpg-2; ORFNames=CBG20011;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
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:P41996}.
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DR   EMBL; HE601481; CAP37144.2; -; Genomic_DNA.
DR   AlphaFoldDB; A8XWX5; -.
DR   SMR; A8XWX5; -.
DR   STRING; 6238.CBG20011; -.
DR   EnsemblMetazoa; CBG20011.1; CBG20011.1; WBGene00039115.
DR   WormBase; CBG20011; CBP27389; WBGene00039115; Cbr-cpg-2.
DR   eggNOG; ENOG502RXZX; Eukaryota.
DR   HOGENOM; CLU_041716_0_0_1; -.
DR   InParanoid; A8XWX5; -.
DR   OMA; VEQYCPN; -.
DR   OrthoDB; 1174178at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
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; 6.
DR   SMART; SM00494; ChtBD2; 6.
DR   SUPFAM; SSF57625; SSF57625; 6.
DR   PROSITE; PS50940; CHIT_BIND_II; 6.
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..491
FT                   /note="Chondroitin proteoglycan 2"
FT                   /id="PRO_0000320220"
FT   DOMAIN          21..78
FT                   /note="Chitin-binding type-2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          125..182
FT                   /note="Chitin-binding type-2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          217..274
FT                   /note="Chitin-binding type-2 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          279..334
FT                   /note="Chitin-binding type-2 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          367..423
FT                   /note="Chitin-binding type-2 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DOMAIN          436..491
FT                   /note="Chitin-binding type-2 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   REGION          80..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        197
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        201
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        158..171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        250..263
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        310..323
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        399..412
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        467..481
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ   SEQUENCE   491 AA;  50710 MW;  70D20DFA6869A87C CRC64;
     MKTIVALGLL ALATAASGQF LQDCTNALDG LYAIGNCESQ FLTCSGGIAR IMDCPADLIY
     NEPLLICDWR HNVVGCEGSG EASGEQSGEG SGEASGEGSG EASGEGSGEA SGEGSGSGEG
     SGEENNVCEG LEDGAYSSGG CTTYYFFCTD NTARFLSCPT PLFYDVATQK CAWKALVEEC
     NGEIIIDGSG ETSGEGSGEA SGENSGENSG EGSGEFEPTC DGKADGIYPN GVCVPNFLTC
     SGGIARVMNC PASLIFNPDI LVCDWPRDVA ECHGLSTPAP VCEDDGYFSF GQCSSSFTAC
     TNGRAIVMFC PAGLKFSQAN QRCDYDDLVN ECQEASGEES SGEASGEQSG EGSGEASGEA
     SGEASGENEC VSLDNGLHAI GCSPRVLSCQ NGHVDIFECP SSLVFNEQTL ICDYPQTSLK
     CLIEDTLLID ETPITPFDCS TNGLFSDGLC SATYHQCSAG QLINFTCAET NAVFSAANAE
     CVDSSTLLQC H