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 27-MAR-2024, entry version 65.
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.A8XWX5; -.
DR GlyCosmos; A8XWX5; 3 sites, No reported glycans.
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; NETAQVC; -.
DR OrthoDB; 3210195at2759; -.
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 Gene3D; 2.170.140.10; Chitin binding domain; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR PANTHER; PTHR23301; CHITIN BINDING PERITROPHIN-A; 1.
DR PANTHER; PTHR23301:SF0; LP10853P; 1.
DR Pfam; PF01607; CBM_14; 6.
DR SMART; SM00494; ChtBD2; 6.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 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
//
