CBD1_CAEEL
ID CBD1_CAEEL Reviewed; 1319 AA.
AC O45599;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Chitin-binding domain protein cbd-1 {ECO:0000312|WormBase:H02I12.1};
DE Flags: Precursor;
GN Name=cbd-1 {ECO:0000312|WormBase:H02I12.1};
GN ORFNames=H02I12.1 {ECO:0000312|WormBase:H02I12.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20971008; DOI=10.1016/j.cub.2010.09.059;
RA Johnston W.L., Krizus A., Dennis J.W.;
RT "Eggshell chitin and chitin-interacting proteins prevent polyspermy in C.
RT elegans.";
RL Curr. Biol. 20:1932-1937(2010).
CC -!- FUNCTION: In unfertilized oocytes, maintains egg-1 and egg-2 at the
CC plasma membrane together with chitin synthase chs-1 and kinase mbk-2.
CC Essential for the formation of a continuous and cohesive chitin layer
CC following fertilization. {ECO:0000269|PubMed:20971008}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:20971008}. Note=Localizes around oocytes in
CC the proximal region of the germline. {ECO:0000269|PubMed:20971008}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes the zygote to exit
CC the spermatheca with a pinched morphology and to leave a trailing
CC section behind. Zygotes have a fragmented chitin eggshell with an
CC accumulation of chitin at one end of the embryo, causing polyspermy. In
CC unfertilized oocytes, disrupts the homogenous distribution of cortical
CC chitin synthase chs-1, pseudophosphatase egg-3 and kinase mbk-2 and
CC causes the loss of egg-1 and egg-2 cell membrane localization resulting
CC in their premature accumulation in cytoplasmic puncta.
CC {ECO:0000269|PubMed:20971008}.
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DR EMBL; BX284604; CAB07215.2; -; Genomic_DNA.
DR PIR; T23024; T23024.
DR RefSeq; NP_502145.2; NM_069744.5.
DR AlphaFoldDB; O45599; -.
DR SMR; O45599; -.
DR DIP; DIP-26633N; -.
DR IntAct; O45599; 4.
DR STRING; 6239.H02I12.1; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR EPD; O45599; -.
DR PaxDb; O45599; -.
DR PeptideAtlas; O45599; -.
DR EnsemblMetazoa; H02I12.1.1; H02I12.1.1; WBGene00010351.
DR GeneID; 178061; -.
DR KEGG; cel:CELE_H02I12.1; -.
DR UCSC; H02I12.1; c. elegans.
DR CTD; 178061; -.
DR WormBase; H02I12.1; CE37527; WBGene00010351; cbd-1.
DR eggNOG; ENOG502SA2C; Eukaryota.
DR GeneTree; ENSGT00940000166041; -.
DR HOGENOM; CLU_261097_0_0_1; -.
DR InParanoid; O45599; -.
DR OMA; WGRKVVM; -.
DR OrthoDB; 1174178at2759; -.
DR PRO; PR:O45599; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00010351; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0071944; C:cell periphery; IDA:WormBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0030703; P:eggshell formation; IMP:UniProtKB.
DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; IMP:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR Pfam; PF01607; CBM_14; 7.
DR SMART; SM00494; ChtBD2; 12.
DR SUPFAM; SSF57625; SSF57625; 8.
DR PROSITE; PS50940; CHIT_BIND_II; 12.
PE 3: Inferred from homology;
KW Chitin-binding; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1319
FT /note="Chitin-binding domain protein cbd-1"
FT /id="PRO_5004158351"
FT DOMAIN 28..83
FT /note="Chitin-binding type-2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 96..141
FT /note="Chitin-binding type-2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 190..236
FT /note="Chitin-binding type-2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 304..357
FT /note="Chitin-binding type-2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 566..614
FT /note="Chitin-binding type-2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 689..745
FT /note="Chitin-binding type-2 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 782..838
FT /note="Chitin-binding type-2 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 883..942
FT /note="Chitin-binding type-2 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 1029..1081
FT /note="Chitin-binding type-2 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 1105..1163
FT /note="Chitin-binding type-2 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 1179..1237
FT /note="Chitin-binding type-2 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DOMAIN 1242..1298
FT /note="Chitin-binding type-2 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT REGION 250..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1016
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 61..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 128..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 222..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 335..348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 601..614
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 721..734
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 814..827
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 916..929
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 1060..1073
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 1139..1152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 1213..1226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 1274..1287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ SEQUENCE 1319 AA; 144194 MW; 2B50C8656061FB3F CRC64;
MGPQLATVSL LLLTFFSNSI QYPHSPAATE CPAYFNGNIA GNACSREYSI CVNGVRQAAT
CSDDSVFYED ECVPVDESPE CRVDENTEED DTPYAEFDCT SKQDGIYSIG CSNQFISCVA
GGAYMAKCPD SLVFNERTQD CRESCDEVKQ DTTTAPQVYE DGEEGYGEAS GEIAGDYERQ
PSNEQPDSID FDCNGLEDGN YADGCNDVFY SCSNNMVFQR YCPPGTVFNI NQQSCDFQCT
TDDPTTTVSY STSTITTPQE DDSEYSSTTS ADVISTTTTP SIDAIETTTT GFDAVTTTTT
TQTPFVCQEG QVNSFGMCSS RFNRCQNNSV RSKQCPVNTL FESSLVMCVF DLPQCQPITV
PAAPAYNSYG PPSDTIVSPF DENVRLKPKF DRRRKYHHGK PSYGPVNGNS YLENPFFIPR
HRGGSHRDHR RYGYGPAIDS PFSTAFRGRA ALSDQFKDYR RARMGKIQGD ARKVDGNKRF
LIDDEFEGPN AKFVESNIEQ VFPKNRHSKK QLGPHEDPDG YDDEKTFDAK DLFGATRRKR
SAYYGTEQSV YGQQSAQISA RQAQVNKDCQ QYTTPTFLTF GDCFDQFIFC SGNGINRMAA
CPIGETFDKT LRSCSETCGV STTIVAVTIG TQTSDDLSAP SEYIENDGVT TQSTWNDQPS
TTQAPNSYES YTTQYSSNDV PSTSAAPIGD RCSLDASGLF SLGCSQKYIQ CSNGAAIVRR
CGESLYFNEA TQECTYRDEV PECGSQGSTS SPVITTPGQD QSSNYYGIPS DDVPSTTQTP
VGDRCAYVAS GLFDLGCSQK YIQCSDSAAS VRECEGSLYF DERSQSCRFR DEVFKCQTAD
VSSSSTVPYL DFTTTPASPS EDEPTTYEPS VAPYIPSVTV NPVDTCTSLS DGTHGTGCSS
FYFVCSHGRL ISSGNCQLGE GYDPSVQGCR TFSEIPARAC DEQEVTTDAG LVQLMPYKTL
EEVLTTTEAA TTVANDGPTD TYITGSTKYS TTDSGEYTIP YGDETTSTRS YDRADNDSED
EEEDDVEHDQ KCTVGSRTPV GFCVRTYLEC TDAGNVEKLC RIGKLFDSHS NRCVPRIGCG
KEAIRDAIKD MIATTPAPAQ PKQFEGRCAH VDGEAVFSIG VCSSKYLRCS YGASKLQQCS
EDRVFSNDKL ECIVRESVSA CTVPKNPSIK KYYTSNDQSA FCDGKEDGLY RNERDCSAIL
QCFGGELFEH PSCQSSLAFN QLTGKCDYPQ KVSGCENHGQ TNGECSEHGS FIADANNCEV
FYRCVWGRKV VMTCPSGTVF NPLLSVCDWP SAVPSCSGQA SDSNSSYGSS TYNDDKSGY
