CDA7_BOMMO
ID CDA7_BOMMO Reviewed; 364 AA.
AC H9JW44;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Chitin deacetylase 7 {ECO:0000303|PubMed:24473143};
DE Short=BmCDA7 {ECO:0000303|PubMed:24473143};
DE EC=3.5.1.41 {ECO:0000269|PubMed:24473143};
DE Flags: Precursor;
GN Name=CDA7 {ECO:0000303|PubMed:24473143};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000312|Proteomes:UP000005204};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=24473143; DOI=10.3390/ijms15021946;
RA Zhong X.W., Wang X.H., Tan X., Xia Q.Y., Xiang Z.H., Zhao P.;
RT "Identification and molecular characterization of a chitin deacetylase from
RT Bombyx mori peritrophic membrane.";
RL Int. J. Mol. Sci. 15:1946-1961(2014).
RN [2] {ECO:0000312|Proteomes:UP000005204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000312|Proteomes:UP000005204};
RX PubMed=15591204; DOI=10.1126/science.1102210;
RA Xia Q., Zhou Z., Lu C., Cheng D., Dai F., Li B., Zhao P., Zha X., Cheng T.,
RA Chai C., Pan G., Xu J., Liu C., Lin Y., Qian J., Hou Y., Wu Z., Li G.,
RA Pan M., Li C., Shen Y., Lan X., Yuan L., Li T., Xu H., Yang G., Wan Y.,
RA Zhu Y., Yu M., Shen W., Wu D., Xiang Z., Yu J., Wang J., Li R., Shi J.,
RA Li H., Li G., Su J., Wang X., Li G., Zhang Z., Wu Q., Li J., Zhang Q.,
RA Wei N., Xu J., Sun H., Dong L., Liu D., Zhao S., Zhao X., Meng Q., Lan F.,
RA Huang X., Li Y., Fang L., Li C., Li D., Sun Y., Zhang Z., Yang Z.,
RA Huang Y., Xi Y., Qi Q., He D., Huang H., Zhang X., Wang Z., Li W., Cao Y.,
RA Yu Y., Yu H., Li J., Ye J., Chen H., Zhou Y., Liu B., Wang J., Ye J.,
RA Ji H., Li S., Ni P., Zhang J., Zhang Y., Zheng H., Mao B., Wang W., Ye C.,
RA Li S., Wang J., Wong G.K.-S., Yang H.;
RT "A draft sequence for the genome of the domesticated silkworm (Bombyx
RT mori).";
RL Science 306:1937-1940(2004).
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=30987273; DOI=10.3390/ijms20071679;
RA Zhang Z., Yan J., Liu Q., Zhang Y., Gong J., Hou Y.;
RT "Genome-Wide Analysis and Hormone Regulation of Chitin Deacetylases in
RT Silkworm.";
RL Int. J. Mol. Sci. 20:0-0(2019).
CC -!- FUNCTION: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine
CC residues in chitin. {ECO:0000269|PubMed:24473143}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate +
CC chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-
CC COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57704; EC=3.5.1.41;
CC Evidence={ECO:0000269|PubMed:24473143};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:H9JW43};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24473143}.
CC -!- TISSUE SPECIFICITY: Expressed in midgut where it is found in the
CC peritrophic membrane, a semi-permeable acellular matrix which lines the
CC digestive tract (at protein level) (PubMed:24473143, PubMed:30987273).
CC Not detected in foregut or hindgut (at protein level)
CC (PubMed:24473143). {ECO:0000269|PubMed:24473143,
CC ECO:0000269|PubMed:30987273}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in newly emerged larvae at
CC second, third, fourth and fifth instar stages (PubMed:24473143,
CC PubMed:30987273). Has lower expression during the molting phases of
CC larval development (PubMed:24473143, PubMed:30987273). No expression
CC detected during pupal stages (PubMed:24473143, PubMed:30987273).
CC {ECO:0000269|PubMed:24473143, ECO:0000269|PubMed:30987273}.
CC -!- INDUCTION: Up-regulated in response to 20-hydroxyecdysone (20E) and
CC juvenile hormone analog. {ECO:0000269|PubMed:30987273}.
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 4 (CE4) family.
CC {ECO:0000305}.
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DR EMBL; BABH01025382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H9JW44; -.
DR SMR; H9JW44; -.
DR EnsemblMetazoa; BGIBMGA013757-RA; BGIBMGA013757-TA; BGIBMGA013757.
DR eggNOG; ENOG502R90A; Eukaryota.
DR HOGENOM; CLU_022576_0_0_1; -.
DR InParanoid; H9JW44; -.
DR OMA; WERIMSS; -.
DR BRENDA; 3.5.1.41; 890.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004099; F:chitin deacetylase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IDA:UniProtKB.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..364
FT /note="Chitin deacetylase 7"
FT /evidence="ECO:0000255"
FT /id="PRO_5012700486"
FT DOMAIN 52..292
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:H9JW43"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:H9JW43"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:H9JW43"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 24..36
FT /evidence="ECO:0000250|UniProtKB:H9J9M0"
FT DISULFID 29..34
FT /evidence="ECO:0000250|UniProtKB:H9J9M0"
FT DISULFID 83..317
FT /evidence="ECO:0000250|UniProtKB:H9J9M0"
FT DISULFID 208..213
FT /evidence="ECO:0000250|UniProtKB:H9J9M0"
FT DISULFID 237..243
FT /evidence="ECO:0000250|UniProtKB:H9J9M0"
FT DISULFID 325..347
FT /evidence="ECO:0000250|UniProtKB:H9J9M0"
FT DISULFID 330..350
FT /evidence="ECO:0000250|UniProtKB:H9J9M0"
SQ SEQUENCE 364 AA; 41184 MW; 4B2248B0B4EABB5C CRC64;
MKLVFYAALL TAVLAKELQL ATECDPEACK LPDCRCSSTS IPGGLEPRNT PQFVTLTFDD
GVNVINVETY REVLYNRVNS NNCPVRATFY VSHEYTNYQL VNELYNRGHE IALHSISHRT
PPSFWAAATY DEIKEEIADQ KVQIAHFANI PFEEVKGVRL PFLQMNGNTS FQVMSDFGLT
YDCTWPASAQ TQRGLWPYTL DYASTQDCTI PPCPTASLPG SWVVPMIAWT DPNGFPCVMV
DACTSFPDRE DPDAWFRFIV TNFERHYLAN RAPFGFFVHE WYISAYPAVK TALVSSSDVV
EWVRNPIPIA EYRSRSCKTF RQTACPASSC GPLVAEHNQL SYWLQLCNRC PAKYPWVGNP
FGLN
