CHIT_MANSE
ID CHIT_MANSE Reviewed; 554 AA.
AC P36362;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Endochitinase;
DE EC=3.2.1.14;
DE Flags: Precursor;
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8353525; DOI=10.1016/0965-1748(93)90043-r;
RA Kramer K.J., Corpuz L., Choi H.K., Muthukrishnan S.;
RT "Sequence of a cDNA and expression of the gene encoding epidermal and gut
RT chitinases of Manduca sexta.";
RL Insect Biochem. Mol. Biol. 23:691-701(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9061927; DOI=10.1016/s0965-1748(96)00066-5;
RA Choi H.K., Choi K.H., Kramer K.J., Muthukrishnan S.;
RT "Isolation and characterization of a genomic clone for the gene of an
RT insect molting enzyme, chitinase.";
RL Insect Biochem. Mol. Biol. 27:37-47(1997).
CC -!- FUNCTION: Digests chitin in the exoskeleton during the molting process.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Epidermis and gut.
CC -!- DEVELOPMENTAL STAGE: High levels seen in the epidermis on day 0, but
CC rapidly disappears and is undetected on days 1-4 of fifth instar. It
CC reappears on day 5 and peaks on day 7 after which a rapid decline is
CC seen. In the gut is detected on day 6 with lower levels seen on days 0,
CC 7 and 8.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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; U02270; AAC04924.1; -; mRNA.
DR EMBL; L49234; AAB53952.1; -; Genomic_DNA.
DR PIR; A56596; A56596.
DR AlphaFoldDB; P36362; -.
DR SMR; P36362; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PRIDE; P36362; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01607; CBM_14; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR SUPFAM; SSF57625; SSF57625; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..554
FT /note="Endochitinase"
FT /id="PRO_0000011949"
FT DOMAIN 23..398
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 495..553
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT REGION 398..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 76..77
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 103..106
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 147
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 213..216
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 370
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 527..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ SEQUENCE 554 AA; 62204 MW; 3989D756C96CD490 CRC64;
MRATLATLAV LALATAVQSD SRARIVCYFS NWAVYRPGVG RYGIEDIPVE KCTHIIYSFI
GVTEGNSEVL IIDPELDVDK NGFRNFTSLR SSHPSVKFMV AVGGWAEGSS KYSHMVAQKS
TRMSFIRSVV SFLKKYDFDG LDLDWEYPGA ADRGGSFSDK DKFLYLVQEL RRAFIRVGKG
WELTAAVPLA NFRLMEGYHV PELCQELDAI HVMSYDLRGN WAGFADVHSP LYKRPHDQWA
YEKLNVNDGL HLWEEKGCPS NKLVVGIPFY GRSFTLSAGN NNYGLGTFIN KEAGGGDPAP
YTNATGFWAY YEICTEVDKD DSGWTKKWDE QGKCPYAYKG TQWVGYEDPR SVEIKMNWIK
QKGYLGAMTW AIDMDDFQGL CGEKNPLIKI LHKHMSSYTV PPPHTENTTP TPEWARPPST
PSDPSEGDPI PTTTTAKPAS TTKTTVKTTT TTTAKPPQSV IDEENDINVR PEPKPEPQPE
PEVEVPPTEN EVDGSEICNS DQDYIPDKKH CDKYWRCVNG EAMQFSCQHG TVFNVELNVC
DWPSNATRRE CQQP
