ID CHI1_TOBAC Reviewed; 329 AA. AC P08252; Q41180; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 2. DT 27-MAR-2024, entry version 142. DE RecName: Full=Endochitinase A; DE Short=CHN-A; DE EC=3.2.1.14; DE Flags: Precursor; GN Name=CHN48; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=cv. Havana 425; TISSUE=Leaf; RX PubMed=1966383; DOI=10.1007/bf00028772; RA Shinshi H., Neuhaus J.-M., Ryals J., Meins F. Jr.; RT "Structure of a tobacco endochitinase gene: evidence that different RT chitinase genes can arise by transposition of sequences encoding a RT cysteine-rich domain."; RL Plant Mol. Biol. 14:357-368(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. RC STRAIN=cv. Samsun; TISSUE=Flower bud; RX PubMed=2152343; DOI=10.1105/tpc.2.7.673; RA Neale A.D., Wahleithner J.A., Lund M., Bonnett H.T., Kelly A., RA Meeks-Wagner D.R., Peacock W.J., Dennis E.S.; RT "Chitinase, beta-1,3-glucanase, osmotin, and extensin are expressed in RT tobacco explants during flower formation."; RL Plant Cell 2:673-684(1990). RN [3] RP SUBCELLULAR LOCATION. RX PubMed=1946457; DOI=10.1073/pnas.88.22.10362; RA Neuhaus J.-M., Sticher L., Meins F. Jr., Boller T.; RT "A short C-terminal sequence is necessary and sufficient for the targeting RT of chitinases to the plant vacuole."; RL Proc. Natl. Acad. Sci. U.S.A. 88:10362-10366(1991). RN [4] RP HYDROXYLATION AT PRO-67; PRO-69; PRO-71; PRO-72; PRO-74 AND PRO-75, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=1496378; DOI=10.1126/science.1496378; RA Sticher L., Hofsteenge J., Milani A., Neuhaus J.-M., Meins F. Jr.; RT "Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing RT proteins."; RL Science 257:655-657(1992). CC -!- FUNCTION: Defense against chitin-containing fungal pathogens. 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: Vacuole {ECO:0000269|PubMed:1946457}. CC Note=Vacuolar and protoplast. CC -!- DEVELOPMENTAL STAGE: Expressed during flower formation. CC {ECO:0000269|PubMed:2152343}. CC -!- INDUCTION: By ethylene. CC -!- PTM: The 4-hydroxyproline residues are not glycosylated in this plant CC vacuolar protein. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase CC class I 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; X16938; CAA34812.1; -; Genomic_DNA. DR EMBL; X16939; CAA34813.1; -; mRNA. DR EMBL; S44869; AAB23374.1; -; mRNA. DR PIR; S08627; S08627. DR RefSeq; NP_001311556.1; NM_001324627.1. DR AlphaFoldDB; P08252; -. DR SMR; P08252; -. DR STRING; 4097.P08252; -. DR CAZy; CBM18; Carbohydrate-Binding Module Family 18. DR CAZy; GH19; Glycoside Hydrolase Family 19. DR PaxDb; 4097-P08252; -. DR ProMEX; P08252; -. DR GeneID; 107759005; -. DR KEGG; nta:107759005; -. DR OMA; CEPSATW; -. DR OrthoDB; 997724at2759; -. DR PhylomeDB; P08252; -. DR Proteomes; UP000084051; Unplaced. DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell. DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW. DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central. DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro. DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW. DR CDD; cd00325; chitinase_GH19; 1. DR CDD; cd06921; ChtBD1_GH19_hevein; 1. DR Gene3D; 1.10.530.10; -; 1. DR Gene3D; 3.30.20.10; Endochitinase, domain 2; 1. DR Gene3D; 3.30.60.10; Endochitinase-like; 1. DR InterPro; IPR001002; Chitin-bd_1. DR InterPro; IPR018371; Chitin-binding_1_CS. DR InterPro; IPR036861; Endochitinase-like_sf. DR InterPro; IPR016283; Glyco_hydro_19. DR InterPro; IPR000726; Glyco_hydro_19_cat. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR PANTHER; PTHR22595:SF79; BASIC ENDOCHITINASE B; 1. DR PANTHER; PTHR22595; CHITINASE-RELATED; 1. DR Pfam; PF00187; Chitin_bind_1; 1. DR Pfam; PF00182; Glyco_hydro_19; 1. DR PIRSF; PIRSF001060; Endochitinase; 1. DR PRINTS; PR00451; CHITINBINDNG. DR SMART; SM00270; ChtBD1; 1. DR SUPFAM; SSF53955; Lysozyme-like; 1. DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1. DR PROSITE; PS00026; CHIT_BIND_I_1; 1. DR PROSITE; PS50941; CHIT_BIND_I_2; 1. DR PROSITE; PS00773; CHITINASE_19_1; 1. DR PROSITE; PS00774; CHITINASE_19_2; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Chitin degradation; Chitin-binding; KW Disulfide bond; Glycosidase; Hydrolase; Hydroxylation; Plant defense; KW Polysaccharide degradation; Reference proteome; Signal; Vacuole. FT SIGNAL 1..23 FT CHAIN 24..322 FT /note="Endochitinase A" FT /id="PRO_0000005330" FT PROPEP 323..329 FT /note="Removed in mature form" FT /id="PRO_0000005331" FT DOMAIN 24..65 FT /note="Chitin-binding type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT ACT_SITE 145 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P29022" FT MOD_RES 67 FT /note="4-hydroxyproline; partial" FT /evidence="ECO:0000269|PubMed:1496378" FT MOD_RES 69 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1496378" FT MOD_RES 71 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1496378" FT MOD_RES 72 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1496378" FT MOD_RES 74 FT /note="4-hydroxyproline" FT /evidence="ECO:0000269|PubMed:1496378" FT MOD_RES 75 FT /note="4-hydroxyproline; partial" FT /evidence="ECO:0000269|PubMed:1496378" FT DISULFID 26..41 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 35..47 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 40..54 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 59..63 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 101..163 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 175..183 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 282..314 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT CONFLICT 73..78 FT /note="TPPGGG -> HPTRC (in Ref. 2; AAB23374)" FT /evidence="ECO:0000305" FT CONFLICT 263 FT /note="A -> S (in Ref. 2; AAB23374)" FT /evidence="ECO:0000305" SQ SEQUENCE 329 AA; 35156 MW; 3EC99D96E6C0114C CRC64; MRLCKFTALS SLLFSLLLLS ASAEQCGSQA GGARCPSGLC CSKFGWCGNT NDYCGPGNCQ SQCPGGPTPT PPTPPGGGDL GSIISSSMFD QMLKHRNDNA CQGKGFYSYN AFINAARSFP GFGTSGDTTA RKREIAAFFA QTSHETTGGW ATAPDGPYAW GYCWLREQGS PGDYCTPSGQ WPCAPGRKYF GRGPIQISHN YNYGPCGRAI GVDLLNNPDL VATDPVISFK SALWFWMTPQ SPKPSCHDVI IGRWQPSAGD RAANRLPGFG VITNIINGGL ECGRGTDSRV QDRIGFYRRY CSILGVSPGD NLDCGNQRSF GNGLLVDTM //