CHI1_TOBAC
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 03-AUG-2022, entry version 136.
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=10.2307/3869130;
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 CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PRIDE; P08252; -.
DR ProMEX; P08252; -.
DR GeneID; 107759005; -.
DR KEGG; nta:107759005; -.
DR OMA; CEPSATW; -.
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:0050832; P:defense response to fungus; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.10; -; 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 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; SSF53955; 1.
DR SUPFAM; SSF57016; SSF57016; 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
