ID   CHIC_SOLLC              Reviewed;         322 AA.
AC   Q05538; P80800;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-JUN-2009, entry version 86.
DE   RecName: Full=Basic 30 kDa endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHI9;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum; Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Moneymaker;
RX   MEDLINE=94003061; PubMed=8400122; DOI=10.1007/BF00028974;
RA   Danhash N., Wagemakers C.A.M., van Kan J.A.L., de Wit P.J.G.M.;
RT   "Molecular characterization of four chitinase cDNAs obtained from
RT   Cladosporium fulvum-infected tomato.";
RL   Plant Mol. Biol. 22:1017-1029(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-38, AND SUBCELLULAR LOCATION.
RX   MEDLINE=97332671; PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
RA   Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
RA   Slabas A.R.;
RT   "Differential extraction and protein sequencing reveals major
RT   differences in patterns of primary cell wall proteins from plants.";
RL   J. Biol. Chem. 272:15841-15848(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 97-124; 160-180; 187-223 AND 259-282.
RA   Almagro L., Briceno Z., Pedreno M.A.;
RL   Submitted (JUL-2008) to UniProtKB.
CC   -!- FUNCTION: Defense against chitin containing fungal pathogens.
CC   -!- CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-
CC       glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
CC   -!- SUBCELLULAR LOCATION: Vacuole. Secreted, cell wall. Note=Vacuolar,
CC       protoplast and cell wall.
CC   -!- INDUCTION: By fungal infection.
CC   -!- PTM: The 4-hydroxyproline residues are not glycosylated in this
CC       plant vacuolar protein (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class I subfamily.
CC   -!- SIMILARITY: Contains 1 chitin-binding type-1 domain.
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DR   EMBL; Z15140; CAA78845.1; -; mRNA.
DR   PIR; S37344; S37344.
DR   UniGene; Les.20044; -.
DR   HSSP; P23951; 1CNS.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   BRENDA; 3.2.1.14; 281054.
DR   GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:EC.
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   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR001002; Chitin_bd_1.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   Gene3D; G3DSA:3.30.60.10; Chitin_bd_1; 1.
DR   PANTHER; PTHR22595; Glyco_hydro_19_cat; 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   ProDom; PD000609; Chitin_binding_1; 1.
DR   ProDom; PD354900; Glyco_hydro_19; 1.
DR   SMART; SM00270; ChtBD1; 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; Cell wall; Chitin degradation;
KW   Chitin-binding; Direct protein sequencing; Disulfide bond;
KW   Glycosidase; Hydrolase; Hydroxylation; Plant defense;
KW   Polysaccharide degradation; Secreted; Signal; Vacuole.
FT   SIGNAL        1     22
FT   CHAIN        23    315       Basic 30 kDa endochitinase.
FT                                /FTId=PRO_0000005301.
FT   PROPEP      316    322       Removed in mature form.
FT                                /FTId=PRO_0000005302.
FT   DOMAIN       23     64       Chitin-binding type-1.
FT   MOD_RES      66     66       4-hydroxyproline (By similarity).
FT   MOD_RES      68     68       4-hydroxyproline (By similarity).
FT   DISULFID     25     40       By similarity.
FT   DISULFID     34     46       By similarity.
FT   DISULFID     39     53       By similarity.
FT   DISULFID     58     62       By similarity.
FT   DISULFID     93    156       By similarity.
FT   DISULFID    168    176       By similarity.
FT   DISULFID    275    307       By similarity.
FT   CONFLICT     34     34       C -> R (in Ref. 2; AA sequence).
FT   CONFLICT     36     36       Missing (in Ref. 2; AA sequence).
FT   CONFLICT    106    106       V -> I (in Ref. 3; AA sequence).
FT   CONFLICT    107    107       T -> N (in Ref. 3; AA sequence).
FT   CONFLICT    107    107       T -> S (in Ref. 3; AA sequence).
SQ   SEQUENCE   322 AA;  34345 MW;  D13A9191AEE8FC5A CRC64;
     MRLSEFTTLF LLFSVLLLSA SAEQCGSQAG GALCASGLCC SKFGWCGNTN EYCGPGNCQS
     QCPGGPGPSG DLGGVISNSM FDQMLNHRND NACQGKNNFY SYNAFVTAAG SFPGFGTTGD
     ITARKREIAA FLAQTSHETT GGWPTAPDGP YAWGYCFLRE QGSPGDYCTP SSQWPCAPGR
     KYFGRGPIQI SHNYNYGPCG RAIGVDLLNN PDLVATDPVI SFKSAIWFWM TPQSPKPSCH
     DVITGRWQPS GADQAANRVP GFGVITNIIN GGLECGHGSD SRVQDRIGFY RRYCGILGVS
     PGENLDCGNQ RSFGNGLLVD IM
//