CHIC_SOLLC
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 03-AUG-2022, entry version 148.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Moneymaker;
RX 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 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 differences
RT 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:
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:9188482}. Secreted,
CC cell wall {ECO:0000269|PubMed:9188482}. Note=Vacuolar, protoplast and
CC cell wall.
CC -!- INDUCTION: By fungal infection.
CC -!- PTM: The 4-hydroxyproline residues are not glycosylated in this plant
CC vacuolar protein. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC class I subfamily. {ECO:0000305}.
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DR EMBL; Z15140; CAA78845.1; -; mRNA.
DR PIR; S37344; S37344.
DR RefSeq; NP_001234403.1; NM_001247474.2.
DR AlphaFoldDB; Q05538; -.
DR SMR; Q05538; -.
DR STRING; 4081.Solyc10g055810.1.1; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR PaxDb; Q05538; -.
DR PRIDE; Q05538; -.
DR EnsemblPlants; Solyc10g055810.2.1; Solyc10g055810.2.1; Solyc10g055810.2.
DR GeneID; 544148; -.
DR Gramene; Solyc10g055810.2.1; Solyc10g055810.2.1; Solyc10g055810.2.
DR KEGG; sly:544148; -.
DR eggNOG; KOG4742; Eukaryota.
DR HOGENOM; CLU_045506_1_0_1; -.
DR InParanoid; Q05538; -.
DR OMA; GNFYSYN; -.
DR OrthoDB; 1132954at2759; -.
DR PhylomeDB; Q05538; -.
DR Proteomes; UP000004994; Chromosome 10.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; Cell wall; Chitin degradation; Chitin-binding;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Hydroxylation; Plant defense; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal; Vacuole.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:9188482"
FT CHAIN 23..315
FT /note="Basic 30 kDa endochitinase"
FT /id="PRO_0000005301"
FT PROPEP 316..322
FT /note="Removed in mature form"
FT /id="PRO_0000005302"
FT DOMAIN 23..64
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P29022"
FT MOD_RES 66
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 68
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 25..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 34..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 39..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 58..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 93..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 168..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DISULFID 275..307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT CONFLICT 34
FT /note="C -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="V -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="T -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="T -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
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
