Reviewed, UniProtKB/Swiss-Prot Q05538 (CHIC_SOLLC)

Names and origin

Protein names

Recommended name:
    Basic 30 kDa endochitinase
    EC=3.2.1.14

Gene names

Name:

CHI9

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Defense against chitin containing fungal pathogens.
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Subcellular location	Vacuole. Secreted › cell wall. Note: Vacuolar, protoplast and cell wall. Ref.2
Induction	By fungal infection.
Post-translational modification	The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily. Contains 1 chitin-binding type-1 domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Plant defense Polysaccharide degradation
Cellular component	Cell wall Secreted Vacuole
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Hydroxylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW defense response Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Ref.2
	Chain	23 – 315	293	Basic 30 kDa endochitinase		PRO_0000005301
	Propeptide	316 – 322	7	Removed in mature form		PRO_0000005302
Regions
	Domain	23 – 64	42	Chitin-binding type-1
Amino acid modifications
	Modified residue	66	1	4-hydroxyproline By similarity
	Modified residue	68	1	4-hydroxyproline By similarity
	Disulfide bond	25 ↔ 40		By similarity
	Disulfide bond	34 ↔ 46		By similarity
	Disulfide bond	39 ↔ 53		By similarity
	Disulfide bond	58 ↔ 62		By similarity
	Disulfide bond	93 ↔ 156		By similarity
	Disulfide bond	168 ↔ 176		By similarity
	Disulfide bond	275 ↔ 307		By similarity
Experimental info
	Sequence conflict	34	1	C → R AA sequence Ref.2
	Sequence conflict	36	1	Missing AA sequence Ref.2
	Sequence conflict	106	1	V → I AA sequence Ref.3
	Sequence conflict	107	1	T → N AA sequence Ref.3
	Sequence conflict	107	1	T → S AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q05538-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: D13A9191AEE8FC5A	FASTA	322	34,345
	10 20 30 40 50 60 MRLSEFTTLF LLFSVLLLSA SAEQCGSQAG GALCASGLCC SKFGWCGNTN EYCGPGNCQS 70 80 90 100 110 120 QCPGGPGPSG DLGGVISNSM FDQMLNHRND NACQGKNNFY SYNAFVTAAG SFPGFGTTGD 130 140 150 160 170 180 ITARKREIAA FLAQTSHETT GGWPTAPDGP YAWGYCFLRE QGSPGDYCTP SSQWPCAPGR 190 200 210 220 230 240 KYFGRGPIQI SHNYNYGPCG RAIGVDLLNN PDLVATDPVI SFKSAIWFWM TPQSPKPSCH 250 260 270 280 290 300 DVITGRWQPS GADQAANRVP GFGVITNIIN GGLECGHGSD SRVQDRIGFY RRYCGILGVS 310 320 PGENLDCGNQ RSFGNGLLVD IM

References

[1]	"Molecular characterization of four chitinase cDNAs obtained from Cladosporium fulvum-infected tomato." Danhash N., Wagemakers C.A.M., van Kan J.A.L., de Wit P.J.G.M. Plant Mol. Biol. 22:1017-1029(1993) [PubMed: 8400122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: cv. Moneymaker.
[2]	"Differential extraction and protein sequencing reveals major differences in patterns of primary cell wall proteins from plants." Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P., Slabas A.R. J. Biol. Chem. 272:15841-15848(1997) [PubMed: 9188482] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-38, SUBCELLULAR LOCATION.
[3]	Almagro L., Briceno Z., Pedreno M.A. Submitted (JUL-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 97-124; 160-180; 187-223 AND 259-282.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z15140 mRNA. Translation: CAA78845.1.
PIR	S37344.
UniGene	Les.20044
3D structure databases
HSSP	HSSP built from PDB template 1CNS based on UniProtKB P23951.
ModBase	Search...
Protein family/group databases
CAZy	CBM18. Carbohydrate-Binding Module Family 18. GH19. Glycoside Hydrolase Family 19.
Enzyme and pathway databases
BRENDA	3.2.1.14. 281054.
Family and domain databases
InterPro	IPR018371. Chitin-binding_1_CS. IPR001002. Chitin_bd_1. IPR016283. Glyco_hydro_19. IPR000726. Glyco_hydro_19_cat. [Graphical view]
Gene3D	G3DSA:3.30.60.10. Chitin_bd_1. 1 hit.
PANTHER	PTHR22595. Glyco_hydro_19_cat. 1 hit.
Pfam	PF00187. Chitin_bind_1. 1 hit. PF00182. Glyco_hydro_19. 1 hit. [Graphical view]
PIRSF	PIRSF001060. Endochitinase. 1 hit.
PRINTS	PR00451. CHITINBINDNG.
ProDom	PD000609. Chitin_binding_1. 1 hit. PD354900. Glyco_hydro_19. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00270. ChtBD1. 1 hit. [Graphical view]
PROSITE	PS00026. CHIT_BIND_I_1. 1 hit. PS50941. CHIT_BIND_I_2. 1 hit. PS00773. CHITINASE_19_1. 1 hit. PS00774. CHITINASE_19_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHIC_SOLLC

Accession

Primary (citable) accession number: Q05538
Secondary accession number(s): P80800

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)