[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=7517787 [NCBI, ExPASy, EBI, Israel, Japan] Ishige F., Mori H., Yamazaki K., Imaseki H.; "Cloning of a complementary DNA that encodes an acidic chitinase which is induced by ethylene and expression of the corresponding gene."; Plant Cell Physiol. 34:103-111(1993).

Comments

FUNCTION: This protein functions as a 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: Secreted, extracellular space.
INDUCTION: By ethylene.
SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D11335; BAA01948.1; ALT_INIT; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S36932; S36932.

3D structure databases

HSSP

P23472; 2HVM. [HSSP ENTRY / PDB]

ModBase

P29024.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0043169;	Molecular function: cation binding (inferred from electronic annotation from InterPro).
GO:0004568;	Molecular function: chitinase activity (inferred from electronic annotation from EC).
GO:0006032;	Biological process: chitin catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001223; Glyco_hydro18cat.
IPR001579; Glyco_hydro_18_chit_AS.
IPR013781; Glyco_hydro_sub_cat.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.80; Glyco_hydro_cat; 1.

Pfam

PF00704; Glyco_hydro_18; 1.
Pfam graphical view of domain structure.

PROSITE

PS01095; CHITINASE_18; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Carbohydrate metabolism; Chitin degradation; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 29`	`29`	`Potential.`
`CHAIN`	`30 298`	`269`	`Acidic endochitinase.`	`PRO_0000011917`
`ACT_SITE`	`156 156`		`Proton donor (By similarity).`
`DISULFID`	`49 96`		`By similarity.`
`DISULFID`	`79 86`		`By similarity.`
`DISULFID`	`185 214`		`By similarity.`

Sequence information

Length: 298 AA [This is the length of the unprocessed precursor]

Molecular weight: 31702 Da [This is the MW of the unprocessed precursor]

CRC64: 3B382DE1C07656A9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKPNMACLKQ VSALLLPLLF ISFFKPSHAG GISVYWGQNG NEGSLADACN TGNYKYVNIA 

        70         80         90        100        110        120 
FLFTFGGGQT PQLNLAGHCN PSINNCNVFS DQIKECQSKD IKVLLSLGGA SGSYSLTSAD 

       130        140        150        160        170        180 
DATQVANYIW NNFLGGQSSS RPLGDAILDG VDFDIESGTG EHWDDLARAL KGFNSQLLLT 

       190        200        210        220        230        240 
AAPQCPIPDA HLDTAIKTGL FDIVWVQFYN NPPCQYSSGN TNDLISSWNQ WTSSQAKQLF 

       250        260        270        280        290 
LGVPASTAAA GSGFIPADVL TSQVLPTIKG SSKYGGVMLW DRFNDGQSGY SGAIIGSV

P29024 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools