[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. STRAIN=cv. Havana 425; TISSUE=Leaf; DOI=10.1007/BF00028772; PubMed=1966383 [NCBI, ExPASy, EBI, Israel, Japan] Shinshi H., Neuhaus J.-M., Ryals J., Meins F. Jr.; "Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain."; Plant Mol. Biol. 14:357-368(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. STRAIN=cv. Samsun; TISSUE=Flower bud; DOI=10.1105/tpc.2.7.673; PubMed=2152343 [NCBI, ExPASy, EBI, Israel, Japan] Neale A.D., Wahleithner J.A., Lund M., Bonnett H.T., Kelly A., Meeks-Wagner D.R., Peacock W.J., Dennis E.S.; "Chitinase, beta-1,3-glucanase, osmotin, and extensin are expressed in tobacco explants during flower formation."; Plant Cell 2:673-684(1990).
[3]	SUBCELLULAR LOCATION. PubMed=1946457 [NCBI, ExPASy, EBI, Israel, Japan] Neuhaus J.-M., Sticher L., Meins F. Jr., Boller T.; "A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole."; Proc. Natl. Acad. Sci. U.S.A. 88:10362-10366(1991).
[4]	HYDROXYLATION AT PRO-67; PRO-69; PRO-71; PRO-72; PRO-74 AND PRO-75, AND MASS SPECTROMETRY. PubMed=1496378 [NCBI, ExPASy, EBI, Israel, Japan] Sticher L., Hofsteenge J., Milani A., Neuhaus J.-M., Meins F. Jr.; "Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins."; Science 257:655-657(1992).

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. Note=Vacuolar and protoplast.
DEVELOPMENTAL STAGE: Expressed during flower formation.
INDUCTION: By ethylene.
PTM: The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein.
SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily [view classification].
SIMILARITY: Contains 1 chitin-binding type-1 domain.

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

X16938; CAA34812.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X16939; CAA34813.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S44869; AAB23374.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S08627; S08627.

3D structure databases

HSSP

P23951; 2BAA. [HSSP ENTRY / PDB]

SMR

P08252; 24-320.

ModBase

P08252.

Ontologies

GO:0005773;	Cellular component: vacuole (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001002; Chitin_bd_1.
IPR016283; Glyco_hydro_19.
IPR000726; Glyco_hydro_19_cat.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.60.10; Chitin_bd_1; 1.

PANTHER

PTHR22595; Glyco_hydro_19_cat; 1.

Pfam

PF00187; Chitin_bind_1; 1.
PF00182; Glyco_hydro_19; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001060; Endochitinase; 1.

PRINTS

PR00451; CHITINBINDNG.

ProDom

PD000609; Chitin_binding_1; 1.
PD354900; Glyco_hydro_19; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00270; ChtBD1; 1.
SMART graphical view of domain structure.

PROSITE

PS00026; CHIT_BIND_I_1; 1.
PS50941; CHIT_BIND_I_2; 1.
PS00773; CHITINASE_19_1; 1.
PS00774; CHITINASE_19_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Carbohydrate metabolism; Chitin degradation; Chitin-binding; Glycosidase; Hydrolase; Hydroxylation; Polysaccharide degradation; Signal; Vacuole.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 322`	`299`	`Endochitinase A.`	`PRO_0000005330`
`PROPEP`	`323 329`	`7`	`Removed in mature form.`	`PRO_0000005331`
`DOMAIN`	`24 65`	`42`	`Chitin-binding type-1.`
`MOD_RES`	`67 67`		`4-hydroxyproline; partial.`
`MOD_RES`	`69 69`		`4-hydroxyproline.`
`MOD_RES`	`71 71`		`4-hydroxyproline.`
`MOD_RES`	`72 72`		`4-hydroxyproline.`
`MOD_RES`	`74 74`		`4-hydroxyproline.`
`MOD_RES`	`75 75`		`4-hydroxyproline; partial.`
`DISULFID`	`26 41`		`By similarity.`
`DISULFID`	`35 47`		`By similarity.`
`DISULFID`	`40 54`		`By similarity.`
`DISULFID`	`59 63`		`By similarity.`
`DISULFID`	`101 163`		`By similarity.`
`DISULFID`	`175 183`		`By similarity.`
`DISULFID`	`282 314`		`By similarity.`
`CONFLICT`	`73 78`		`TPPGGG -> HPTRC (in Ref. 2; AAB23374).`
`CONFLICT`	`263 263`		`A -> S (in Ref. 2; AAB23374).`

Sequence information

Length: 329 AA [This is the length of the unprocessed precursor]

Molecular weight: 35156 Da [This is the MW of the unprocessed precursor]

CRC64: 3EC99D96E6C0114C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRLCKFTALS SLLFSLLLLS ASAEQCGSQA GGARCPSGLC CSKFGWCGNT NDYCGPGNCQ 

        70         80         90        100        110        120 
SQCPGGPTPT PPTPPGGGDL GSIISSSMFD QMLKHRNDNA CQGKGFYSYN AFINAARSFP 

       130        140        150        160        170        180 
GFGTSGDTTA RKREIAAFFA QTSHETTGGW ATAPDGPYAW GYCWLREQGS PGDYCTPSGQ 

       190        200        210        220        230        240 
WPCAPGRKYF GRGPIQISHN YNYGPCGRAI GVDLLNNPDL VATDPVISFK SALWFWMTPQ 

       250        260        270        280        290        300 
SPKPSCHDVI IGRWQPSAGD RAANRLPGFG VITNIINGGL ECGRGTDSRV QDRIGFYRRY 

       310        320 
CSILGVSPGD NLDCGNQRSF GNGLLVDTM

P08252 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