NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Havana 425;
TISSUE=Leaf;
DOI=10.1007/BF00266251; PubMed=1588915 [NCBI, ExPASy, EBI, Israel, Japan]
van Buuren M., Neuhaus J.-M., Shinshi H., Ryals J., Meins F. Jr.;
"The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin.";
Mol. Gen. Genet. 232:460-469(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 (Probable). Note=Vacuolar and protoplast (Probable).
PTM: The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein (By similarity).
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

X64518; CAA45821.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S20982; S20982.

3D structure databases

HSSP

P27275; 1MMC. [HSSP ENTRY / PDB]

ModBase

P29059.

Ontologies

GO:0005773;	Cellular component: vacuole (inferred from electronic annotation from UniProtKB-KW).
GO:0008061;	Molecular function: chitin binding (inferred from electronic annotation from InterPro).
GO:0004568;	Molecular function: chitinase activity (inferred from electronic annotation from InterPro).
GO:0016998;	Biological process: cell wall catabolic process (inferred from electronic annotation from InterPro).
GO:0006032;	Biological process: chitin catabolic process (inferred from electronic annotation from InterPro).
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; Plant defense; Polysaccharide degradation; Signal; Vacuole.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 327`	`304`	`Endochitinase 3.`	`PRO_0000005334`
`PROPEP`	`328 334`	`7`	`Removed in mature form (Probable).`	`PRO_0000005335`
`DOMAIN`	`24 65`	`42`	`Chitin-binding type-1.`
`MOD_RES`	`73 73`		`4-hydroxyproline (By similarity).`
`MOD_RES`	`74 74`		`4-hydroxyproline (By similarity).`
`MOD_RES`	`76 76`		`4-hydroxyproline (By similarity).`
`DISULFID`	`26 41`		`By similarity.`
`DISULFID`	`35 47`		`By similarity.`
`DISULFID`	`40 54`		`By similarity.`
`DISULFID`	`59 63`		`By similarity.`
`DISULFID`	`106 168`		`By similarity.`
`DISULFID`	`180 188`		`By similarity.`
`DISULFID`	`287 319`		`By similarity.`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 36221 Da [This is the MW of the unprocessed precursor]

CRC64: 4F684CE1FBD432FB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRLLEFTALS SLLVLFLLLA VSAEQCGKQA GGARCPSGMC CSNFGWCGNT QDYCGPGKCQ 

        70         80         90        100        110        120 
SQCPSGPGPT PRPPTPTPGP STGDISNIIS SSMFDQMLKH RNDNTCQGKS FYTYNAFITA 

       130        140        150        160        170        180 
ARSFRGFGTT GDTTRRKREV AAFFAQTSHE TTGGWDTAPD GRYAWGYCYL REQGNPPSYC 

       190        200        210        220        230        240 
VQSSQWPCAP GQKYYGRGPI QISYNYNYGP CGRAIGQNLL NNPDLVATNA VVSFKSAIWF 

       250        260        270        280        290        300 
WMTAQSPKPS CHDVITGRWT PSAADRAANR LPGYGVITNI INGGLECGHG SDARVQDRIG 

       310        320        330 
FYRRYCSILG VSPGDNIDCG NQKSFNSGLL LETM

P29059 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