[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cv. Alcan; DOI=10.1007/BF00042042; PubMed=7787175 [NCBI, ExPASy, EBI, Israel, Japan] Chang M.M., Horovitz D., Culley D., Hadwiger L.A.; "Molecular cloning and characterization of a pea chitinase gene expressed in response to wounding, fungal infection and the elicitor chitosan."; Plant Mol. Biol. 28:105-111(1995).
[2]	PROTEIN SEQUENCE OF 21-36. STRAIN=cv. Birte; TISSUE=Leaf; Vad K., Mikkelsen J.D., Collinge D.B.; "Induction, purification and characterization of chitinase isolated from pea leaves inoculated with Ascochyta pisi."; Planta 184:24-29(1991).

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.
INDUCTION: By infection with the fungal pathogen Ascochyta pisi.
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

L37876; AAA75196.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S56694; S56694.

3D structure databases

HSSP

P02877; 1HEV. [HSSP ENTRY / PDB]

SMR

P21226; 21-307.

ModBase

P21226.

Ontologies

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).

ProtoNet

P21226.

Other

UniRef

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

Keywords

Carbohydrate metabolism; Chitin degradation; Chitin-binding; Direct protein sequencing; Glycosidase; Hydrolase; Plant defense; Polysaccharide degradation; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`
`CHAIN`	`21 309`	`289`	`Endochitinase A2.`	`PRO_0000005308`
`PROPEP`	`310 324`	`15`	`Removed in mature form (By similarity).`	`PRO_0000005309`
`DOMAIN`	`21 61`	`41`	`Chitin-binding type-1.`
`DISULFID`	`23 38`		`By similarity.`
`DISULFID`	`32 44`		`By similarity.`
`DISULFID`	`37 51`		`By similarity.`
`DISULFID`	`55 59`		`By similarity.`
`DISULFID`	`151 170`		`By similarity.`
`DISULFID`	`269 301`		`By similarity.`

Sequence information

Length: 324 AA [This is the length of the unprocessed precursor]

Molecular weight: 34678 Da [This is the MW of the unprocessed precursor]

CRC64: 540F0DA5EC1DC2FA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKLRIPILL VLFIVSCCSA EQCGTQAGGA LCPGGLCCSK FGWCGSTSEY CGDGCQSQCS 

        70         80         90        100        110        120 
GSSGGGTLSS LISGDTFNNM LKHRNDNACQ GKPFYTYDAF LSAAKAFPNF ANKGDTATKK 

       130        140        150        160        170        180 
REIAAFLGQT SHETTGGWPT APDGPYAWGY CFLREQNPST YCQASSEFPC ASGKQYYGRG 

       190        200        210        220        230        240 
PIQISWNYNY GQCGRAIGVD LLNNPDLVAT DPVISFKTAL WFWMTPQSPK PSCHDVITGG 

       250        260        270        280        290        300 
WTPSSADRAA GRLPGYGTVT NIINGGLECG RGQDSRVQDR IGFYKRYCDI FGIGYGDNLD 

       310        320 
CYSQRPFGSS LPLSSILLDT VAAA

P21226 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