[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=cv. Piggy; PubMed=1899089 [NCBI, ExPASy, EBI, Israel, Japan] Leah R., Tommerup H., Svendsen I., Mundy J.; "Biochemical and molecular characterization of three barley seed proteins with antifungal properties."; J. Biol. Chem. 266:1564-1573(1991).
[2]	PRELIMINARY PROTEIN SEQUENCE OF 24-77 AND 148-188. TISSUE=Endosperm; Leah R., Mikkelsen J.D., Mundy J., Svendsen I.; "Identification of a 28,000 dalton endochitinase in barley endosperm."; Carlsberg Res. Commun. 52:31-37(1987).
[3]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). TISSUE=Seed; DOI=10.1006/jmbi.1993.1017; PubMed=8421299 [NCBI, ExPASy, EBI, Israel, Japan] Hart P.J., Monzingo A.F., Ready M.P., Ernst S.R., Robertus J.D.; "Crystal structure of an endochitinase from Hordeum vulgare L. seeds."; J. Mol. Biol. 229:189-193(1993).

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.
SIMILARITY: Belongs to the glycosyl hydrolase 19 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

L34210; AAA56786.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M62904; AAA32941.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A29104; A29104.
A38664; A38664.

UniGene

Hv.23168

3D structure databases

PDB

1CNS; X-ray; 1.91 A; A/B=24-266.	[ExPASy / RCSB / EBI]
2BAA; X-ray; 1.80 A; A=24-266.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1CNS; -.
2BAA; -.

ModBase

P23951.

Organism-specific databases

Gramene

P23951; -.

Ontologies

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

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

PANTHER

PTHR22595; Glyco_hydro_19_cat; 1.

Pfam

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

PIRSF

PIRSF001060; Endochitinase; 1.

ProDom

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

PROSITE

PS00773; CHITINASE_19_1; 1.
PS00774; CHITINASE_19_2; 1.

Other

P23951; -.

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

Keywords

3D-structure; Carbohydrate metabolism; Chitin degradation; Direct protein sequencing; Glycosidase; Hydrolase; Plant defense; Polysaccharide degradation; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 266`	`243`	`26 kDa endochitinase 2.`	`PRO_0000005297`
`DISULFID`	`46 108`
`DISULFID`	`120 128`
`DISULFID`	`227 259`
`VARIANT`	`205 205`	`1`	`D -> S.`
`CONFLICT`	`173 173`		`G -> A (in Ref. 1; AA sequence).`
`CONFLICT`	`205 205`		`D -> S (in Ref. 1; AA sequence).`
`HELIX`	`25 28`	`4`
`HELIX`	`31 37`	`7`
`TURN`	`38 42`	`5`
`TURN`	`49 51`	`3`
`HELIX`	`54 63`	`10`
`TURN`	`65 68`	`4`
`STRAND`	`70 72`	`3`
`HELIX`	`73 90`	`18`
`HELIX`	`102 104`	`3`
`STRAND`	`124 126`	`3`
`TURN`	`138 141`	`4`
`HELIX`	`145 155`	`11`
`TURN`	`159 161`	`3`
`HELIX`	`163 167`	`5`
`HELIX`	`170 182`	`13`
`HELIX`	`191 195`	`5`
`HELIX`	`203 207`	`5`
`HELIX`	`214 226`	`13`
`STRAND`	`227 230`	`4`
`HELIX`	`233 249`	`17`

Sequence information

Length: 266 AA [This is the length of the unprocessed precursor]

Molecular weight: 28156 Da [This is the MW of the unprocessed precursor]

CRC64: 0949BE88CC20B664 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRSLAVVVAV VATVAMAIGT ARGSVSSIVS RAQFDRMLLH RNDGACQAKG FYTYDAFVAA 

        70         80         90        100        110        120 
AAAFPGFGTT GSADAQKREV AAFLAQTSHE TTGGWATAPD GAFAWGYCFK QERGASSDYC 

       130        140        150        160        170        180 
TPSAQWPCAP GKRYYGRGPI QLSHNYNYGP AGRAIGVDLL ANPDLVATDA TVGFKTAIWF 

       190        200        210        220        230        240 
WMTAQPPKPS SHAVIAGQWS PSGADRAAGR VPGFGVITNI INGGIECGHG QDSRVADRIG 

       250        260 
FYKRYCDILG VGYGNNLDCY SQRPFA

P23951 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