Reviewed, UniProtKB/Swiss-Prot Q9FRV1 (CHIA_SECCE)

Names and origin

Protein names

Recommended name:
    Basic endochitinase A
    EC=3.2.1.14
Alternative name(s):
    Rye seed chitinase-a
      Short name=RSC-a

Gene names

Name:

rsca

Organism

Secale cereale (Rye)

Taxonomic identifier

4550 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Secale

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Defense against chitin containing fungal pathogens. Binds the hyphal tips, lateral walls and septa of fungi and degrades mature chitin. Ref.1 Ref.3 Ref.5 Ref.6
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Ref.1 Ref.3 Ref.5
Tissue specificity	Localized in the aleurone cells of the seed endosperm (at protein level). Ref.5
Developmental stage	Levels increase from 23 to 40 days after flowering, and are maintained until maturation (at protein level). Ref.5
Sequence similarities	Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily. Contains 1 chitin-binding type-1 domain.
Biophysicochemical properties	pH dependence: Optimum pH is about 5.0. Stable between pH 4-8. Temperature dependence: Enzyme activity is retained almost fully under 40 degrees Celsius and completely destroyed at 70 degrees Celsius. At 60 degrees Celsius the activity was over 80% compared to the untreated enzyme. Ref.3

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Plant defense Polysaccharide degradation
Domain	Signal
Ligand	Chitin-binding
Molecular function	Antimicrobial Fungicide Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Ref.6 Inferred from direct assay. Source: UniProtKB chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW defense response to fungus Ref.5 Ref.6 Inferred from direct assay. Source: UniProtKB killing of cells of another organism Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Ref.1 Inferred by curator. Source: UniProtKB
Molecular function	chitin binding Ref.1 Inferred from direct assay. Source: UniProtKB chitinase activity Ref.1 Ref.3 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Ref.1 Ref.3 Ref.2
	Chain	20 – 321	302	Basic endochitinase A Ref.1		PRO_0000042670
Regions
	Domain	20 – 60	41	Chitin-binding type-1
	Region	62 – 79	18	Hinge region (Gly/Pro/Thr-rich)
	Region	80 – 321	242	Catalytic
Amino acid modifications
	Disulfide bond	22 ↔ 37		Ref.4
	Disulfide bond	31 ↔ 43		Ref.4
	Disulfide bond	34 ↔ 61		Ref.4
	Disulfide bond	36 ↔ 50		Ref.4
	Disulfide bond	54 ↔ 58		Ref.4
	Disulfide bond	101 ↔ 163		Ref.4
	Disulfide bond	175 ↔ 183		Ref.4
	Disulfide bond	301 ↔ 314		Ref.4
Experimental info
	Mutagenesis	42	1	W → A: Reduces chitinase activity towards soluble chitin to 65.5% and towards insoluble chitin. Reduces chitin-binding activity and anti-fungal activity. Ref.1
	Mutagenesis	145	1	E → Q: Abolishes chitinase activity towards insoluble and soluble chitin. Abolishes chitin-binding activity and anti-fungal activity. Ref.1
	Sequence conflict	305	1	R → G AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9FRV1-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 76E5902BBC337C8E	FASTA	321	33,642
	10 20 30 40 50 60 MGAFALFAVL AMAVTMAVAE QCGSQAGGAT CPNCLCCSRF GWCGSTSDYC GDGCQSQCAG 70 80 90 100 110 120 CGGGGTPVTP TPTPSGGGGV SSIVSRALFD RMLLHRNDGA CQAKGFYTYD AFVAAAGAFP 130 140 150 160 170 180 GFGTTGSTDT RKREVAAFLA QTSHETTGGW ATAPDGAFAW GYCFKQERGA TSNYCTPSAQ 190 200 210 220 230 240 WPCAPGKSYY GRGPIQLSHN YNYGPAGRAI GVDLLRNPDL VATDPTVSFK TAMWFWMTAQ 250 260 270 280 290 300 APKPSSHAVI TGQWSPSGTD RAAGRVPGFG VITNIVNGGI ECGHGQDSRV ADRIGFYKRY 310 320 CDILRVGYGN NLDCYNQRPF A

References

[1]	"Molecular cloning, functional expression, and mutagenesis of cDNA encoding class I chitinase from rye (Secale cereale) seeds." Ohnuma T., Taira T., Yamagami T., Aso Y., Ishiguro M. Biosci. Biotechnol. Biochem. 68:324-332(2004) [PubMed: 14981295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-24, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TRP-42 AND GLU-145. Tissue: Seed.
[2]	"The complete amino acid sequence of chitinase-a from the seeds of rye (Secale cereal)." Yamagami T., Funatsu G. Biosci. Biotechnol. Biochem. 58:322-329(1994) [PubMed: 7764543] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-321.
[3]	"Purification and some properties of three chitinases from the seeds of rye (Secale cereale)." Yamagami T., Funatsu G. Biosci. Biotechnol. Biochem. 57:643-647(1993) [PubMed: 7763659] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-26, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"Positions of disulfide bonds in rye (Secale cereale) seed chitinase-a." Yamagami T., Funatsu G., Ishiguro M. Biosci. Biotechnol. Biochem. 64:1313-1316(2000) [PubMed: 10923812] [Abstract] Cited for: DISULFIDE BONDS.
[5]	"Localization, accumulation, and antifungal activity of chitinases in rye (Secale cereale) seed." Taira T., Yamagami T., Aso Y., Ishiguro M., Ishihara M. Biosci. Biotechnol. Biochem. 65:2710-2718(2001) [PubMed: 11826968] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[6]	"Antifungal activity of rye (Secale cereale) seed chitinases: the different binding manner of class I and class II chitinases to the fungal cell walls." Taira T., Ohnuma T., Yamagami T., Aso Y., Ishiguro M., Ishihara M. Biosci. Biotechnol. Biochem. 66:970-977(2002) [PubMed: 12092848] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB051578 mRNA. Translation: BAB18519.1.
PIR	JC2071.
3D structure databases
SMR	Q9FRV1. Positions 20-320, 80-321.
ModBase	Search...
Protein family/group databases
CAZy	CBM18. Carbohydrate-Binding Module Family 18. GH19. Glycoside Hydrolase Family 19.
Organism-specific databases
Gramene	Q9FRV1.
Enzyme and pathway databases
BRENDA	3.2.1.14. 1472.
Family and domain databases
InterPro	IPR018371. Chitin-binding_1_CS. IPR001002. Chitin_bd_1. IPR016283. Glyco_hydro_19. IPR000726. Glyco_hydro_19_cat. [Graphical view]
Gene3D	G3DSA:3.30.60.10. Chitin_bd_1. 1 hit.
PANTHER	PTHR22595. Glyco_hydro_19_cat. 1 hit.
Pfam	PF00187. Chitin_bind_1. 1 hit. PF00182. Glyco_hydro_19. 1 hit. [Graphical view]
PIRSF	PIRSF001060. Endochitinase. 1 hit.
PRINTS	PR00451. CHITINBINDNG.
ProDom	PD000609. Chitin_bd_1. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00270. ChtBD1. 1 hit. [Graphical view]
PROSITE	PS00026. CHIT_BIND_I_1. 1 hit. PS50941. CHIT_BIND_I_2. 1 hit. PS00773. CHITINASE_19_1. 1 hit. PS00774. CHITINASE_19_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHIA_SECCE

Accession

Primary (citable) accession number: Q9FRV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	March 1, 2001
Last modified:	November 24, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)