Q9FRV0 (CHIC_SECCE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Basic endochitinase C
EC=3.2.1.14

Alternative name(s):
Rye seed chitinase-c
Short name=RSC-c

Gene names

Name:

rscc

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	266 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 of fungi and degrades nascent chitin. Ref.1 Ref.6 Ref.7
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Ref.1 Ref.3
Tissue specificity	Localized to the starchy endoderm of the seed May localize to other parts of the seed including the aleurone cells (at protein level). Ref.5 Ref.6
Developmental stage	Levels increase from 23 to 40 days after flowering, and are maintained until maturation (at protein level). Ref.5 Ref.6
Sequence similarities	Belongs to the glycosyl hydrolase 19 family. Chitinase class II subfamily. Ref.1
Biophysicochemical properties	pH dependence: Optimum pH is about 5.0. Stable between pH 4-8. Ref.3 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 15-30% 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 Inferred from direct assay Ref.7. Source: UniProtKB chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW defense response to fungus Inferred from direct assay Ref.6Ref.1Ref.7. Source: UniProtKB killing of cells of other organism Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred by curator Ref.1. Source: UniProtKB
Molecular function	chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from direct assay Ref.1Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Ref.1 Ref.2 Ref.3
	Chain	24 – 266	243	Basic endochitinase C Ref.1		PRO_0000042671
Sites
	Site	95	1	May be involved in substrate-binding Ref.5
	Site	118	1	May be involved in substrate-binding Ref.4
Amino acid modifications
	Disulfide bond	46 ↔ 108		Ref.2
	Disulfide bond	120 ↔ 128		Ref.2
	Disulfide bond	246 ↔ 259		Ref.2
Experimental info
	Mutagenesis	90	1	E → Q: Abolishes chitinase activity. Ref.1
	Mutagenesis	95	1	W → A: Chitinase activity is reduced to 51.2% of wild-type. Decreased anti-fungal activity. Ref.1
	Mutagenesis	112	1	E → Q: Chitinase activity is reduced to 0.33% of wild-type. Decreased anti-fungal activity. Ref.1
	Mutagenesis	118	1	D → A: Chitinase activity is reduced to 79% of wild-type. Decreased anti-fungal activity. Ref.1
	Mutagenesis	143	1	S → A: Chitinase activity is reduced to 1.2% of wild-type. Decreased anti-fungal activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9FRV0 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: E5E22C5BE43DB589	FASTA	266	28,302
	10 20 30 40 50 60 MRSLAVVVAV VATVAMAIGT AHGSVSSIIS HAQFDRMLLH RNDGACQAKG FYTYDAFVAA 70 80 90 100 110 120 ANAFPGFGAT GSTDARKRDV AAFLAQTSHE TTGGWATAPD GAFAWGYCFK QERGAAADYC 130 140 150 160 170 180 TPSAQWPCAP GKRYYGRGPI QLSHNYNYGP AGRAIGVDLL RNPDLVATDP TVSFKTALWF 190 200 210 220 230 240 WMTAQAPKPS SHAVITGKWS PSGADRAAGR APGFGVITNI INGGLECGHG QDSRVADRIG 250 260 FYKRYCDILG VGYGDNLDCY NQRPFA

References

[1]	"Molecular cloning, functional expression, and mutagenesis of cDNA encoding rye (Secale cereale) seed chitinase-c." Ohnuma T., Yagi M., Yamagami T., Taira T., Aso Y., Ishiguro M. Biosci. Biotechnol. Biochem. 66:277-284(2002) [PubMed: 11999399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-28, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-90; TRP-95; GLU-112; ASP-118 AND SER-143. Tissue: Seed.
[2]	"The complete amino acid sequence of chitinase-c from the seeds of rye (Secale cereal)." Yamagami T., Funatsu G. Biosci. Biotechnol. Biochem. 57:1854-1861(1993) [PubMed: 7764335] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-266, DISULFIDE BONDS. Tissue: Seed.
[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 24-30, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"Identification of the aspartic acid residue located at or near substrate-binding site of rye seed chitinase-c." Yamagami T., Funatsu G. Biosci. Biotechnol. Biochem. 62:383-385(1998) [PubMed: 9532801] [Abstract] Cited for: PROTEIN SEQUENCE OF 114-133 AND 254-260, ROLE OF ASP-118 IN SUBSTRATE BINDING.
[5]	"Identification of the tryptophan residue located at the substrate-binding site of rye seed chitinase-c." Yamagami T., Funatsu G. Biosci. Biotechnol. Biochem. 59:1076-1081(1995) Cited for: ROLE OF TRP-95 IN SUBSTRATE BINDING.
[6]	"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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB051579 mRNA. Translation: BAB18520.1.
PIR	JC7816. JN0884.
3D structure databases
ProteinModelPortal	Q9FRV0.
SMR	Q9FRV0. Positions 24-266.
ModBase	Search...
Protein family/group databases
CAZy	GH19. Glycoside Hydrolase Family 19.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Gramene	Q9FRV0.
Family and domain databases
InterPro	IPR016283. Glyco_hydro_19. IPR000726. Glyco_hydro_19_cat. IPR023346. Lysozyme-like_dom. [Graphical view]
Pfam	PF00182. Glyco_hydro_19. 1 hit. [Graphical view]
PIRSF	PIRSF001060. Endochitinase. 1 hit.
SUPFAM	SSF53955. SSF53955. 1 hit.
PROSITE	PS00773. CHITINASE_19_1. 1 hit. PS00774. CHITINASE_19_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHIC_SECCE

Accession

Primary (citable) accession number: Q9FRV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	March 1, 2001
Last modified:	October 19, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program