P29022 (CHIA_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Endochitinase A EC=3.2.1.14 Alternative name(s): Seed chitinase A
Organism	Zea mays (Maize)
Taxonomic identifier	4577 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	280 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.
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Miscellaneous	Maize chitinase B seems to be less active than chitinase A.
Sequence similarities	Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily. Contains 1 chitin-binding type-1 domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Plant defense Polysaccharide degradation
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW defense response Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW somatic embryogenesis Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Cellular_component	apoplast Inferred from electronic annotation. Source: EnsemblPlants/Gramene plant-type cell wall Inferred from electronic annotation. Source: EnsemblPlants/Gramene plasma membrane Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Molecular_function	chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 280	255	Endochitinase A		PRO_0000005303
Regions
	Domain	26 – 60	35	Chitin-binding type-1
	Region	61 – 77	17	Hinge region (poly-Gly)
	Region	78 – 280	203	Catalytic
Amino acid modifications
	Disulfide bond	28 ↔ 36		By similarity
	Disulfide bond	30 ↔ 42		By similarity
	Disulfide bond	35 ↔ 49		By similarity
	Disulfide bond	53 ↔ 58		By similarity
	Disulfide bond	100 ↔ 149		By similarity
	Disulfide bond	161 ↔ 170		By similarity
	Disulfide bond	248 ↔ 280		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29022 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 4FC5BB7D938C1CC1	FASTA	280	29,125
	10 20 30 40 50 60 MANAPRILAL GLLALLCAAA GPAAAQNCGC QPNFCCSKFG YCGTTDAYCG DGCQSGPCRS 70 80 90 100 110 120 GGGGGGGGGG GGGGSGGANV ANVVTDAFFN GIKNQAGSGC EGKNFYTRSA FLSAVNAYPG 130 140 150 160 170 180 FAHGGTEVEG KREIAAFFAH VTHETGHFCY ISEINKSNAY CDASNRQWPC AAGQKYYGRG 190 200 210 220 230 240 PLQISWNYNY GPAGRDIGFN GLADPNRVAQ DAVIAFKTAL WFWMNNVHGV MPQGFGATIR 250 260 270 280 AINGALECNG NNPAQMNARV GYYKQYCQQL RVDPGPNLIC

References

[1]	"Antifungal proteins from plants. Purification, molecular cloning, and antifungal properties of chitinases from maize seed." Huynh Q.K., Hironaka C.M., Levine E.B., Smith C.E., Borgmeyer J.R., Shah D.M. J. Biol. Chem. 267:6635-6640(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Seed.
[2]	"Identification of an essential tyrosine residue in the catalytic site of a chitinase isolated from Zea mays that is selectively modified during inactivation with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide." Verburg J.G., Smith C.E., Lisek C.A., Huynh Q.K. J. Biol. Chem. 267:3886-3893(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 180-195. Tissue: Seed.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M84164 Genomic DNA. Translation: AAA33444.1.
PIR	A42424.
UniGene	Zm.119908.
3D structure databases
ProteinModelPortal	P29022.
ModBase	Search...
Protein family/group databases
CAZy	CBM18. Carbohydrate-Binding Module Family 18. GH19. Glycoside Hydrolase Family 19.
Proteomic databases
PRIDE	P29022.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
Gramene	P29022.
MaizeGDB	25130.
Family and domain databases
Gene3D	3.30.60.10. 1 hit.
InterPro	IPR001002. Chitin-bd_1. IPR018371. Chitin-binding_1_CS. IPR016283. Glyco_hydro_19. IPR000726. Glyco_hydro_19_cat. IPR023346. Lysozyme-like_dom. [Graphical view]
Pfam	PF00187. Chitin_bind_1. 1 hit. PF00182. Glyco_hydro_19. 1 hit. [Graphical view]
PIRSF	PIRSF001060. Endochitinase. 1 hit.
ProDom	PD000609. Chitin_bd_1. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00270. ChtBD1. 1 hit. [Graphical view]
SUPFAM	SSF57016. Chitin_bd_1. 1 hit. SSF53955. SSF53955. 1 hit.
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_MAIZE

Accession

Primary (citable) accession number: P29022

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program