P52404 (CHI2_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endochitinase 2
EC=3.2.1.14

Gene names

Name:

CHTB2

Organism

Solanum tuberosum (Potato)

Taxonomic identifier

4113 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	316 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subcellular location	Vacuole By similarity. Note: Vacuolar and protoplast By similarity.
Developmental stage	Highest levels in younger leaves or stems segments and in older ones. Leaves and stems of intermediate age show a decreased expression. Appreciable amounts are also found in old root segments, and carpels.
Induction	In response to infection, elicitor, ethylene, wounding.
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
Cellular component	Vacuole
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
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
Cellular component	vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 18	›18	Potential
	Chain	19 – 309	291	Endochitinase 2		PRO_0000005322
	Propeptide	310 – 316	7	Removed in mature form, vacuolar targeting Potential		PRO_0000005323
Regions
	Domain	19 – 60	42	Chitin-binding type-1
Amino acid modifications
	Disulfide bond	21 ↔ 36		By similarity
	Disulfide bond	30 ↔ 42		By similarity
	Disulfide bond	35 ↔ 49		By similarity
	Disulfide bond	54 ↔ 58		By similarity
	Disulfide bond	87 ↔ 150		By similarity
	Disulfide bond	162 ↔ 170		By similarity
	Disulfide bond	269 ↔ 301		By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P52404 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 81FB3DB3F222A0C6	FASTA	316	33,629
	10 20 30 40 50 60 EFTTLFLLFS VLLLSASAEQ CGSQAGGALC ASGLCCSKFG WCGNTNDYCG PGNCQSQCPG 70 80 90 100 110 120 GSPGDLGGVI SNSMFDQMLN HRNDNACQGK GNFYSYNAFI SAAGSFPGFG TTGDITARKR 130 140 150 160 170 180 EIAAFFAQTS HETTGGWASA PDGPYAWGYC FLREQGSPGD YCTPSNQWPC APGRKYFGRG 190 200 210 220 230 240 PIQISHNYNY GPCGRAIGVD LLNNPDLVAT DSIISFKSAI WFWMTPQSPK PSCHDVITGR 250 260 270 280 290 300 WQPSGTDQAA NRVPGFGVIT NIINGGLECG HGSDSRVQDR IGFYRRYCGI LGVSPGDNLD 310 CGNQRSFGNG LLVDTV

References

[1]	"Primary structure and expression of mRNAs encoding basic chitinase and 1,3-beta-glucanase in potato." Beerhues L., Kombrink E. Plant Mol. Biol. 24:353-367(1994) [PubMed: 8111037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Datura. Tissue: Leaf.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U02606 mRNA. Translation: AAA17408.1.
PIR	S65020.
3D structure databases
ProteinModelPortal	P52404.
SMR	P52404. Positions 19-307.
ModBase	Search...
Protein family/group databases
CAZy	CBM18. Carbohydrate-Binding Module Family 18. GH19. Glycoside Hydrolase Family 19.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
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]
Gene3D	G3DSA:3.30.60.10. Chitin_bd_1. 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]
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

CHI2_SOLTU

Accession

Primary (citable) accession number: P52404

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 31, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program