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P06215 (CHIT_PHAVU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subcellular location

Vacuole By similarity. Note: Vacuolar and protoplast By similarity.

Induction

By ethylene.

Sequence similarities

Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily.

Contains 1 chitin-binding type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.2
Chain28 – 317290Endochitinase
PRO_0000005311
Propeptide318 – 32811Removed in mature form Probable
PRO_0000005312

Regions

Domain28 – 6841Chitin-binding type-1

Amino acid modifications

Disulfide bond30 ↔ 45 By similarity
Disulfide bond39 ↔ 51 By similarity
Disulfide bond44 ↔ 58 By similarity
Disulfide bond62 ↔ 66 By similarity
Disulfide bond97 ↔ 159 By similarity
Disulfide bond170 ↔ 178 By similarity
Disulfide bond277 ↔ 309 By similarity

Natural variations

Natural variant881M → V.
Natural variant1681T → A.
Natural variant2101L → F.

Experimental info

Sequence conflict401P → L in AAA33757. Ref.3
Sequence conflict541T → S AA sequence Ref.2
Sequence conflict561D → E AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P06215 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 0B5A73626C776C8A

FASTA32835,444
        10         20         30         40         50         60 
MKKNRMMMMI WSVGVVWMLL LVGGSYGEQC GRQAGGALCP GGNCCSQFGW CGSTTDYCGP 

        70         80         90        100        110        120 
GCQSQCGGPS PAPTDLSALI SRSTFDQMLK HRNDGACPAK GFYTYDAFIA AAKAYPSFGN 

       130        140        150        160        170        180 
TGDTATRKRE IAAFLGQTSH ETTGGWATAP DGPYAWGYCF VRERNPSTYC SATPQFPCAP 

       190        200        210        220        230        240 
GQQYYGRGPI QISWNYNYGQ CGRAIGVDLL NKPDLVATDS VISFKSALWF WMTAQSPKPS 

       250        260        270        280        290        300 
SHDVITSRWT PSSADVAARR LPGYGTVTNI INGGLECGRG QDSRVQDRIG FFKRYCDLLG 

       310        320 
VGYGNNLDCY SQTPFGNSLL LSDLVTSQ 

« Hide

References

[1]"Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris."
Broglie K.E., Gaynor J.J., Broglie R.M.
Proc. Natl. Acad. Sci. U.S.A. 83:6820-6824(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Saxa.
[2]"Amino-terminal sequence of ethylene-induced bean leaf chitinase reveals similarities to sugar-binding domains of wheat germ agglutinin."
Lucas J., Henschen A., Lottspeich F., Voegeli U., Boller T.
FEBS Lett. 193:208-210(1985)
Cited for: PROTEIN SEQUENCE OF 28-57.
[3]"Chitinase cDNA cloning and mRNA induction by fungal elicitor, wounding, and infection."
Hedrick S.A., Bell J.N., Boller T., Lamb C.J.
Plant Physiol. 86:182-186(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-51.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13968 mRNA. Translation: AAA33756.1.
M19052 mRNA. Translation: AAA33757.1.

3D structure databases

ProteinModelPortalP06215.
SMRP06215. Positions 28-316.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Proteomic databases

ProMEXP06215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.60.10. 1 hit.
InterProIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR016283. Glyco_hydro_19.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00187. Chitin_bind_1. 1 hit.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
PIRSFPIRSF001060. Endochitinase. 1 hit.
PRINTSPR00451. CHITINBINDNG.
ProDomPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEPS00026. 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]
ProtoNetSearch...

Entry information

Entry nameCHIT_PHAVU
AccessionPrimary (citable) accession number: P06215
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: February 19, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries