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P08252 (CHI1_TOBAC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. 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 namesRecommended name:
Endochitinase A

Short name=CHN-A
EC=3.2.1.14
Gene names
Name:CHN48
OrganismNicotiana tabacum (Common tobacco)
Taxonomic identifier4097 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Protein attributes

Sequence length329 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. Note: Vacuolar and protoplast. Ref.3

Developmental stage

Expressed during flower formation. Ref.2

Induction

By ethylene.

Post-translational modification

The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein.

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 – 2323
Chain24 – 322299Endochitinase A
PRO_0000005330
Propeptide323 – 3297Removed in mature form
PRO_0000005331

Regions

Domain24 – 6542Chitin-binding type-1

Amino acid modifications

Modified residue6714-hydroxyproline; partial Ref.4
Modified residue6914-hydroxyproline Ref.4
Modified residue7114-hydroxyproline Ref.4
Modified residue7214-hydroxyproline Ref.4
Modified residue7414-hydroxyproline Ref.4
Modified residue7514-hydroxyproline; partial Ref.4
Disulfide bond26 ↔ 41 By similarity
Disulfide bond35 ↔ 47 By similarity
Disulfide bond40 ↔ 54 By similarity
Disulfide bond59 ↔ 63 By similarity
Disulfide bond101 ↔ 163 By similarity
Disulfide bond175 ↔ 183 By similarity
Disulfide bond282 ↔ 314 By similarity

Experimental info

Sequence conflict73 – 786TPPGGG → HPTRC in AAB23374. Ref.2
Sequence conflict2631A → S in AAB23374. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P08252 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 3EC99D96E6C0114C

FASTA32935,156
        10         20         30         40         50         60 
MRLCKFTALS SLLFSLLLLS ASAEQCGSQA GGARCPSGLC CSKFGWCGNT NDYCGPGNCQ 

        70         80         90        100        110        120 
SQCPGGPTPT PPTPPGGGDL GSIISSSMFD QMLKHRNDNA CQGKGFYSYN AFINAARSFP 

       130        140        150        160        170        180 
GFGTSGDTTA RKREIAAFFA QTSHETTGGW ATAPDGPYAW GYCWLREQGS PGDYCTPSGQ 

       190        200        210        220        230        240 
WPCAPGRKYF GRGPIQISHN YNYGPCGRAI GVDLLNNPDL VATDPVISFK SALWFWMTPQ 

       250        260        270        280        290        300 
SPKPSCHDVI IGRWQPSAGD RAANRLPGFG VITNIINGGL ECGRGTDSRV QDRIGFYRRY 

       310        320 
CSILGVSPGD NLDCGNQRSF GNGLLVDTM 

« Hide

References

[1]"Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding a cysteine-rich domain."
Shinshi H., Neuhaus J.-M., Ryals J., Meins F. Jr.
Plant Mol. Biol. 14:357-368(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: cv. Havana 425.
Tissue: Leaf.
[2]"Chitinase, beta-1,3-glucanase, osmotin, and extensin are expressed in tobacco explants during flower formation."
Neale A.D., Wahleithner J.A., Lund M., Bonnett H.T., Kelly A., Meeks-Wagner D.R., Peacock W.J., Dennis E.S.
Plant Cell 2:673-684(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
Strain: cv. Samsun.
Tissue: Flower bud.
[3]"A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole."
Neuhaus J.-M., Sticher L., Meins F. Jr., Boller T.
Proc. Natl. Acad. Sci. U.S.A. 88:10362-10366(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[4]"Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins."
Sticher L., Hofsteenge J., Milani A., Neuhaus J.-M., Meins F. Jr.
Science 257:655-657(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: HYDROXYLATION AT PRO-67; PRO-69; PRO-71; PRO-72; PRO-74 AND PRO-75, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16938 Genomic DNA. Translation: CAA34812.1.
X16939 mRNA. Translation: CAA34813.1.
S44869 mRNA. Translation: AAB23374.1.
PIRS08627.

3D structure databases

ProteinModelPortalP08252.
SMRP08252. Positions 24-320.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

Proteomic databases

ProMEXP08252.

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 nameCHI1_TOBAC
AccessionPrimary (citable) accession number: P08252
Secondary accession number(s): Q41180
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 108 of the entry and version 2 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