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UniProtKB/Swiss-Prot entry P24091


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CHI2_TOBAC
Primary accession number P24091
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 1992
Sequence was last modified on March 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 82)
Name and origin of the protein
Protein name Endochitinase B [Precursor]
Synonyms CHN-B
EC 3.2.1.14
Gene name
Name: CHN50
From
Nicotiana tabacum (Common tobacco) [TaxID: 4097] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; Nicotiana.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Bright Yellow 4;
TISSUE=Leaf;
DOI=10.1007/BF00017912; PubMed=1888889 [NCBI, ExPASy, EBI, Israel, Japan]
Fukuda Y., Ohme M., Shinshi H.;
"Gene structure and expression of a tobacco endochitinase gene in suspension-cultured tobacco cells.";
Plant Mol. Biol. 16:1-10(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Havana 425;
TISSUE=Leaf;
DOI=10.1007/BF00266251; PubMed=1588915 [NCBI, ExPASy, EBI, Israel, Japan]
van Buuren M., Neuhaus J.-M., Shinshi H., Ryals J., Meins F. Jr.;
"The structure and regulation of homeologous tobacco endochitinase genes of Nicotiana sylvestris and N. tomentosiformis origin.";
Mol. Gen. Genet. 232:460-469(1992).
[3]
NUCLEOTIDE SEQUENCE OF 15-324, AND PROTEIN SEQUENCE OF 24-53.
STRAIN=cv. Havana;
PubMed=16593796 [NCBI, ExPASy, EBI, Israel, Japan]
Shinshi H., Mohnen D., Meins F. Jr.;
"Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin.";
Proc. Natl. Acad. Sci. U.S.A. 84:89-93(1987).
[4]
SUBCELLULAR LOCATION.
PubMed=1946457 [NCBI, ExPASy, EBI, Israel, Japan]
Neuhaus J.-M., Sticher L., Meins F. Jr., Boller T.;
"A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole.";
Proc. Natl. Acad. Sci. U.S.A. 88:10362-10366(1991).
[5]
HYDROXYLATION AT PRO-67 AND PRO-69, AND MASS SPECTROMETRY.
PubMed=1496378 [NCBI, ExPASy, EBI, Israel, Japan]
Sticher L., Hofsteenge J., Milani A., Neuhaus J.-M., Meins F. Jr.;
"Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins.";
Science 257:655-657(1992).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X51599; CAA35945.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X64519; CAA45822.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M15173; AAA34070.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S20981; S20981.
3D structure databases
HSSP P23951; 1CNS. [HSSP ENTRY / PDB]
SMR P24091; 24-315.
ModBase P24091.
Ontologies
GO
GO:0005773; Cellular component: vacuole (inferred from electronic annotation from UniProtKB-KW).
GO:0008061; Molecular function: chitin binding (inferred from electronic annotation from InterPro).
GO:0004568; Molecular function: chitinase activity (inferred from electronic annotation from InterPro).
GO:0016998; Biological process: cell wall catabolic process (inferred from electronic annotation from InterPro).
GO:0006032; Biological process: chitin catabolic process (inferred from electronic annotation from InterPro).
GO:0009626; Biological process: plant-type hypersensitive response (inferred from electronic annotation from UniProtKB-KW).
GO:0009607; Biological process: response to biotic stimulus (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001002; Chitin_bd_1.
IPR016283; Glyco_hydro_19.
IPR000726; Glyco_hydro_19_cat.
Graphical view of domain structure.
Gene3D G3DSA:3.30.60.10; Chitin_bd_1; 1.
PANTHER PTHR22595; Glyco_hydro_19_cat; 1.
Pfam PF00187; Chitin_bind_1; 1.
PF00182; Glyco_hydro_19; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001060; Endochitinase; 1.
PRINTS PR00451; CHITINBINDNG.
ProDom PD000609; Chitin_binding_1; 1.
PD354900; Glyco_hydro_19; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00270; ChtBD1; 1.
SMART graphical view of domain structure.
PROSITE PS00026; CHIT_BIND_I_1; 1.
PS50941; CHIT_BIND_I_2; 1.
PS00773; CHITINASE_19_1; 1.
PS00774; CHITINASE_19_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P24091.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carbohydrate metabolism; Chitin degradation; Chitin-binding; Direct protein sequencing; Glycosidase; Hydrolase; Hydroxylation; Hypersensitive response; Pathogenesis-related protein; Plant defense; Polysaccharide degradation; Signal; Vacuole.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    23  23      
CHAIN   24   317  294     Endochitinase B. PRO_0000005332
PROPEP   318   324  7     Removed in mature form (Probable). PRO_0000005333
DOMAIN   24    65  42     Chitin-binding type-1. 
MOD_RES   67    67        4-hydroxyproline. 
MOD_RES   69    69        4-hydroxyproline. 
DISULFID   26    41        By similarity. 
DISULFID   35    47        By similarity. 
DISULFID   40    54        By similarity. 
DISULFID   59    63        By similarity. 
DISULFID   96   158        By similarity. 
DISULFID   170   178        By similarity. 
DISULFID   277   309        By similarity. 
Sequence information
Length: 324 AA [This is the length of the unprocessed precursor] Molecular weight: 34721 Da [This is the MW of the unprocessed precursor] CRC64: FA65DC2113B33EB6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRLREFTALS SLLFSLLLLS ASAEQCGSQA GGARCASGLC CSKFGWCGNT NDYCGPGNCQ 

        70         80         90        100        110        120 
SQCPGGPTPP GGGDLGSIIS SSMFDQMLKH RNDNACQGKG FYSYNAFINA ARSFPGFGTS 

       130        140        150        160        170        180 
GDTTARKREI AAFFAQTSHE TTGGWATAPD GPYAWGYCWL REQGSPGDYC TPSGQWPCAP 

       190        200        210        220        230        240 
GRKYFGRGPI QISHNYNYGP CGRAIGVDLL NNPDLVATDP VISFKSALWF WMTPQSPKPS 

       250        260        270        280        290        300 
CHDVIIGRWQ PSSADRAANR LPGFGVITNI INGGLECGRG TDSRVQDRIG FYRRYCSILG 

       310        320 
VSPGDNLDCG NQRSFGNGLL VDTM 

P24091 in FASTA format

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