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UniProtKB/Swiss-Prot entry P23472


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

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Entry information
Entry name CHLY_HEVBR
Primary accession number P23472
Secondary accession number Q0GBZ6
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on May 15, 2002 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 74)
Name and origin of the protein
Protein name Hevamine-A [Precursor]
Synonyms None
Includes Chitinase
     (EC 3.2.1.14)
Lysozyme
     (EC 3.2.1.17)
Gene name None
From
Hevea brasiliensis (Para rubber tree) [TaxID: 3981] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids I; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae; Hevea.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. RRIM;
TISSUE=Latex, and Leaf;
Bokma E.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Philip S., Abraham T., Joseph A., Zacharia C.A., Jacob C.K.;
"Cloning and sequencing of chitinase gene in Hevea brasiliensis.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 27-299.
TISSUE=Latex;
PubMed=1879417 [NCBI, ExPASy, EBI, Israel, Japan]
Jekel P.A., Hartmann J.B.H., Beintema J.J.;
"The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex.";
Eur. J. Biochem. 200:123-130(1991).
[4]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1016/S0969-2126(94)00120-0; PubMed=7704528 [NCBI, ExPASy, EBI, Israel, Japan]
van Scheltinga A.C.T., Kalk K.H., Beintema J.J., Dijkstra B.W.;
"Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor.";
Structure 2:1181-1189(1994).
[5]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
DOI=10.1021/bi00048a003; PubMed=7495789 [NCBI, ExPASy, EBI, Israel, Japan]
van Scheltinga A.C.T., Armand S., Kalk K.H., Isogai A., Henrissat B., Dijkstra B.W.;
"Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis.";
Biochemistry 34:15619-15623(1995).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1006/jmbi.1996.0510; PubMed=8831791 [NCBI, ExPASy, EBI, Israel, Japan]
van Scheltinga A.C.T., Hennig M., Dijkstra B.W.;
"The 1.8-A resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18.";
J. Mol. Biol. 262:243-257(1996).
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
AJ007701; CAA07608.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ873889; ABI32402.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ010397; CAA09110.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T10761; T10761.
3D structure databases
PDB
1HVQ; X-ray; 2.20 A; A=27-299.[ExPASy / RCSB / EBI]
1KQY; X-ray; 1.92 A; A=27-299.[ExPASy / RCSB / EBI]
1KQZ; X-ray; 1.92 A; A=27-299.[ExPASy / RCSB / EBI]
1KR0; X-ray; 1.92 A; A=27-299.[ExPASy / RCSB / EBI]
1KR1; X-ray; 2.00 A; A=27-299.[ExPASy / RCSB / EBI]
1LLO; X-ray; 1.85 A; A=27-299.[ExPASy / RCSB / EBI]
2HVM; X-ray; 1.80 A; A=27-299.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1HVQ; -.
1KQY; -.
1KQZ; -.
1KR0; -.
1KR1; -.
1LLO; -.
2HVM; -.
ModBase P23472.
Ontologies
GO
GO:0005773; Cellular component: vacuole (inferred from electronic annotation from UniProtKB-KW).
GO:0043169; Molecular function: cation binding (inferred from electronic annotation from InterPro).
GO:0004568; Molecular function: chitinase activity (inferred from electronic annotation from EC).
GO:0003796; Molecular function: lysozyme activity (inferred from electronic annotation from EC).
GO:0006032; Biological process: chitin catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001223; Glyco_hydro18cat.
IPR001579; Glyco_hydro_18_chit_AS.
IPR013781; Glyco_hydro_sub_cat.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
Pfam PF00704; Glyco_hydro_18; 1.
Pfam graphical view of domain structure.
PROSITE PS01095; CHITINASE_18; 1.
BLOCKS P23472.
ProtoNet P23472.
Other
LinkHub P23472; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Carbohydrate metabolism; Chitin degradation; Direct protein sequencing; Glycosidase; Hydrolase; Multifunctional enzyme; Polysaccharide degradation; Signal; Vacuole.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    26  26      
CHAIN   27   299  273     Hevamine-A. PRO_0000011952
PROPEP   300   311  12     Removed in mature form. PRO_0000011953
ACT_SITE   153   153        Proton donor. 
DISULFID   46    93         
DISULFID   76    83         
DISULFID   185   214         
VARIANT   296   296  1     L -> R (in hevamine-B). 
VARIANT   306   306  1     E -> K (in hevamine-B). 
STRAND   28    35  8      
HELIX   37    39  3      
HELIX   42    47  6      
STRAND   51    63  13      
STRAND   66    70  5      
HELIX   79    85  7      
HELIX   86    95  10      
STRAND   99   105  7      
HELIX   116   130  15      
STRAND   131   133  3      
STRAND   146   151  6      
HELIX   160   170  11      
STRAND   173   175  3      
STRAND   178   181  4      
STRAND   184   188  5      
TURN   190   192  3      
HELIX   193   196  4      
STRAND   202   207  6      
HELIX   212   214  3      
HELIX   222   234  13      
STRAND   238   247  10      
HELIX   248   250  3      
STRAND   251   253  3      
HELIX   258   264  7      
HELIX   266   269  4      
STRAND   275   281  7      
HELIX   283   289  7      
HELIX   291   295  5      
HELIX   296   298  3      
Sequence information
Length: 311 AA [This is the length of the unprocessed precursor] Molecular weight: 33718 Da [This is the MW of the unprocessed precursor] CRC64: 2CEED8658A28C908 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAKRTQAILL LLLAISLIMS SSHVDGGGIA IYWGQNGNEG TLTQTCSTRK YSYVNIAFLN 

        70         80         90        100        110        120 
KFGNGQTPQI NLAGHCNPAA GGCTIVSNGI RSCQIQGIKV MLSLGGGIGS YTLASQADAK 

       130        140        150        160        170        180 
NVADYLWNNF LGGKSSSRPL GDAVLDGIDF DIEHGSTLYW DDLARYLSAY SKQGKKVYLT 

       190        200        210        220        230        240 
AAPQCPFPDR YLGTALNTGL FDYVWVQFYN NPPCQYSSGN INNIINSWNR WTTSINAGKI 

       250        260        270        280        290        300 
FLGLPAAPEA AGSGYVPPDV LISRILPEIK KSPKYGGVML WSKFYDDKNG YSSSILDSVL 

       310 
FLHSEECMTV L 

P23472 in FASTA format

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