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Protein

Hevamine-A

Gene
N/A
Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Bifunctional enzyme with lysozyme / chitinase activity. May have a role in plugging the latex vessel and cessation of latex flow.

Miscellaneous

Two components of hevamine have been isolated: hevamine A (shown here), the most abundant, and hevamine B.

Catalytic activityi

Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei153Proton donor1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase, Multifunctional enzyme
Biological processCarbohydrate metabolism, Chitin degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH18 Glycoside Hydrolase Family 18

Names & Taxonomyi

Protein namesi
Recommended name:
Hevamine-A
Including the following 2 domains:
Chitinase (EC:3.2.1.14)
Lysozyme (EC:3.2.1.17)
OrganismiHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifieri3981 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Protein family/group databases

Allergomei1531 Hev b 14

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000001195227 – 299Hevamine-AAdd BLAST273
PropeptideiPRO_0000011953300 – 311Removed in mature formAdd BLAST12

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46 ↔ 93
Disulfide bondi76 ↔ 83
Disulfide bondi185 ↔ 214

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP23472

Structurei

Secondary structure

1311
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP23472
SMRiP23472
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23472

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiView protein in InterPro
IPR001223 Glyco_hydro18_cat
IPR001579 Glyco_hydro_18_chit_AS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00704 Glyco_hydro_18, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS01095 CHITINASE_18, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23472-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKRTQAILL LLLAISLIMS SSHVDGGGIA IYWGQNGNEG TLTQTCSTRK
60 70 80 90 100
YSYVNIAFLN KFGNGQTPQI NLAGHCNPAA GGCTIVSNGI RSCQIQGIKV
110 120 130 140 150
MLSLGGGIGS YTLASQADAK NVADYLWNNF LGGKSSSRPL GDAVLDGIDF
160 170 180 190 200
DIEHGSTLYW DDLARYLSAY SKQGKKVYLT AAPQCPFPDR YLGTALNTGL
210 220 230 240 250
FDYVWVQFYN NPPCQYSSGN INNIINSWNR WTTSINAGKI FLGLPAAPEA
260 270 280 290 300
AGSGYVPPDV LISRILPEIK KSPKYGGVML WSKFYDDKNG YSSSILDSVL
310
FLHSEECMTV L
Length:311
Mass (Da):33,718
Last modified:May 15, 2002 - v2
Checksum:i2CEED8658A28C908
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti296L → R in hevamine-B. 1
Natural varianti306E → K in hevamine-B. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007701 Genomic DNA Translation: CAA07608.1
DQ873889 mRNA Translation: ABI32402.2
AJ010397 mRNA Translation: CAA09110.1
PIRiT10761

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007701 Genomic DNA Translation: CAA07608.1
DQ873889 mRNA Translation: ABI32402.2
AJ010397 mRNA Translation: CAA09110.1
PIRiT10761

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HVQX-ray2.20A27-299[»]
1KQYX-ray1.92A27-299[»]
1KQZX-ray1.92A27-299[»]
1KR0X-ray1.92A27-299[»]
1KR1X-ray2.00A27-299[»]
1LLOX-ray1.85A27-299[»]
2HVMX-ray1.80A27-299[»]
ProteinModelPortaliP23472
SMRiP23472
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei1531 Hev b 14
CAZyiGH18 Glycoside Hydrolase Family 18

Proteomic databases

PRIDEiP23472

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP23472

Family and domain databases

InterProiView protein in InterPro
IPR001223 Glyco_hydro18_cat
IPR001579 Glyco_hydro_18_chit_AS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00704 Glyco_hydro_18, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS01095 CHITINASE_18, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCHLY_HEVBR
AccessioniPrimary (citable) accession number: P23472
Secondary accession number(s): Q0GBZ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 15, 2002
Last modified: May 10, 2017
This is version 108 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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