Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P02877 (HEVE_HEVBR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Pro-hevein
Alternative name(s):
Major hevein

Cleaved into the following 2 chains:

  1. Hevein
    Alternative name(s):
    Allergen=Hev b 6
  2. Win-like protein
Gene names
Name:HEV1
OrganismHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifier3981 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin. Can inhibit fungal growth.

Tissue specificity

Laticifer.

Post-translational modification

Proteolytically processed to yield the two chains of the mature protein.

Allergenic properties

Causes an allergic reaction in human.

Sequence similarities

Contains 1 barwin domain.

Contains 1 chitin-binding type-1 domain.

Ontologies

Keywords
   DiseaseAllergen
   DomainSignal
   LigandChitin-binding
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from electronic annotation. Source: InterPro

defense response to fungus

Inferred from electronic annotation. Source: InterPro

   Molecular_functionchitin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.2 Ref.4 Ref.5
Chain18 – 204187Pro-hevein
PRO_0000005280
Chain18 – 6043Hevein
PRO_0000005281
Propeptide61 – 666
PRO_0000005282
Chain67 – 204138Win-like protein
PRO_0000005283

Regions

Domain18 – 6043Chitin-binding type-1
Domain68 – 189122Barwin

Amino acid modifications

Disulfide bond20 ↔ 35 Ref.7
Disulfide bond29 ↔ 41 Ref.7
Disulfide bond34 ↔ 48 Ref.7
Disulfide bond54 ↔ 58 Ref.7
Disulfide bond96 ↔ 128 By similarity
Disulfide bond117 ↔ 151 By similarity
Disulfide bond131 ↔ 187 By similarity

Natural variations

Natural variant311N → D Possible deamidation.
Natural variant731V → M.

Secondary structure

............ 204
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02877 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: FBCEE57CDFC80569

FASTA20421,859
        10         20         30         40         50         60 
MNIFIVVLLC LTGVAIAEQC GRQAGGKLCP NNLCCSQWGW CGSTDEYCSP DHNCQSNCKD 

        70         80         90        100        110        120 
SGEGVGGGSA SNVLATYHLY NSQDHGWDLN AASAYCSTWD ANKPYSWRSK YGWTAFCGPV 

       130        140        150        160        170        180 
GAHGQSSCGK CLSVTNTGTG AKTTVRIVDQ CSNGGLDLDV NVFRQLDTDG KGYERGHITV 

       190        200 
NYQFVDCGDS FNPLFSVMKS SVIN 

« Hide

References

[1]"Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis)."
Broekaert W.F., Lee H.I., Kush A., Chua N.H., Raikhel N.
Proc. Natl. Acad. Sci. U.S.A. 87:7633-7637(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Amino-acid sequence of hevein."
Walujono K., Scholma R.A., Beintema J.J., Mariono A., Hahn A.M.
(In) Proceedings of the international rubber conference, pp.2:518-531, Rubber Research Institute of Malaysia, Kuala Lumpur (1975)
Cited for: PROTEIN SEQUENCE OF 18-60.
Tissue: Latex.
[3]Beintema J.J.
Submitted (JUN-1977) to the PIR data bank
Cited for: SEQUENCE REVISION TO 51-52.
[4]"Co- and post-translational processing of the hevein preproprotein of latex of the rubber tree (Hevea brasiliensis)."
Lee H.-I., Broekaert W.F., Raikhel N.V.
J. Biol. Chem. 266:15944-15948(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-26 AND 67-77, PROTEOLYTIC PROCESSING.
Tissue: Latex.
[5]"Characterization of latex allergenic components by capillary zone electrophoresis and N-terminal sequence analysis."
Chen H.-D., Chen C.-L., Huang S.-W., Kung H.-F., Chen H.-C.
J. Biomed. Sci. 5:421-427(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-35.
Tissue: Latex.
[6]"Crystal structure of hevein at 2.8-A resolution."
Rodriguez-Romero A., Ravichandran K.G., Soriano-Garcia M.
FEBS Lett. 291:307-309(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-60.
[7]"Hevein: NMR assignment and assessment of solution-state folding for the agglutinin-toxin motif."
Andersen N.H., Cao B., Rodriguez-Romero A., Arreguin B.
Biochemistry 32:1407-1422(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 18-60, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36986 mRNA. Translation: AAA33357.1.
PIRHVHV. A38288.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HEVNMR-A18-60[»]
1Q9BX-ray1.50A18-60[»]
1T0WNMR-A18-49[»]
1WKXX-ray1.70A18-60[»]
ProteinModelPortalP02877.
SMRP02877. Positions 18-60, 70-189.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome390. Hev b 6.
391. Hev b 6.01.
392. Hev b 6.02.
393. Hev b 6.03.
CAZyCBM18. Carbohydrate-Binding Module Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.40.10. 1 hit.
3.30.60.10. 1 hit.
InterProIPR001153. Barwin.
IPR014733. Barwin-like_endoglucanase.
IPR018226. Barwin_CS.
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR009009. RlpA-like_DPBB.
[Graphical view]
PfamPF00967. Barwin. 1 hit.
PF00187. Chitin_bind_1. 1 hit.
[Graphical view]
PRINTSPR00602. BARWIN.
PR00451. CHITINBINDNG.
ProDomPD004535. Barwin. 1 hit.
PD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMSSF50685. SSF50685. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEPS00771. BARWIN_1. 1 hit.
PS00772. BARWIN_2. 1 hit.
PS51174. BARWIN_3. 1 hit.
PS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02877.

Entry information

Entry nameHEVE_HEVBR
AccessionPrimary (citable) accession number: P02877
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: June 11, 2014
This is version 113 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Allergens

Nomenclature of allergens and list of entries