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Protein

Pro-hevein

Gene

HEV1

Organism
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. chitin binding Source: UniProtKB-KW

GO - Biological processi

  1. defense response to bacterium Source: InterPro
  2. defense response to fungus Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-hevein
Alternative name(s):
Major hevein
Cleaved into the following 2 chains:
Alternative name(s):
Allergen: Hev b 6
Gene namesi
Name:HEV1
OrganismiHevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Taxonomic identifieri3981 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeCrotonoideaeMicrandreaeHevea

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei390. Hev b 6.
391. Hev b 6.01.
392. Hev b 6.02.
393. Hev b 6.03.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17173 PublicationsAdd
BLAST
Chaini18 – 204187Pro-heveinPRO_0000005280Add
BLAST
Chaini18 – 6043HeveinPRO_0000005281Add
BLAST
Propeptidei61 – 6661 PublicationPRO_0000005282
Chaini67 – 204138Win-like proteinPRO_0000005283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 35PROSITE-ProRule annotation1 Publication
Disulfide bondi29 ↔ 41PROSITE-ProRule annotation1 Publication
Disulfide bondi34 ↔ 48PROSITE-ProRule annotation1 Publication
Disulfide bondi54 ↔ 58PROSITE-ProRule annotation1 Publication
Disulfide bondi96 ↔ 128PROSITE-ProRule annotation
Disulfide bondi117 ↔ 151PROSITE-ProRule annotation
Disulfide bondi131 ↔ 187PROSITE-ProRule annotation

Post-translational modificationi

Proteolytically processed to yield the two chains of the mature protein.1 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Laticifer.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 244Combined sources
Helixi30 – 323Combined sources
Beta strandi37 – 393Combined sources
Beta strandi41 – 444Combined sources
Helixi45 – 484Combined sources
Helixi50 – 523Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HEVNMR-A18-60[»]
1Q9BX-ray1.50A18-60[»]
1T0WNMR-A18-49[»]
1WKXX-ray1.70A18-60[»]
4WP4X-ray1.43A18-60[»]
ProteinModelPortaliP02877.
SMRiP02877. Positions 18-60, 70-189.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02877.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 6043Chitin-binding type-1PROSITE-ProRule annotationAdd
BLAST
Domaini68 – 189122BarwinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 barwin domain.PROSITE-ProRule annotation
Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.40.40.10. 1 hit.
3.30.60.10. 1 hit.
InterProiIPR001153. Barwin.
IPR014733. Barwin-like_endoglucanase.
IPR018226. Barwin_CS.
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR009009. RlpA-like_DPBB.
[Graphical view]
PfamiPF00967. Barwin. 1 hit.
PF00187. Chitin_bind_1. 1 hit.
[Graphical view]
PRINTSiPR00602. BARWIN.
PR00451. CHITINBINDNG.
ProDomiPD004535. Barwin. 1 hit.
PD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF50685. SSF50685. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00771. 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]

Sequencei

Sequence statusi: Complete.

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

P02877-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIFIVVLLC LTGVAIAEQC GRQAGGKLCP NNLCCSQWGW CGSTDEYCSP
60 70 80 90 100
DHNCQSNCKD SGEGVGGGSA SNVLATYHLY NSQDHGWDLN AASAYCSTWD
110 120 130 140 150
ANKPYSWRSK YGWTAFCGPV GAHGQSSCGK CLSVTNTGTG AKTTVRIVDQ
160 170 180 190 200
CSNGGLDLDV NVFRQLDTDG KGYERGHITV NYQFVDCGDS FNPLFSVMKS

SVIN
Length:204
Mass (Da):21,859
Last modified:November 1, 1990 - v2
Checksum:iFBCEE57CDFC80569
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311N → D Possible deamidation.
Natural varianti73 – 731V → M.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36986 mRNA. Translation: AAA33357.1.
PIRiA38288. HVHV.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36986 mRNA. Translation: AAA33357.1.
PIRiA38288. HVHV.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HEVNMR-A18-60[»]
1Q9BX-ray1.50A18-60[»]
1T0WNMR-A18-49[»]
1WKXX-ray1.70A18-60[»]
4WP4X-ray1.43A18-60[»]
ProteinModelPortaliP02877.
SMRiP02877. Positions 18-60, 70-189.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei390. Hev b 6.
391. Hev b 6.01.
392. Hev b 6.02.
393. Hev b 6.03.
CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02877.

Family and domain databases

Gene3Di2.40.40.10. 1 hit.
3.30.60.10. 1 hit.
InterProiIPR001153. Barwin.
IPR014733. Barwin-like_endoglucanase.
IPR018226. Barwin_CS.
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR009009. RlpA-like_DPBB.
[Graphical view]
PfamiPF00967. Barwin. 1 hit.
PF00187. Chitin_bind_1. 1 hit.
[Graphical view]
PRINTSiPR00602. BARWIN.
PR00451. CHITINBINDNG.
ProDomiPD004535. Barwin. 1 hit.
PD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF50685. SSF50685. 1 hit.
SSF57016. SSF57016. 1 hit.
PROSITEiPS00771. 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]
ProtoNetiSearch...

Publicationsi

  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. 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.

Entry informationi

Entry nameiHEVE_HEVBR
AccessioniPrimary (citable) accession number: P02877
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: April 29, 2015
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.