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Protein

Defensin-like protein 1

Gene
N/A
Organism
Aesculus hippocastanum (Horse chestnut)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Possesses antimicrobial activity sensitive to inorganic cations. Binds specifically to the fungal plasma membrane. Has no inhibitory effect on insect gut alpha-amylase.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Fungicide

Keywords - Biological processi

Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Defensin-like protein 1
Alternative name(s):
Cysteine-rich antimicrobial protein 1
Defensin AMP1
Short name:
AhAMP1
OrganismiAesculus hippocastanum (Horse chestnut)
Taxonomic identifieri43364 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsSapindalesHippocastanaceaeAesculus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5050Defensin-like protein 1PRO_0000366950Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi2 ↔ 50
Disulfide bondi14 ↔ 35
Disulfide bondi20 ↔ 44
Disulfide bondi24 ↔ 46

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
50
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi8 – 103Combined sources
Helixi17 – 259Combined sources
Beta strandi26 – 283Combined sources
Beta strandi31 – 388Combined sources
Beta strandi41 – 488Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BK8NMR-A1-50[»]
ProteinModelPortaliQ7M1F3.
SMRiQ7M1F3. Positions 1-50.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7M1F3.

Family & Domainsi

Sequence similaritiesi

Belongs to the DEFL family.Curated

Family and domain databases

Gene3Di3.30.30.10. 1 hit.
InterProiIPR003614. Scorpion_toxin-like.
[Graphical view]
SMARTiSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMiSSF57095. SSF57095. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7M1F3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LCNERPSQTW SGNCGNTAHC DKQCQDWEKA SHGACHKREN HWKCFCYFNC
Length:50
Mass (Da):5,863
Last modified:December 15, 2003 - v1
Checksum:iA87D5BF8752BB560
GO

Sequence databases

PIRiS66218.

Cross-referencesi

Sequence databases

PIRiS66218.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BK8NMR-A1-50[»]
ProteinModelPortaliQ7M1F3.
SMRiQ7M1F3. Positions 1-50.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ7M1F3.

Family and domain databases

Gene3Di3.30.30.10. 1 hit.
InterProiIPR003614. Scorpion_toxin-like.
[Graphical view]
SMARTiSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMiSSF57095. SSF57095. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae."
    Osborn R.W., De Samblanx G.W., Thevissen K., Goderis I., Torrekens S., Van Leuven F., Attenborough S., Rees S.B., Broekaert W.F.
    FEBS Lett. 368:257-262(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION.
    Tissue: Seed.
  2. "The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance."
    Fant F., Vranken W.F., Borremans F.A.M.
    Proteins 37:388-403(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  3. "Specific binding sites for an antifungal plant defensin from Dahlia (Dahlia merckii) on fungal cells are required for antifungal activity."
    Thevissen K., Osborn R.W., Acland D.P., Broekaert W.F.
    Mol. Plant Microbe Interact. 13:54-61(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiDEF1_AESHI
AccessioniPrimary (citable) accession number: Q7M1F3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 15, 2003
Last modified: December 9, 2015
This is version 46 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.