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P27275 (AMP_AMACA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 5, 2011. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Antimicrobial peptide 2

Short name=AMP2

Cleaved into the following chain:

  1. Antimicrobial peptide 1
    Short name=AMP1
OrganismAmaranthus caudatus (Love-lies-bleeding) (Inca-wheat)
Taxonomic identifier3567 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesAmaranthaceaeAmaranthus

Protein attributes

Sequence length86 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chitin-binding protein with a defensive function against numerous chitin containing fungal pathogens. It is also a potent inhibitor of Gram-positive bacteria.

Subunit structure

Homodimer Probable.

Miscellaneous

Its chitin-binding activity is strongly inhibited by divalent cations.

Sequence similarities

Contains 1 chitin-binding type-1 domain.

Ontologies

Keywords
   Biological processPlant defense
   DomainSignal
   LigandChitin-binding
   Molecular functionAntibiotic
Antimicrobial
Fungicide
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processdefense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to fungus

Inferred from electronic annotation. Source: UniProtKB-KW

killing of cells of other organism

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 2525 Ref.2
Peptide26 – 5530Antimicrobial peptide 2 Ref.2
PRO_0000005275
Peptide26 – 5429Antimicrobial peptide 1
PRO_0000005276
Propeptide56 – 8631Removed in mature form
PRO_0000005277

Regions

Domain29 – 5325Chitin-binding type-1

Amino acid modifications

Disulfide bond29 ↔ 40 Ref.4
Disulfide bond34 ↔ 46 Ref.4
Disulfide bond39 ↔ 53 Ref.4

Secondary structure

...... 86
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27275 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: C2C220E7DF373CB4

FASTA868,912
        10         20         30         40         50         60 
MVNMKCVALI VIVMMAFMMV DPSMGVGECV RGRCPSGMCC SQFGYCGKGP KYCGRASTTV 

        70         80 
DHQADVAATK TAKNPTDAKL AGAGSP 

« Hide

References

[1]"Cloning and characterization of a cDNA encoding an antimicrobial chitin-binding protein from amaranth, Amaranthus caudatus."
de Bolle M.F.C., David K.M.M., Rees S.B., Vanderleyden J., Cammue B.P.A., Broekaert W.F.
Plant Mol. Biol. 22:1187-1190(1993) [PubMed: 8400136] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Seed.
[2]"Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins."
Broekaert W.F., Marien W., Terras F.R.G., de Bolle M.F.C., Proost P., van Damme J., Dillen L., Claeys M., Rees S.B., Vanderleyden J., Cammue B.P.A.
Biochemistry 31:4308-4314(1992) [PubMed: 1567877] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-55.
Tissue: Seed.
[3]"H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus."
Martins J.C., Maes D., Loris R., Pepermans H.A.M., Wyns L., Willem R., Verheyden P.
J. Mol. Biol. 258:322-333(1996) [PubMed: 8627629] [Abstract]
Cited for: STRUCTURE BY NMR.
[4]"Location of the three disulfide bonds in an antimicrobial peptide from Amaranthus caudatus using mass spectrometry."
el Boiyoussfi M., Laus G., Verheyden P., Wyns L., Tourwe D., van Binst G.
J. Pept. Res. 49:336-340(1997) [PubMed: 9176817] [Abstract]
Cited for: DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72641 mRNA. Translation: CAA51210.1.
PIRS37381.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MMCNMR-A26-55[»]
1ZNTNMR-A26-55[»]
1ZUVNMR-A26-55[»]
1ZWUNMR-A26-55[»]
ProteinModelPortalP27275.
SMRP27275. Positions 26-55.
ModBaseSearch...

Protein family/group databases

CAZyCBM18. Carbohydrate-Binding Module Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013006. Antimicrobial_C6_CS.
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
Gene3DG3DSA:3.30.60.10. Chitin_bd_1. 1 hit.
PfamPF00187. Chitin_bind_1. 1 hit.
[Graphical view]
PRINTSPR00451. CHITINBINDNG.
ProDomPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMSSF57016. Chitin_bd_1. 1 hit.
PROSITEPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. False negative.
PS60011. PLANT_C6_AMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMP_AMACA
AccessionPrimary (citable) accession number: P27275
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1996
Last modified: April 5, 2011
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families