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Protein

Antimicrobial peptide 2

Gene
N/A
Organism
Amaranthus caudatus (Love-lies-bleeding) (Inca-wheat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Fungicide

Keywords - Biological processi

Plant defense

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Antimicrobial peptide 2
Short name:
AMP2
Cleaved into the following chain:
Antimicrobial peptide 1
Short name:
AMP1
OrganismiAmaranthus caudatus (Love-lies-bleeding) (Inca-wheat)
Taxonomic identifieri3567 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeAmaranthus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Peptidei26 – 5530Antimicrobial peptide 2PRO_0000005275Add
BLAST
Peptidei26 – 5429Antimicrobial peptide 1PRO_0000005276Add
BLAST
Propeptidei56 – 8631Removed in mature formPRO_0000005277Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 401 Publication
Disulfide bondi34 ↔ 461 Publication
Disulfide bondi39 ↔ 531 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.Curated

Structurei

Secondary structure

1
86
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 323Combined sources
Beta strandi46 – 494Combined sources
Helixi50 – 534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MMCNMR-A26-55[»]
1ZNTNMR-A26-55[»]
1ZUVNMR-A26-55[»]
1ZWUNMR-A26-55[»]
ProteinModelPortaliP27275.
SMRiP27275. Positions 26-55.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27275.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 5325Chitin-binding type-1Add
BLAST

Sequence similaritiesi

Contains 1 chitin-binding type-1 domain.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR013006. Antimicrobial_C6_CS.
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 1 hit.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS60011. PLANT_C6_AMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P27275-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNMKCVALI VIVMMAFMMV DPSMGVGECV RGRCPSGMCC SQFGYCGKGP
60 70 80
KYCGRASTTV DHQADVAATK TAKNPTDAKL AGAGSP
Length:86
Mass (Da):8,912
Last modified:October 1, 1996 - v2
Checksum:iC2C220E7DF373CB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72641 mRNA. Translation: CAA51210.1.
PIRiS37381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72641 mRNA. Translation: CAA51210.1.
PIRiS37381.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MMCNMR-A26-55[»]
1ZNTNMR-A26-55[»]
1ZUVNMR-A26-55[»]
1ZWUNMR-A26-55[»]
ProteinModelPortaliP27275.
SMRiP27275. Positions 26-55.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP27275.

Family and domain databases

Gene3Di3.30.60.10. 1 hit.
InterProiIPR013006. Antimicrobial_C6_CS.
IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 1 hit.
[Graphical view]
PRINTSiPR00451. CHITINBINDNG.
ProDomiPD000609. Chitin_bd_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 1 hit.
[Graphical view]
SUPFAMiSSF57016. SSF57016. 1 hit.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS60011. PLANT_C6_AMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.

Entry informationi

Entry nameiAMP_AMACA
AccessioniPrimary (citable) accession number: P27275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1996
Last modified: December 9, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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.