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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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
PeptideiPRO_000000527526 – 55Antimicrobial peptide 2Add BLAST30
PeptideiPRO_000000527626 – 54Antimicrobial peptide 1Add BLAST29
PropeptideiPRO_000000527756 – 86Removed in mature formAdd BLAST31

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi29 ↔ 401 Publication
Disulfide bondi34 ↔ 461 Publication
Disulfide bondi39 ↔ 531 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.Curated

Structurei

Secondary structure

186
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 32Combined sources3
Beta strandi46 – 49Combined sources4
Helixi50 – 53Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP27275.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 53Chitin-binding type-1Add BLAST25

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MMCNMR-A26-55[»]
1ZNTNMR-A26-55[»]
1ZUVNMR-A26-55[»]
1ZWUNMR-A26-55[»]
ProteinModelPortaliP27275.
SMRiP27275.
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...

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: November 2, 2016
This is version 101 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.