Reviewed, UniProtKB/Swiss-Prot P27275 (AMP_AMACA)

Names and origin

Protein names	Recommended name:     Antimicrobial peptide 2       Short name=AMP2 Cleaved into the following chain:     1- Recommended name:             Antimicrobial peptide 1                 Short name=AMP1
Organism	Amaranthus caudatus (Love-lies-bleeding) (Inca-wheat)
Taxonomic identifier	3567 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Amaranthus

Protein attributes

Sequence length	86 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Plant defense
Domain	Signal
Ligand	Chitin-binding
Molecular function	Antibiotic Antimicrobial Fungicide
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro chitin catabolic process Inferred from electronic annotation. Source: InterPro defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW defense response to fungus Inferred from electronic annotation. Source: UniProtKB-KW xenobiotic metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.2

Peptide

26 – 55

30

Antimicrobial peptide 2

PRO_0000005275

Peptide

26 – 54

29

Antimicrobial peptide 1

PRO_0000005276

Propeptide

56 – 86

31

Removed in mature form

PRO_0000005277

Regions

Domain

29 – 53

25

Chitin-binding type-1

Amino acid modifications

Disulfide bond

29 ↔ 40

Ref.4

Disulfide bond

34 ↔ 46

Ref.4

Disulfide bond

39 ↔ 53

Ref.4

Secondary structure

1

.

.

.

.

.

.

86

Helix Strand Turn

Details...

Beta strand

30 – 32

3

Beta strand

47 – 49

3

Helix

50 – 53

4

Sequences

	Sequence		Length	Mass (Da)
	P27275-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: C2C220E7DF373CB4	FASTA	86	8,912
	10 20 30 40 50 60 MVNMKCVALI VIVMMAFMMV DPSMGVGECV RGRCPSGMCC SQFGYCGKGP KYCGRASTTV 70 80 DHQADVAATK TAKNPTDAKL AGAGSP

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

EMBLGenBankDDBJ

X72641 mRNA. Translation: CAA51210.1.

PIR

S37381.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MMC	NMR	-	A	26-55	[»]
1ZNT	NMR	-	A	26-55	[»]
1ZUV	NMR	-	A	26-55	[»]
1ZWU	NMR	-	A	26-55	[»]

ModBase

Search...

Protein family/group databases

CAZy

CBM18. Carbohydrate-Binding Module Family 18.

Family and domain databases

InterPro

IPR013006. Antimicrobial_peptide_C6_CS.
IPR018371. Chitin-binding_1_CS.
IPR001002. Chitin_bd_1.
IPR000726. Glyco_hydro_19_cat.
[Graphical view]

PANTHER

PTHR22595. Glyco_hydro_19_cat. 1 hit.

Pfam

PF00187. Chitin_bind_1. 1 hit.
[Graphical view]

PRINTS

PR00451. CHITINBINDNG.

ProDom

PD000609. Chitin_binding_1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00270. ChtBD1. 1 hit.
[Graphical view]

PROSITE

PS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. False negative.
PS60011. PLANT_C6_AMP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AMP_AMACA

Accession

Primary (citable) accession number: P27275

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)