ID   AMP_AMACA               Reviewed;          86 AA.
AC   P27275;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Antimicrobial peptide 2;
DE            Short=AMP2;
DE   Contains:
DE     RecName: Full=Antimicrobial peptide 1;
DE              Short=AMP1;
DE   Flags: Precursor;
OS   Amaranthus caudatus (Love-lies-bleeding) (Inca-wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Amaranthaceae; Amaranthus.
OX   NCBI_TaxID=3567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=8400136; DOI=10.1007/bf00028991;
RA   de Bolle M.F.C., David K.M.M., Rees S.B., Vanderleyden J., Cammue B.P.A.,
RA   Broekaert W.F.;
RT   "Cloning and characterization of a cDNA encoding an antimicrobial chitin-
RT   binding protein from amaranth, Amaranthus caudatus.";
RL   Plant Mol. Biol. 22:1187-1190(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 26-55.
RC   TISSUE=Seed;
RX   PubMed=1567877; DOI=10.1021/bi00132a023;
RA   Broekaert W.F., Marien W., Terras F.R.G., de Bolle M.F.C., Proost P.,
RA   van Damme J., Dillen L., Claeys M., Rees S.B., Vanderleyden J.,
RA   Cammue B.P.A.;
RT   "Antimicrobial peptides from Amaranthus caudatus seeds with sequence
RT   homology to the cysteine/glycine-rich domain of chitin-binding proteins.";
RL   Biochemistry 31:4308-4314(1992).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=8627629; DOI=10.1006/jmbi.1996.0253;
RA   Martins J.C., Maes D., Loris R., Pepermans H.A.M., Wyns L., Willem R.,
RA   Verheyden P.;
RT   "H NMR study of the solution structure of Ac-AMP2, a sugar binding
RT   antimicrobial protein isolated from Amaranthus caudatus.";
RL   J. Mol. Biol. 258:322-333(1996).
RN   [4]
RP   DISULFIDE BONDS.
RX   PubMed=9176817; DOI=10.1111/j.1399-3011.1997.tb01134.x;
RA   el Boiyoussfi M., Laus G., Verheyden P., Wyns L., Tourwe D., van Binst G.;
RT   "Location of the three disulfide bonds in an antimicrobial peptide from
RT   Amaranthus caudatus using mass spectrometry.";
RL   J. Pept. Res. 49:336-340(1997).
CC   -!- FUNCTION: Chitin-binding protein with a defensive function against
CC       numerous chitin containing fungal pathogens. It is also a potent
CC       inhibitor of Gram-positive bacteria.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Its chitin-binding activity is strongly inhibited by
CC       divalent cations.
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DR   EMBL; X72641; CAA51210.1; -; mRNA.
DR   PIR; S37381; S37381.
DR   PDB; 1MMC; NMR; -; A=26-55.
DR   PDB; 1ZNT; NMR; -; A=26-55.
DR   PDB; 1ZUV; NMR; -; A=26-55.
DR   PDB; 1ZWU; NMR; -; A=26-55.
DR   PDBsum; 1MMC; -.
DR   PDBsum; 1ZNT; -.
DR   PDBsum; 1ZUV; -.
DR   PDBsum; 1ZWU; -.
DR   AlphaFoldDB; P27275; -.
DR   BMRB; P27275; -.
DR   SMR; P27275; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   UniLectin; P27275; -.
DR   EvolutionaryTrace; P27275; -.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR013006; Antimicrobial_C6_CS.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS60011; PLANT_C6_AMP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Chitin-binding;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Plant defense;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:1567877"
FT   PEPTIDE         26..55
FT                   /note="Antimicrobial peptide 2"
FT                   /id="PRO_0000005275"
FT   PEPTIDE         26..54
FT                   /note="Antimicrobial peptide 1"
FT                   /id="PRO_0000005276"
FT   PROPEP          56..86
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000005277"
FT   DOMAIN          29..53
FT                   /note="Chitin-binding type-1"
FT   DISULFID        29..40
FT                   /evidence="ECO:0000269|PubMed:9176817"
FT   DISULFID        34..46
FT                   /evidence="ECO:0000269|PubMed:9176817"
FT   DISULFID        39..53
FT                   /evidence="ECO:0000269|PubMed:9176817"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:1MMC"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:1MMC"
FT   HELIX           50..53
FT                   /evidence="ECO:0007829|PDB:1MMC"
SQ   SEQUENCE   86 AA;  8912 MW;  C2C220E7DF373CB4 CRC64;
     MVNMKCVALI VIVMMAFMMV DPSMGVGECV RGRCPSGMCC SQFGYCGKGP KYCGRASTTV
     DHQADVAATK TAKNPTDAKL AGAGSP