ID   AMP2_FAGES              Reviewed;          40 AA.
AC   P0DKH8;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Antimicrobial peptide 2;
DE            Short=Fa-AMP2;
OS   Fagopyrum esculentum (Common buckwheat) (Polygonum fagopyrum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Polygonaceae; Polygonoideae; Fagopyreae; Fagopyrum.
OX   NCBI_TaxID=3617;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND LACK
RP   OF GLYCOSYLATION.
RC   TISSUE=Seed;
RX   PubMed=12951494; DOI=10.1271/bbb.67.1636;
RA   Fujimura M., Minami Y., Watanabe K., Tadera K.;
RT   "Purification, characterization, and sequencing of a novel type of
RT   antimicrobial peptides, Fa-AMP1 and Fa-AMP2, from seeds of buckwheat
RT   (Fagopyrum esculentum Moench.).";
RL   Biosci. Biotechnol. Biochem. 67:1636-1642(2003).
CC   -!- FUNCTION: Antimicrobial peptide active against plant pathogenic fungi
CC       and Gram-negative and -positive bacteria.
CC       {ECO:0000269|PubMed:12951494}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:12951494}.
CC   -!- MASS SPECTROMETRY: Mass=3906.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12951494};
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DR   AlphaFoldDB; P0DKH8; -.
DR   SMR; P0DKH8; -.
DR   Allergome; 12014; Fag e 4.
DR   Allergome; 12016; Fag e 4.0102.
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; 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; PS50941; CHIT_BIND_I_2; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Chitin-binding; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Plant defense.
FT   CHAIN           1..40
FT                   /note="Antimicrobial peptide 2"
FT                   /id="PRO_0000431411"
FT   DOMAIN          1..40
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        3..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        12..24
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        17..31
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        35..39
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   40 AA;  3915 MW;  A0190CCA6ECB98C7 CRC64;
     AQCGAQGGGA TCPGGLCCSQ WGWCGSTPKY CGAGCQSNCR