ID   AMP_IPONI               Reviewed;          41 AA.
AC   P81591;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Antimicrobial protein PN-AMP1;
DE   Contains:
DE     RecName: Full=Antimicrobial protein PN-AMP2;
OS   Ipomoea nil (Japanese morning glory) (Pharbitis nil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=35883;
RN   [1]
RP   PROTEIN SEQUENCE, CHARACTERIZATION, PYROGLUTAMATE FORMATION AT GLN-1, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Seed;
RX   PubMed=9507071; DOI=10.1016/s0167-4838(97)00148-9;
RA   Koo J.C., Lee S.Y., Chun H.J., Cheong Y.H., Choi J.S., Kawabata S.,
RA   Miyagi M., Tsunasawa S., Ha K.S., Bae D.W., Han C.-D., Lee B.L., Cho M.J.;
RT   "Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit
RT   potent antifungal activity.";
RL   Biochim. Biophys. Acta 1382:80-90(1998).
CC   -!- FUNCTION: Chitin-binding protein with a defensive function against
CC       numerous chitin containing fungal pathogens. It is also an inhibitor of
CC       Gram-positive bacteria such as B.subtilis.
CC   -!- MASS SPECTROMETRY: [Antimicrobial protein PN-AMP1]: Mass=4299.72;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:9507071};
CC   -!- MASS SPECTROMETRY: [Antimicrobial protein PN-AMP2]: Mass=4213.17;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:9507071};
CC   -!- MISCELLANEOUS: Its antimicrobial activity is strongly inhibited by
CC       divalent cations.
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DR   AlphaFoldDB; P81591; -.
DR   SMR; P81591; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
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; Pyrrolidone carboxylic acid.
FT   CHAIN           1..41
FT                   /note="Antimicrobial protein PN-AMP1"
FT                   /id="PRO_0000005278"
FT   CHAIN           1..40
FT                   /note="Antimicrobial protein PN-AMP2"
FT                   /id="PRO_0000005279"
FT   DOMAIN          1..41
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:9507071"
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   41 AA;  4326 MW;  326C9E2DA00724DB CRC64;
     QQCGRQASGR LCGNRLCCSQ WGYCGSTASY CGAGCQSQCR S