ID   AMP3_STEME              Reviewed;          35 AA.
AC   C0HJU5;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Antimicrobial peptide 3 {ECO:0000303|PubMed:26196691};
DE            Short=SmAMP3 {ECO:0000303|PubMed:26196691};
OS   Stellaria media (Common chickweed) (Alsine media).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Alsineae; Stellaria.
OX   NCBI_TaxID=13274 {ECO:0000303|PubMed:26196691};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, PRESENCE OF DISULFIDE
RP   BONDS, AND MASS SPECTROMETRY.
RC   TISSUE=Leaf {ECO:0000303|PubMed:26196691};
RX   PubMed=26196691; DOI=10.1016/j.biochi.2015.07.014;
RA   Rogozhin E.A., Slezina M.P., Slavokhotova A.A., Istomina E.A.,
RA   Korostyleva T.V., Smirnov A.N., Grishin E.V., Egorov T.A., Odintsova T.I.;
RT   "A novel antifungal peptide from leaves of the weed Stellaria media L.";
RL   Biochimie 116:125-132(2015).
CC   -!- FUNCTION: Has antifungal activity against A.niger (IC(50)=5.4 uM),
CC       B.sorokiniana (IC(50)=2.0 uM), B.cinerea (IC(50)=1.6 uM), F.solani
CC       (IC(50)=3.7 uM) and A.alternata (IC(50)=5.0 uM). Binds chitin in vitro.
CC       Has no antibacterial activity at concentrations up to 10 uM.
CC       {ECO:0000269|PubMed:26196691}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaf, flower, stem and seed with
CC       highest expression in leaf (at protein level).
CC       {ECO:0000269|PubMed:26196691}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:26196691}.
CC   -!- MASS SPECTROMETRY: Mass=3364.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:26196691};
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DR   AlphaFoldDB; C0HJU5; -.
DR   SMR; C0HJU5; -.
DR   GO; GO:0008061; F:chitin binding; 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; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Chitin-binding; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Plant defense.
FT   PEPTIDE         1..35
FT                   /note="Antimicrobial peptide 3"
FT                   /id="PRO_0000434197"
FT   DOMAIN          4..35
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        7..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        14..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        19..33
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   35 AA;  3371 MW;  B38BE1DC297F62F5 CRC64;
     VGPGGECGGR FGGCAGGQCC SRFGFCGSGP KYCAH