ID   AMP_LYMAR               Reviewed;          44 AA.
AC   P86521;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 2.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Antimicrobial peptide 1b {ECO:0000303|PubMed:21434417};
DE            Short=LAMP-1b {ECO:0000303|PubMed:21434417};
DE   Contains:
DE     RecName: Full=Antimicrobial peptide 1a {ECO:0000303|PubMed:21434417};
DE              Short=LAMP-1a {ECO:0000303|PubMed:21434417};
OS   Leymus arenarius (Lyme grass) (Elymus arenarius).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Leymus.
OX   NCBI_TaxID=220462 {ECO:0000303|PubMed:21434417};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION OF ANTIMICROBIAL PEPTIDE 1A, MASS SPECTROMETRY,
RP   AND PRESENCE OF DISULFIDE BONDS.
RC   TISSUE=Seed {ECO:0000303|PubMed:21434417};
RX   PubMed=21434417;
RA   Utkina L.L., Zhabon E.O., Slavokhotova A.A., Rogozhin E.A., Shiian A.N.,
RA   Grishin E.V., Egorov T.A., Odintsova T.I., Pukhal'skii V.A.;
RT   "[Heterologous expression of a synthetic gene encoding a novel hevein-type
RT   antimicrobial peptide of Leymus arenarius in Escherichia coli cells].";
RL   Genetika 46:1645-1651(2010).
CC   -!- FUNCTION: [Antimicrobial peptide 1a]: Binds chitin (By similarity). Has
CC       antifungal activity against F.oxysporum 16/10 (IC(50)=4.1 uM) and
CC       B.sorokiniana 6/10 (IC(50)=2.7 uM) (PubMed:21434417). Inhibits
CC       germination of fungal spores (PubMed:21434417).
CC       {ECO:0000250|UniProtKB:P85966, ECO:0000269|PubMed:21434417}.
CC   -!- PTM: Contains 5 disulfide bonds. {ECO:0000269|PubMed:21434417}.
CC   -!- MASS SPECTROMETRY: [Antimicrobial peptide 1a]: Mass=4444.0;
CC       Method=MALDI; Note=Antimicrobial peptide 1a.;
CC       Evidence={ECO:0000269|PubMed:21434417};
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DR   AlphaFoldDB; P86521; -.
DR   SMR; P86521; -.
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; IPR001002; Chitin-bd_1.
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; PS50941; CHIT_BIND_I_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Chitin-binding; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Plant defense.
FT   PEPTIDE         1..44
FT                   /note="Antimicrobial peptide 1b"
FT                   /evidence="ECO:0000269|PubMed:21434417"
FT                   /id="PRO_0000445024"
FT   PEPTIDE         1..43
FT                   /note="Antimicrobial peptide 1a"
FT                   /evidence="ECO:0000269|PubMed:21434417"
FT                   /id="PRO_0000394409"
FT   DOMAIN          1..42
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        4..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        13..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        16..43
FT                   /evidence="ECO:0000250|UniProtKB:P85966"
FT   DISULFID        18..32
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        36..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   44 AA;  4612 MW;  2313DC1434B0DBAA CRC64;
     AQKCGEQGRG AKCPNCLCCG RYGFCGSTPD YCGVGCQSQC RGCR