ID   DEFGA_MYTGA             Reviewed;          68 AA.
AC   P00000;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   03-AUG-2022, entry version 6.
DE   RecName: Full=Defensin gallicin {ECO:0000303|PubMed:20508130};
DE   Flags: Precursor;
OS   Mytilus galloprovincialis (Mediterranean mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC   Mytilus.
OX   NCBI_TaxID=29158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=17010391; DOI=10.1016/j.mrfmmm.2006.08.007;
RA   Venier P., De Pitta C., Pallavicini A., Marsano F., Varotto L.,
RA   Romualdi C., Dondero F., Viarengo A., Lanfranchi G.;
RT   "Development of mussel mRNA profiling: Can gene expression trends reveal
RT   coastal water pollution?";
RL   Mutat. Res. 602:121-134(2006).
RN   [2]
RP   FUNCTION, AND BINDING TO LIPID II.
RX   PubMed=20508130; DOI=10.1126/science.1185723;
RA   Schneider T., Kruse T., Wimmer R., Wiedemann I., Sass V., Pag U.,
RA   Jansen A., Nielsen A.K., Mygind P.H., Raventos D.S., Neve S., Ravn B.,
RA   Bonvin A.M., De Maria L., Andersen A.S., Gammelgaard L.K., Sahl H.G.,
RA   Kristensen H.H.;
RT   "Plectasin, a fungal defensin, targets the bacterial cell wall precursor
RT   Lipid II.";
RL   Science 328:1168-1172(2010).
CC   -!- FUNCTION: Shows antibacterial activity against numerous Gram-positive
CC       bacteria (Probable). It selectively inhibits peptidoglycan biosynthesis
CC       through complex formation with the cell wall precursor lipid II (1:1
CC       molar ratio) thus inhibiting cell wall synthesis (PubMed:20508130).
CC       {ECO:0000305|PubMed:20508130}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell membrane
CC       {ECO:0000305|PubMed:20508130}.
CC   -!- TISSUE SPECIFICITY: Expressed in hemolymph, gills, digestive gland,
CC       foot, adductor muscles and mantle. {ECO:0000269|PubMed:17010391}.
CC   -!- PTM: Contains 5 disulfide bonds. {ECO:0000305}.
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DR   EMBL; AJ624472; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P00000; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Defensin; Disulfide bond; Immunity;
KW   Innate immunity; Lipid-binding; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000305"
FT   CHAIN           17..68
FT                   /note="Defensin gallicin"
FT                   /evidence="ECO:0000305|PubMed:20508130"
FT                   /id="PRO_0000449379"
SQ   SEQUENCE   68 AA;  7355 MW;  ACDAEB1EC64158E3 CRC64;
     MWIESDAGVA IDRHARGACS LGEAGCATYC FYQGKHHGGC CGENYTKCLG TCYCNGSGYE
     YRCHSCDL