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DEF1_GALME
ID   DEF1_GALME              Reviewed;          72 AA.
AC   P85213; Q6QR79;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Defensin;
DE   AltName: Full=Galiomicin;
DE   Flags: Precursor;
OS   Galleria mellonella (Greater wax moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC   Pyralidae; Galleriinae; Galleria.
OX   NCBI_TaxID=7137;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Larval fat body;
RX   PubMed=14728668; DOI=10.1111/j.1365-2583.2004.00462.x;
RA   Lee Y.S., Yun E.K., Jang W.S., Kim I., Lee J.H., Park S.Y., Ryu K.S.,
RA   Seo S.J., Kim C.H., Lee I.H.;
RT   "Purification, cDNA cloning and expression of an insect defensin from the
RT   great wax moth, Galleria mellonella.";
RL   Insect Mol. Biol. 13:65-72(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 30-72, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, INDUCTION, MASS SPECTROMETRY, AND DISULFIDE BONDS.
RC   TISSUE=Larval hemolymph {ECO:0000269|PubMed:17194500};
RX   PubMed=17194500; DOI=10.1016/j.peptides.2006.11.010;
RA   Cytrynska M., Mak P., Zdybicka-Barabas A., Suder P., Jakubowicz T.;
RT   "Purification and characterization of eight peptides from Galleria
RT   mellonella immune hemolymph.";
RL   Peptides 28:533-546(2007).
RN   [3]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION BY A.NIGER
RP   ALPHA-1,3-GLUCAN.
RX   PubMed=34443685; DOI=10.3390/molecules26165097;
RA   Staczek S., Zdybicka-Barabas A., Wojda I., Wiater A., Mak P., Suder P.,
RA   Skrzypiec K., Cytrynska M.;
RT   "Fungal alpha-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in
RT   the Insect Model Host Galleria mellonella.";
RL   Molecules 26:5097-5097(2021).
CC   -!- FUNCTION: Has antifungal activity against A.niger (MIC=2.1 uM),
CC       C.albicans (MIC=8.5 uM), C.fructus (MIC=8.5 uM), F.oxysporum (MIC=16.9
CC       uM), P.pastoris (MIC=16.9 uM), P.tannophilus (MIC=8.5 uM), T.harzianum
CC       (MIC=4.2 uM), and Z.marxianus (MIC=8.5 uM). Lacks antibacterial
CC       activity against the Gram-positive bacteria L.monocytogenes, M.luteus,
CC       S.aureus, and S.lutea, and the Gram-negative bacteria E.coli D31,
CC       E.coli ATCC 25922, and S.typhimurium. {ECO:0000269|PubMed:17194500}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710,
CC       ECO:0000269|PubMed:14728668, ECO:0000269|PubMed:17194500,
CC       ECO:0000269|PubMed:34443685}. Note=Secreted in the hemolymph.
CC       {ECO:0000269|PubMed:14728668, ECO:0000269|PubMed:17194500,
CC       ECO:0000269|PubMed:34443685}.
CC   -!- TISSUE SPECIFICITY: Hemolymph and midgut. {ECO:0000269|PubMed:14728668,
CC       ECO:0000269|PubMed:17194500}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fat body of last instar larvae.
CC       {ECO:0000269|PubMed:34443685}.
CC   -!- INDUCTION: By bacterial infection (PubMed:17194500). Induced by A.niger
CC       alpha-1,3-glucan (PubMed:34443685). {ECO:0000269|PubMed:17194500,
CC       ECO:0000269|PubMed:34443685}.
CC   -!- MASS SPECTROMETRY: Mass=4716.75; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:14728668};
CC   -!- MASS SPECTROMETRY: Mass=4714.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17194500};
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 2
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR   EMBL; AY528421; AAS19170.1; -; mRNA.
DR   AlphaFoldDB; P85213; -.
DR   SMR; P85213; -.
DR   Proteomes; UP000504614; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   CDD; cd00107; Knot1; 1.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Defensin; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Immunity; Innate immunity; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:14728668,
FT                   ECO:0000269|PubMed:17194500"
FT   CHAIN           30..72
FT                   /note="Defensin"
FT                   /id="PRO_0000298768"
FT   DISULFID        36..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:17194500"
FT   DISULFID        47..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:17194500"
FT   DISULFID        51..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:17194500"
FT   CONFLICT        35
FT                   /note="S -> R (in Ref. 1; AAS19170)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   72 AA;  7823 MW;  707D4A4D34034E85 CRC64;
     MAKNFQSVLL LVCLSFLVIV SSPQNAVQAD TLIGSCVWGA TNYTSDCNAE CKRRGYKGGH
     CGSFLNVNCW CE
 
 
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