DEF2_GALME
ID DEF2_GALME Reviewed; 44 AA.
AC P85215;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Defensin-like peptide;
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] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP 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).
CC -!- FUNCTION: Has antibacterial activity against the Gram-positive
CC bacterium S.lutea (MIC=1.9 uM). Lacks antibacterial activity against
CC the Gram-positive bacteria L.monocytogenes and M.luteus, and the Gram-
CC negative bacteria E.coli D31, E.coli ATCC 25922, and S.typhimurium. Has
CC antifungal activity against A.niger (MIC=2.9 uM), C.albicans (MIC=2.9
CC uM), C.fructus (MIC=2.9 uM), C.wickerhamii (MIC=2.9 uM), P.pastoris
CC (MIC=2.9 uM), P.stiptis (MIC=2.9 uM), P.tannophilus (MIC=2.9 uM),
CC T.harzianum (MIC=2.9 uM), and Z.marxianus (MIC=2.9 uM), but lacks
CC antifungal activity against C.albidus, F.oxysporum, and S.cerevisiae.
CC {ECO:0000269|PubMed:17194500}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710,
CC ECO:0000269|PubMed:17194500}.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:17194500}.
CC -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:17194500}.
CC -!- MASS SPECTROMETRY: Mass=4943.9; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P85215; -.
DR SMR; P85215; -.
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:0050830; P:defense response to Gram-positive bacterium; 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 Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR001542; Defensin_invertebrate/fungal.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR Pfam; PF01097; Defensin_2; 1.
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.
FT CHAIN 1..44
FT /note="Defensin-like peptide"
FT /id="PRO_0000298769"
FT DISULFID 7..32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT ECO:0000269|PubMed:17194500"
FT DISULFID 18..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT ECO:0000269|PubMed:17194500"
FT DISULFID 22..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT ECO:0000269|PubMed:17194500"
SQ SEQUENCE 44 AA; 4949 MW; 3C55F2DD3376FCD5 CRC64;
DKLIGSCVWG ATNYTSDCNA ECKRRGYKGG HCGSFWNVNC WCEE
