ID   DEFI_PROTE              Reviewed;          94 AA.
AC   P10891;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Phormicin;
DE   AltName: Full=Insect defensin A/B;
DE   Flags: Precursor;
OS   Protophormia terraenovae (Northern blowfly) (Lucilia terraenovae).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Chrysomyinae; Protophormia.
OX   NCBI_TaxID=34676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2369900; DOI=10.1002/j.1460-2075.1990.tb07430.x;
RA   Dimarcq J.-L., Zachary D., Hoffmann J.A., Hoffmann D., Reichhart J.-M.;
RT   "Insect immunity: expression of the two major inducible antibacterial
RT   peptides, defensin and diptericin, in Phormia terranovae.";
RL   EMBO J. 9:2507-2515(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 55-94.
RC   TISSUE=Hemolymph;
RX   PubMed=2911573; DOI=10.1073/pnas.86.1.262;
RA   Lambert J., Keppi E., Dimarcq J.-L., Wicker C., Reichhart J.-M., Dunbar B.,
RA   Lepage P., van Dorsselaer A., Hoffmann J.A., Fothergill J., Hoffmann D.;
RT   "Insect immunity: isolation from immune blood of the dipteran Phormia
RT   terranovae of two insect antibacterial peptides with sequence homology to
RT   rabbit lung macrophage bactericidal peptides.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:262-266(1989).
RN   [3]
RP   DISULFIDE BONDS.
RX   PubMed=2013293; DOI=10.1111/j.1432-1033.1991.tb15872.x;
RA   Lepage P., Bitsch F., Roecklin D., Keppi E., Dimarcq J.-L.,
RA   Reichhart J.-M., Hoffmann J.A., Roitsch C., van Dorsselaer A.;
RT   "Determination of disulfide bridges in natural and recombinant insect
RT   defensin A.";
RL   Eur. J. Biochem. 196:735-742(1991).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=1467342; DOI=10.1016/0300-9084(92)90065-m;
RA   Bonmatin J.-M., Genest M., Petit M.-C., Gincel E., Simorre J.-P.,
RA   Cornet B., Gallet X., Caille A., Labbe H., Vovelle F., Ptak M.;
RT   "Progress in multidimensional NMR investigations of peptide and protein 3-D
RT   structures in solution. From structure to functional aspects.";
RL   Biochimie 74:825-836(1992).
RN   [5]
RP   STRUCTURE BY NMR OF 55-94.
RX   PubMed=7663941; DOI=10.1016/s0969-2126(01)00177-0;
RA   Cornet B., Bonmatin J.-M., Hetru C., Hoffmann J.A., Ptak M., Vovelle F.;
RT   "Refined three-dimensional solution structure of insect defensin A.";
RL   Structure 3:435-448(1995).
CC   -!- FUNCTION: Responsible for the anti Gram-positive activity of immune
CC       hemolymph of P.terraenovae.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR   EMBL; X55546; CAA39152.1; -; mRNA.
DR   PIR; S12558; S12558.
DR   PDB; 1ICA; NMR; -; A=55-94.
DR   PDBsum; 1ICA; -.
DR   AlphaFoldDB; P10891; -.
DR   BMRB; P10891; -.
DR   SMR; P10891; -.
DR   TCDB; 1.C.47.1.2; the insect/fungal defensin (insect/fungal defensin) family.
DR   EvolutionaryTrace; P10891; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:UniProt.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR017982; Defensin_insect.
DR   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   Pfam; PF01097; Defensin_2; 1.
DR   PRINTS; PR00271; DEFENSIN.
DR   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Defensin; Direct protein sequencing;
KW   Disulfide bond; Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..54
FT                   /evidence="ECO:0000269|PubMed:2911573"
FT                   /id="PRO_0000006748"
FT   CHAIN           55..94
FT                   /note="Phormicin"
FT                   /id="PRO_0000006749"
FT   DISULFID        57..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:2013293"
FT   DISULFID        70..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:2013293"
FT   DISULFID        74..92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:2013293"
FT   VARIANT         86
FT                   /note="G -> R (in defensin B)"
FT   HELIX           68..77
FT                   /evidence="ECO:0007829|PDB:1ICA"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:1ICA"
SQ   SEQUENCE   94 AA;  10110 MW;  CE24ED83D7CBE6D9 CRC64;
     MKFFMVFVVT FCLAVCFVSQ SLAIPADAAN DAHFVDGVQA LKEIEPELHG RYKRATCDLL
     SGTGINHSAC AAHCLLRGNR GGYCNGKGVC VCRN