DEFI_PHLDU
ID DEFI_PHLDU Reviewed; 98 AA.
AC P83404;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Defensin;
DE Flags: Precursor;
OS Phlebotomus duboscqi (Sandfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC Phlebotomus; Phlebotomus.
OX NCBI_TaxID=37738;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 59-98, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND MASS SPECTROMETRY.
RC STRAIN=Senegal; TISSUE=Hemolymph;
RX PubMed=15557638; DOI=10.1128/iai.72.12.7140-7146.2004;
RA Boulanger N., Lowenberger C., Volf P., Ursic R., Sigutova L., Sabatier L.,
RA Svobodova M., Beverley S.M., Spaeth G., Brun R., Pesson B., Bulet P.;
RT "Characterization of a defensin from the sand fly Phlebotomus duboscqi
RT induced by challenge with bacteria or the protozoan parasite Leishmania
RT major.";
RL Infect. Immun. 72:7140-7146(2004).
CC -!- FUNCTION: Has antiparasitic activity against promastigote forms of
CC L.major, and antibacterial activity against Gram-positive bacterium
CC S.aureus. Has antifungal activity against the yeasts C.albicans and
CC S.cerevisiae, but not C.glabrata. Has antifungal activity against
CC filamentous fungi A.fumigatus, F.culmorum, F.oxysporum, N.crassa,
CC T.viride and T.mentagrophytes, but not B.bassiana.
CC {ECO:0000269|PubMed:15557638}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710,
CC ECO:0000269|PubMed:15557638}.
CC -!- TISSUE SPECIFICITY: Is synthesized by the fat body and eventually
CC secreted into the hemolymph. {ECO:0000269|PubMed:15557638}.
CC -!- INDUCTION: By bacterial and parasitic hemolymph and gut infections.
CC Expression peaks at 24 hours post infection by bacterium P.carotovorum,
CC and at day four post infection by the parasite L.major.
CC {ECO:0000269|PubMed:15557638}.
CC -!- MASS SPECTROMETRY: Mass=4095.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15557638};
CC -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR AlphaFoldDB; P83404; -.
DR SMR; P83404; -.
DR GO; GO:0005576; C:extracellular region; 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; IEA:UniProtKB-KW.
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 Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW Direct protein sequencing; Disulfide bond; Fungicide; Immunity;
KW Innate immunity; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..58
FT /evidence="ECO:0000269|PubMed:15557638"
FT /id="PRO_0000006746"
FT CHAIN 59..98
FT /note="Defensin"
FT /id="PRO_0000006747"
FT DISULFID 61..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
FT DISULFID 74..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
FT DISULFID 78..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
SQ SEQUENCE 98 AA; 10743 MW; 099D68906B1E29C9 CRC64;
MRTFLVTFVL VVVVGVISAY PSNPVEVEAE DFDAQDPDLQ TFQDTFYEVP QVHSRQKRAT
CDLLSAFGVG HAACAAHCIG HGYRGGYCNS KAVCTCRR
