DEF_GLOMM
ID DEF_GLOMM Reviewed; 87 AA.
AC Q8WTD4;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Defensin-A {ECO:0000303|PubMed:11592981, ECO:0000303|PubMed:11886771};
DE Short=DefA {ECO:0000312|EMBL:AAL34112.1};
DE Short=GmDefA {ECO:0000303|PubMed:11592981};
DE Flags: Precursor;
OS Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL34112.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=11592981; DOI=10.1073/pnas.221363798;
RA Hao Z., Kasumba I., Lehane M.J., Gibson W.C., Kwon J., Aksoy S.;
RT "Tsetse immune responses and trypanosome transmission: implications for the
RT development of tsetse-based strategies to reduce trypanosomiasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12648-12653(2001).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 45-87, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND MASS SPECTROMETRY.
RC TISSUE=Hemolymph {ECO:0000269|PubMed:11886771};
RX PubMed=11886771; DOI=10.1016/s0965-1748(02)00029-2;
RA Boulanger N., Brun R., Ehret-Sabatier L., Kunz C., Bulet P.;
RT "Immunopeptides in the defense reactions of Glossina morsitans to bacterial
RT and Trypanosoma brucei brucei infections.";
RL Insect Biochem. Mol. Biol. 32:369-375(2002).
CC -!- FUNCTION: Antibacterial peptide mostly active against Gram-positive and
CC Gram negative bacteria. {ECO:0000269|PubMed:11592981,
CC ECO:0000269|PubMed:11886771}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710,
CC ECO:0000269|PubMed:11592981, ECO:0000269|PubMed:11886771}.
CC -!- TISSUE SPECIFICITY: Hemolymph and fat body.
CC {ECO:0000269|PubMed:11592981, ECO:0000269|PubMed:11886771}.
CC -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:11592981,
CC ECO:0000269|PubMed:11886771}.
CC -!- MASS SPECTROMETRY: Mass=3596.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11886771};
CC -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR EMBL; AF368907; AAL34112.1; -; mRNA.
DR AlphaFoldDB; Q8WTD4; -.
DR SMR; Q8WTD4; -.
DR Proteomes; UP000092444; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; 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 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 PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Defensin; Direct protein sequencing;
KW Disulfide bond; Immunity; Innate immunity; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..44
FT /evidence="ECO:0000255, ECO:0000269|PubMed:11886771"
FT /id="PRO_0000386437"
FT CHAIN 45..87
FT /note="Defensin-A"
FT /evidence="ECO:0000269|PubMed:11886771"
FT /id="PRO_0000386438"
FT DISULFID 57..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
FT DISULFID 64..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
FT DISULFID 68..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710"
SQ SEQUENCE 87 AA; 9592 MW; C160DF6FAC8E5413 CRC64;
MKFYLVLAFL TLCAVAVTAL PAGDETRIDL ETLEEDLRLV DGAQVTGELK RDKRVTCNIG
EWVCVAHCNS KSKKSGYCSR GVCYCTN
