ID   ATTA_GLOMM              Reviewed;         208 AA.
AC   Q8WTD3;
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=Attacin-A {ECO:0000303|PubMed:11592981, ECO:0000303|PubMed:11886771};
DE            Short=AttA {ECO:0000312|EMBL:AAL34113.1};
DE            Short=GmAttA {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:AAL34113.1}
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 48-69, 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: Hemolymph antibacterial protein against Gram-negative
CC       bacteria. {ECO:0000269|PubMed:11592981, ECO:0000269|PubMed:11886771}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11592981,
CC       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=19342.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11886771};
CC   -!- SIMILARITY: Belongs to the attacin/sarcotoxin-2 family. {ECO:0000255}.
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DR   EMBL; AF368909; AAL34113.1; -; mRNA.
DR   AlphaFoldDB; Q8WTD3; -.
DR   STRING; 37546.Q8WTD3; -.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR005521; Attacin_C.
DR   InterPro; IPR005520; Attacin_N.
DR   Pfam; PF03769; Attacin_C; 1.
DR   Pfam; PF03768; Attacin_N; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Immunity;
KW   Innate immunity; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..47
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:11886771"
FT                   /id="PRO_0000386435"
FT   CHAIN           48..208
FT                   /note="Attacin-A"
FT                   /evidence="ECO:0000269|PubMed:11886771"
FT                   /id="PRO_0000386436"
SQ   SEQUENCE   208 AA;  21754 MW;  1D0BB1D7CA04B47F CRC64;
     MQSFKICFFI SCLSVVLVKG QFGGTVSSNP NGGLDVNARL SKTIGDPNAN VVGGVFAAGN
     TDGGPATRGA FLAANKDGHG LSLQHSKTDN FGSSLTSSAH AHLFNDKTHK LDANAFHSRT
     HLDNGFKFDR VGGGLRYDHV TGHGASLTAS RIPQLDMNTL GLTGKANLWS SPNRATTLDL
     TGGVSKHFGG PFDGQTNKQI GLGLNSRF