ID   CTXA2_CERCA             Reviewed;          71 AA.
AC   O17512;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Ceratotoxin-A;
DE   Flags: Precursor;
GN   Name=CTXA2;
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Female accessory gland;
RX   PubMed=9569644; DOI=10.1016/s0965-1748(97)00090-8;
RA   Rosetto M., de Filippis T., Manetti A.G.O., Marchini D., Baldari C.T.,
RA   Dallai R.;
RT   "The genes encoding the antibacterial sex-specific peptides ceratotoxins
RT   are clustered in the genome of the medfly Ceratitis capitata.";
RL   Insect Biochem. Mol. Biol. 27:1039-1046(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 36-64.
RC   TISSUE=Female accessory gland;
RX   PubMed=8353519; DOI=10.1016/0965-1748(93)90032-n;
RA   Marchini D., Giordano P.C., Amons R., Bernini L.F., Dallai R.;
RT   "Purification and primary structure of ceratotoxin A and B, two
RT   antibacterial peptides from the female reproductive accessory glands of the
RT   medfly Ceratitis capitata (Insecta: Diptera).";
RL   Insect Biochem. Mol. Biol. 23:591-598(1993).
CC   -!- FUNCTION: Female-specific peptides with potent activity against Gram-
CC       positive and Gram-negative bacteria. They have as well hemolytic
CC       activity.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable. Still active at 100 degrees Celsius.;
CC   -!- SUBUNIT: Homomer of four to six subunits.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   EMBL; Y15373; CAA75595.1; -; Genomic_DNA.
DR   AlphaFoldDB; O17512; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Cytolysis;
KW   Direct protein sequencing; Hemolysis; Immunity; Innate immunity; Secreted;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..35
FT                   /evidence="ECO:0000269|PubMed:8353519"
FT                   /id="PRO_0000004967"
FT   PEPTIDE         36..64
FT                   /note="Ceratotoxin-A"
FT                   /id="PRO_0000004968"
FT   PROPEP          65..71
FT                   /id="PRO_0000004969"
SQ   SEQUENCE   71 AA;  7199 MW;  FFF40E2FE8F1F27C CRC64;
     MANLKAVFLI CIVAFIAFQC VVAEPAAEDS IVVKRSIGSA LKKALPVAKK IGKIALPIAK
     AALPVAAGLV G