CTXB_CERCA
ID CTXB_CERCA Reviewed; 29 AA.
AC P36191;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Ceratotoxin-B;
GN Name=CTXB;
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 PROTEIN SEQUENCE.
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 PIR; B61613; B61613.
DR AlphaFoldDB; P36191; -.
DR TCDB; 1.C.52.2.2; the dermaseptin (dermaseptin) family.
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; Cytolysis; Direct protein sequencing; Hemolysis;
KW Immunity; Innate immunity; Secreted.
FT PEPTIDE 1..29
FT /note="Ceratotoxin-B"
FT /id="PRO_0000043593"
SQ SEQUENCE 29 AA; 2861 MW; EE57F4EECB2DA6B0 CRC64;
SIGSAFKKAL PVAKKIGKAA LPIAKAALP