CF4_COTFL
ID CF4_COTFL Reviewed; 54 AA.
AC P0DQT4;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=H-bracotoxin-Cf4 {ECO:0000303|PubMed:34547307};
DE Short=H-BCTX-Cf4 {ECO:0000303|PubMed:34547307};
DE Flags: Precursor;
OS Cotesia flavipes (Parasitic wasp) (Apanteles flavipes).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Parasitoida;
OC Ichneumonoidea; Braconidae; Microgastrinae; Cotesia.
OX NCBI_TaxID=89805;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SYNTHESIS OF 22-54, AND
RP BIOTECHNOLOGY.
RX PubMed=34547307; DOI=10.1016/j.toxicon.2021.09.002;
RA Pinto C.P.G., Walker A.A., Robinson S.D., Chin Y.K., King G.F., Rossi G.D.;
RT "Venom composition of the endoparasitoid wasp Cotesia flavipes
RT (Hymenoptera: Braconidae) and functional characterization of a major venom
RT peptide.";
RL Toxicon 202:1-12(2021).
CC -!- FUNCTION: This endoparasitoid wasp peptide has a role in disruption of
CC the cellular host immune response, since it reduces the capacity of
CC D.saccharalis hemocytes to encapsulate foreign bodies. On the other
CC hand, it shows no effect on the humoral immune response, since it has
CC no effect on phenoloxidase activity. {ECO:0000269|PubMed:34547307}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:34547307}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:34547307}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- BIOTECHNOLOGY: Potential candidate for insect pest control through
CC ingestion. Feeding leaves coated with this peptide to neonate
CC D.saccharalis result in increased mortality and significantly reduced
CC feeding compared to caterpillars fed untreated leaves.
CC {ECO:0000269|PubMed:34547307}.
CC -!- MISCELLANEOUS: Highly abundant in venom. {ECO:0000269|PubMed:34547307}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MZ442218; UEP64248.1; -; mRNA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Disulfide bond; Knottin; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..54
FT /note="H-bracotoxin-Cf4"
FT /evidence="ECO:0000305|PubMed:34547307"
FT /id="PRO_0000455164"
FT DISULFID 24..39
FT /evidence="ECO:0000305|PubMed:34547307"
FT DISULFID 31..43
FT /evidence="ECO:0000305|PubMed:34547307"
FT DISULFID 38..53
FT /evidence="ECO:0000305|PubMed:34547307"
SQ SEQUENCE 54 AA; 5740 MW; DCD722E26EF8FC68 CRC64;
MSKLFIFFLL VALLAFVSSE AAECVAKGQN CIVGKSTCCI GQCIIKDHVL GSCE