ID   VN46_COTRU              Reviewed;          65 AA.
AC   Q8WQK0;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Venom protein Vn4.6;
DE   Flags: Precursor;
OS   Cotesia rubecula (Cabbage white butterfly parasite) (Apanteles rubecula).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Parasitoida;
OC   Ichneumonoidea; Braconidae; Microgastrinae; Cotesia.
OX   NCBI_TaxID=32392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-59, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=12761876; DOI=10.1002/arch.10088;
RA   Asgari S., Zareie R., Zhang G., Schmidt O.;
RT   "Isolation and characterization of a novel venom protein from an
RT   endoparasitoid, Cotesia rubecula (Hym: Braconidae).";
RL   Arch. Insect Biochem. Physiol. 53:92-100(2003).
CC   -!- FUNCTION: Endoparasitoid venom protein that interferes with the
CC       activation of host hemolymph prophenoloxidase. May act in conjunction
CC       with other venom proteins (such as Vn50), by competitive binding to the
CC       zymogen and thereby interrupting the enzyme.
CC       {ECO:0000269|PubMed:12761876}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12761876}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:12761876}.
CC   -!- PTM: Contains 2 disulfide bonds.
CC   -!- MASS SPECTROMETRY: Mass=4653.9; Method=Electrospray; Note=Oxidized
CC       mass.; Evidence={ECO:0000269|PubMed:12761876};
CC   -!- MASS SPECTROMETRY: Mass=4670.5; Method=Electrospray; Note=Reduced
CC       mass.; Evidence={ECO:0000269|PubMed:12761876};
CC   -!- MISCELLANEOUS: This species is an endoparasitoid, that contain
CC       symbiotic polydnaviruses (PDV) in its genome. PDVs, used to overcome
CC       the host defenses, are introduced into the body of the host larva at
CC       oviposition by the female wasp and have been shown to be essential for
CC       successful parasitism and development of the parasitoid inside the
CC       host. Interestingly, the coding region for Vn4.6 is located in the
CC       opposite direction upstream of a gene coding for a C.rubecula PDV
CC       structural protein (Crp32).
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DR   EMBL; AY069984; AAL58518.2; -; mRNA.
DR   AlphaFoldDB; Q8WQK0; -.
DR   SMR; Q8WQK0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0010466; P:negative regulation of peptidase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:12761876"
FT   CHAIN           24..65
FT                   /note="Venom protein Vn4.6"
FT                   /id="PRO_0000401919"
SQ   SEQUENCE   65 AA;  7133 MW;  1787D09A05F6037B CRC64;
     MSKIILAIFL IVLCGLIFVT VDAMIDAPCK DNDDCDRFTE YCAIYADENG NEAGKRCEDA
     IGLLV