ID   VKT2_PIMHY              Reviewed;          77 AA.
AC   Q8T0W4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Kunitz-type serine protease inhibitor cvp2;
DE   AltName: Full=Cysteine-rich venom protein 2;
DE            Short=cvp2;
DE   Flags: Precursor;
OS   Pimpla hypochondriaca (Parasitoid wasp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Parasitoida;
OC   Ichneumonoidea; Ichneumonidae; Pimplinae; Pimplini; Pimpla.
OX   NCBI_TaxID=135724;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAD27738.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-29.
RC   TISSUE=Venom {ECO:0000269|PubMed:15147757}, and
RC   Venom gland {ECO:0000269|PubMed:15147757};
RX   PubMed=15147757; DOI=10.1016/j.ibmb.2004.03.003;
RA   Parkinson N.M., Conyers C., Keen J., MacNicoll A., Smith I., Audsley N.,
RA   Weaver R.;
RT   "Towards a comprehensive view of the primary structure of venom proteins
RT   from the parasitoid wasp Pimpla hypochondriaca.";
RL   Insect Biochem. Mol. Biol. 34:565-571(2004).
CC   -!- FUNCTION: Serine protease inhibitor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15147757}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:15147757}.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR   EMBL; AJ438993; CAD27738.1; -; mRNA.
DR   AlphaFoldDB; Q8T0W4; -.
DR   SMR; Q8T0W4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00109; KU; 1.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:15147757"
FT   CHAIN           24..77
FT                   /note="Kunitz-type serine protease inhibitor cvp2"
FT                   /id="PRO_0000016860"
FT   DOMAIN          28..76
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            35..36
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        28..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        37..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        51..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   77 AA;  7873 MW;  FF40C07F3C7E0D75 CRC64;
     MNAKIVALLI VVGFVGMFNV ATAADPLCSL EPAVGLCKAS IPRFASVGGK CQEFIYGGCG
     GNANNFQTQA ECEAKCG