ID   CVP4_PIMHY              Reviewed;         203 AA.
AC   Q8T0W2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Pacifastin-like protease inhibitor cvp4 {ECO:0000303|PubMed:15147757};
DE   AltName: Full=Cysteine-rich venom protein 4 {ECO:0000303|PubMed:15147757};
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:CAD27740.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-25, AND SUBCELLULAR
RP   LOCATION.
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: Inhibits trypsin activity and prophenoloxidase (PPO)
CC       activation, an enzyme essential for both clotting and insect innate
CC       immune responses. It does not inhibit activity of chymotrypsin and
CC       protease K, and has no effect on phenoloxidase (PO) activity.
CC       {ECO:0000250|UniProtKB:A0A7M6UNN1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15147757}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15147757}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I19 family.
CC       {ECO:0000305}.
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; AJ438995; CAD27740.1; -; mRNA.
DR   AlphaFoldDB; Q8T0W2; -.
DR   SMR; Q8T0W2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR008037; Pacifastin_dom.
DR   InterPro; IPR036201; Pacifastin_dom_sf.
DR   InterPro; IPR016307; Prtase-inh_pacifastin.
DR   Pfam; PF05375; Pacifastin_I; 3.
DR   PIRSF; PIRSF001625; Prot_inhib_pacifastin; 1.
DR   SUPFAM; SSF57283; SSF57283; 2.
DR   PROSITE; PS51446; PACIFASTIN; 3.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Repeat;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:15147757"
FT   CHAIN           20..203
FT                   /note="Pacifastin-like protease inhibitor cvp4"
FT                   /evidence="ECO:0000305|PubMed:15147757"
FT                   /id="PRO_0000026713"
FT   DOMAIN          23..59
FT                   /note="Pacifastin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DOMAIN          85..121
FT                   /note="Pacifastin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DOMAIN          147..184
FT                   /note="Pacifastin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   REGION          129..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        26..41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DISULFID        36..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DISULFID        39..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00776"
FT   DISULFID        88..103
FT                   /evidence="ECO:0000250|UniProtKB:O46162"
FT   DISULFID        98..118
FT                   /evidence="ECO:0000250|UniProtKB:O46162"
FT   DISULFID        101..113
FT                   /evidence="ECO:0000250|UniProtKB:O46162"
FT   DISULFID        150..165
FT                   /evidence="ECO:0000250|UniProtKB:O46162"
FT   DISULFID        160..181
FT                   /evidence="ECO:0000250|UniProtKB:O46162"
FT   DISULFID        163..176
FT                   /evidence="ECO:0000250|UniProtKB:O46162"
SQ   SEQUENCE   203 AA;  23077 MW;  9D81C5F5658F0901 CRC64;
     MGFLACALLV VATAHAATAI VNPETCEIGS NFKNYCNNCY CFDGVMDHAL CTRESCDRNV
     WNEDGTRKFP KPGKWISEKE NKKNDEPCTP GENFKYYCND CQCLDGLRAH AMCTRMRCDR
     NVFNEDGTRK YPEPEKWNSE KERKKSDESC APGASFKYYC NSCTCGAEGK VAEAQCTSQE
     CDRYKWKKDG SKRPFTLDPV LHD