ID VKTI1_ANTFU Reviewed; 56 AA.
AC P0DMJ3;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=PI-actitoxin-Afv2a {ECO:0000303|PubMed:22683676};
DE Short=PI-AITX-Afv2a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Kunitz-type protease inhibitor AFAPI-I {ECO:0000303|PubMed:18450492};
OS Anthopleura fuscoviridis (Sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Anthopleura.
OX NCBI_TaxID=6111;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Tentacle;
RX PubMed=18450492; DOI=10.1016/j.cbpb.2008.03.010;
RA Minagawa S., Sugiyama M., Ishida M., Nagashima Y., Shiomi K.;
RT "Kunitz-type protease inhibitors from acrorhagi of three species of sea
RT anemones.";
RL Comp. Biochem. Physiol. 150B:240-245(2008).
RN [2]
RP NOMENCLATURE.
RX PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA Oliveira J.S., Fuentes-Silva D., King G.F.;
RT "Development of a rational nomenclature for naming peptide and protein
RT toxins from sea anemones.";
RL Toxicon 60:539-550(2012).
CC -!- FUNCTION: Serine protease inhibitor that is strongly active against
CC trypsin (950 IU/mg) and moderately active against plasmin.
CC {ECO:0000269|PubMed:18450492}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by acrorhagi.
CC {ECO:0000269|PubMed:18450492}.
CC -!- MISCELLANEOUS: Does not inhibit potassium channels (Kv), as well as
CC metalloproteases, and cysteine proteases (papain and bromelain).
CC {ECO:0000305|PubMed:18450492}.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2
CC potassium channel toxin subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DMJ3; -.
DR SMR; P0DMJ3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; BPTI-like; 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; Nematocyst; Protease inhibitor;
KW Secreted; Serine protease inhibitor.
FT CHAIN 1..56
FT /note="PI-actitoxin-Afv2a"
FT /evidence="ECO:0000269|PubMed:18450492"
FT /id="PRO_0000429350"
FT DOMAIN 5..55
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 15..16
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250"
FT DISULFID 5..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 14..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 30..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 56 AA; 6097 MW; C3616D2DC44CE26A CRC64;
VPANCLLPMK VGFCRAHVPR FYYNSSSGKC EGFTYGGCGA NANNFQTKAQ CEKACR
//
