VKT3A_ACTEQ
ID VKT3A_ACTEQ Reviewed; 59 AA.
AC P0DMW6;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=PI-actitoxin-Aeq3a {ECO:0000303|PubMed:22683676};
DE Short=PI-AITX-Aeq3a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Kunitz-type proteinase inhibitor AEPI-I {ECO:0000303|Ref.1};
OS Actinia equina (Beadlet anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Actinia.
OX NCBI_TaxID=6106;
RN [1]
RP PROTEIN SEQUENCE.
RA Ishida M., Minagawa S., Miyauchi K., Shimakura K., Nagashima Y., Shiomi K.;
RT "Amino acid sequences of Kunitz-type protease inhibitors from the sea
RT anemone Actinia equina.";
RL Fish. Sci. 63:794-798(1997).
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: Dual-function toxin that inhibits both the serine protease
CC trypsin and voltage-gated potassium channels (Kv).
CC {ECO:0000250|UniProtKB:B1B5I8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
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; P0DMW6; -.
DR SMR; P0DMW6; -.
DR EnsemblMetazoa; EGACTEQ4350017687-RA; EGACTEQ4350017687-PA; EGACTEQ4350017687.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin 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; Ion channel impairing toxin;
KW Nematocyst; Potassium channel impairing toxin; Protease inhibitor;
KW Secreted; Serine protease inhibitor; Toxin.
FT CHAIN 1..59
FT /note="PI-actitoxin-Aeq3a"
FT /id="PRO_0000433570"
FT DOMAIN 6..56
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 6..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 15..39
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 31..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 59 AA; 6648 MW; 86A1CFC643B58C5D CRC64;
DANSFCQLPA VVGKCRGYFP RYYYNTEAGK CQQFIYGGCG GNRNNFETVE DCRATCHSH