VKT3_ANESU
ID VKT3_ANESU Reviewed; 59 AA.
AC Q9TWF8;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=KappaPI-actitoxin-Avd3d {ECO:0000303|PubMed:22683676};
DE Short=KappaPI-AITX-Avd3d {ECO:0000303|PubMed:22683676};
DE AltName: Full=Kalicludine-3 {ECO:0000303|PubMed:7559645};
DE Short=AsKC3 {ECO:0000303|PubMed:7559645};
OS Anemonia sulcata (Mediterranean snakelocks sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Anemonia.
OX NCBI_TaxID=6108;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=7559645; DOI=10.1074/jbc.270.42.25121;
RA Schweitz H., Bruhn T., Guillemare E., Moinier D., Lancelin J.-M.,
RA Beress L., Lazdunski M.;
RT "Kalicludines and kaliseptine. Two different classes of sea anemone toxins
RT for voltage sensitive K+ channels.";
RL J. Biol. Chem. 270:25121-25126(1995).
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 (Kd<30 nM) and voltage-gated potassium channels Kv1.2/KCNA2
CC (IC(50)=1300 nM). {ECO:0000269|PubMed:7559645}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:7559645}. Nematocyst
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2
CC potassium channel toxin subfamily. {ECO:0000305}.
CC -!- CAUTION: Opinions are divided on whether Anemonia viridis (Forsskal,
CC 1775) and Anemonia sulcata (Pennant, 1777) are separate species.
CC {ECO:0000305}.
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DR AlphaFoldDB; Q9TWF8; -.
DR SMR; Q9TWF8; -.
DR TCDB; 8.B.13.1.1; the sea anemone peptide toxin class 2 (kalicludine) family.
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;
KW Voltage-gated potassium channel impairing toxin.
FT CHAIN 1..59
FT /note="KappaPI-actitoxin-Avd3d"
FT /evidence="ECO:0000269|PubMed:7559645"
FT /id="PRO_0000155414"
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|UniProtKB:P31713"
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 59 AA; 6738 MW; 0C7695C3F394D4A5 CRC64;
INGDCELPKV VGRCRARFPR YYYNLSSRRC EKFIYGGCGG NANNFHTLEE CEKVCGVRS
