ID   VKT5_ANEVI              Reviewed;          82 AA.
AC   P0DN09;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=U-actitoxin-Avd3h {ECO:0000303|PubMed:22683676};
DE            Short=U-AITX-Avd3h {ECO:0000303|PubMed:22683676};
DE   AltName: Full=AsKC5 {ECO:0000303|PubMed:21281459};
DE   Flags: Precursor;
OS   Anemonia viridis (Snakelocks anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anemonia.
OX   NCBI_TaxID=51769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=19627569; DOI=10.1186/1471-2164-10-333;
RA   Sabourault C., Ganot P., Deleury E., Allemand D., Furla P.;
RT   "Comprehensive EST analysis of the symbiotic sea anemone, Anemonia
RT   viridis.";
RL   BMC Genomics 10:333-333(2009).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=21281459; DOI=10.1186/1471-2164-12-88;
RA   Kozlov S., Grishin E.;
RT   "The mining of toxin-like polypeptides from EST database by single residue
RT   distribution analysis.";
RL   BMC Genomics 12:88-88(2011).
RN   [3]
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)=2800 nM). {ECO:0000250|UniProtKB:Q9TWG0}.
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}.
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   EMBL; FK731360; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FK744399; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FK727999; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FK723059; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DN09; -.
DR   SMR; P0DN09; -.
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   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Nematocyst;
KW   Potassium channel impairing toxin; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000250|UniProtKB:Q9TWG0"
FT   CHAIN           17..75
FT                   /note="U-actitoxin-Avd3h"
FT                   /id="PRO_0000433757"
FT   PROPEP          76..82
FT                   /evidence="ECO:0000305|PubMed:21281459"
FT                   /id="PRO_0000433758"
FT   DOMAIN          21..71
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            31..32
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        21..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        30..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        46..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   82 AA;  9357 MW;  86A413E9E9C29D9D CRC64;
     MVFLLCFFLV ADVSYGINGD CELPKVVGPC RARFPRYYYN SSSKRCEKFI YGGCRGNANN
     FHTLEECEKV CGVRSRDSPK EN