VKT53_ANEVI
ID VKT53_ANEVI Reviewed; 82 AA.
AC P0DN08;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=KappaPI-actitoxin-Avd3e {ECO:0000303|PubMed:22683676};
DE Short=KappaPI-AITX-Avd3e {ECO:0000303|PubMed:22683676};
DE AltName: Full=Proteinase inhibitor 5 III {ECO:0000303|PubMed:21281459};
DE Short=SA5 III {ECO:0000303|PubMed:22683676};
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: Serine protease inhibitor that inhibits both tissue and
CC plasma kallikreins. Has hemolytic activity. Inhibits voltage-gated
CC potassium channels (Kv). {ECO:0000250|UniProtKB:P10280,
CC ECO:0000250|UniProtKB:Q9TWF8}.
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; FK749713; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; FK721810; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DN08; -.
DR SMR; P0DN08; -.
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; 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; Nematocyst; Protease inhibitor; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250|UniProtKB:P10280"
FT CHAIN 17..75
FT /note="KappaPI-actitoxin-Avd3e"
FT /id="PRO_0000433755"
FT PROPEP 76..82
FT /evidence="ECO:0000305|PubMed:21281459"
FT /id="PRO_0000433756"
FT DOMAIN 21..71
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 31..32
FT /note="Reactive bond"
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; 9258 MW; 86A413FDB8879D9D CRC64;
MVFLLCFFLV ADVSYGINGD CELPKVVGPC RARFPRYYYN SSSKRCEKFI YGGCGGNANN
FHTLEECEKV CGVRSRDSPK EN
