ID   TX9A2_ANEVI             Reviewed;         159 AA.
AC   P0DMZ9;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=U-actitoxin-Avd13b {ECO:0000303|PubMed:22683676};
DE   AltName: Full=AnmTX Avi 9a-1 {ECO:0000303|PubMed:23801332};
DE   AltName: Full=Peptide toxin AV-2 {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).
RN   [4]
RP   NOMENCLATURE.
RX   PubMed=23801332; DOI=10.1074/jbc.m113.485516;
RA   Osmakov D.I., Kozlov S.A., Andreev Y.A., Koshelev S.G., Sanamyan N.P.,
RA   Sanamyan K.E., Dyachenko I.A., Bondarenko D.A., Murashev A.N., Mineev K.S.,
RA   Arseniev A.S., Grishin E.V.;
RT   "Sea anemone peptide with uncommon beta-hairpin structure inhibits acid-
RT   sensing ion channel 3 (ASIC3) and reveals analgesic activity.";
RL   J. Biol. Chem. 288:23116-23127(2013).
CC   -!- FUNCTION: Inhibits ion channels. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the sea anemone structural class 9a family.
CC       {ECO:0000305|PubMed:23801332}.
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; FK736087; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DMZ9; -.
DR   SMR; P0DMZ9; -.
DR   PRIDE; P0DMZ9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Nematocyst; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..26
FT                   /evidence="ECO:0000305|PubMed:21281459"
FT                   /id="PRO_0000433722"
FT   PEPTIDE         27..55
FT                   /note="U-actitoxin-Avd13b"
FT                   /id="PRO_0000433723"
FT   PROPEP          59..60
FT                   /evidence="ECO:0000305|PubMed:21281459"
FT                   /id="PRO_0000433724"
FT   PEPTIDE         61..89
FT                   /note="U-actitoxin-Avd13b"
FT                   /id="PRO_0000433725"
FT   PROPEP          93..94
FT                   /evidence="ECO:0000305|PubMed:21281459"
FT                   /id="PRO_0000433726"
FT   PEPTIDE         95..123
FT                   /note="U-actitoxin-Avd13b"
FT                   /id="PRO_0000433727"
FT   PROPEP          127..128
FT                   /evidence="ECO:0000305|PubMed:21281459"
FT                   /id="PRO_0000433728"
FT   PEPTIDE         129..157
FT                   /note="U-actitoxin-Avd13b"
FT                   /id="PRO_0000433729"
FT   DISULFID        33..45
FT                   /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT   DISULFID        36..52
FT                   /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT   DISULFID        67..79
FT                   /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT   DISULFID        70..86
FT                   /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT   DISULFID        101..113
FT                   /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT   DISULFID        104..120
FT                   /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT   DISULFID        135..147
FT                   /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT   DISULFID        138..154
FT                   /evidence="ECO:0000250|UniProtKB:R4ZCU1"
SQ   SEQUENCE   159 AA;  17736 MW;  14A972F0B3B0A695 CRC64;
     MKSIFLVFFA VCLVKAEAGK GRKREPNIIN PPCRECYVQD SSGNCVYDKW GCGGARKREP
     NIINPPCREC YVQDSSGNCV YDKWGCGGAR KREPNIINPP CRECYVQDSS GNCVYDKWGC
     GGARKREPNI INPPCRECYV QDSSGNCVYD KWGCGGARK