ID   TX60A_ACTVL             Reviewed;         498 AA.
AC   Q76DT2;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=DELTA-thalatoxin-Avl2a {ECO:0000303|PubMed:22683676};
DE            Short=DELTA-TATX-Avl2a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Toxin AvTX-60A {ECO:0000303|PubMed:15019483};
DE            Short=Av60A {ECO:0000303|PubMed:15019483};
DE   Flags: Precursor;
OS   Actineria villosa (Okinawan sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Nynantheae; Aliciidae; Actineria.
OX   NCBI_TaxID=227975;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-63, AND FUNCTION.
RC   TISSUE=Nematoblast;
RX   PubMed=15019483; DOI=10.1016/j.toxicon.2003.11.017;
RA   Oshiro N., Kobayashi C., Iwanaga S., Nozaki M., Namikoshi M., Spring J.,
RA   Nagai H.;
RT   "A new membrane-attack complex/perforin (MACPF) domain lethal toxin from
RT   the nematocyst venom of the Okinawan sea anemone Actineria villosa.";
RL   Toxicon 43:225-228(2004).
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: Is lethal to mice, and may cause hemolytic activity.
CC       {ECO:0000269|PubMed:15019483}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
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DR   EMBL; AB107916; BAD04943.1; -; mRNA.
DR   AlphaFoldDB; Q76DT2; -.
DR   TCDB; 1.C.39.10.1; the membrane attack complex/perforin (macpf) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR020864; MACPF.
DR   Pfam; PF01823; MACPF; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS51412; MACPF_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytolysis; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Hemolysis; Nematocyst; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..35
FT                   /evidence="ECO:0000269|PubMed:15019483"
FT                   /id="PRO_0000239811"
FT   CHAIN           36..498
FT                   /note="DELTA-thalatoxin-Avl2a"
FT                   /id="PRO_0000239812"
FT   DOMAIN          23..359
FT                   /note="MACPF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT   DOMAIN          410..422
FT                   /note="EGF-like"
FT   COILED          135..159
FT                   /evidence="ECO:0000255"
FT   DISULFID        389..402
FT                   /evidence="ECO:0000250"
FT   DISULFID        396..410
FT                   /evidence="ECO:0000250"
FT   DISULFID        412..422
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   498 AA;  55463 MW;  515D5766108838C0 CRC64;
     MSPYFKLSSA LIFLAITMEA LCSPIENTST SNKDNDKETE HIEISAKPSG ISRGALGQGF
     EIHREDLLSK QFEATGEKIF EDLPMDECTV TTTLGTIERD DSFYNSTESL YQSVASSTKI
     SGSLKGAYTL GVSVAAVTNN IASSEEEVQG LSLNLKAYSM SSILKKNCVN TKPLSKDLVS
     DFEALDSEIT KPWKLSSWKK YKVLLEKYGS HIVKESISGS SIYQYVFAKS NQKFNHRSFT
     VKACVSLAGP KNASKVGFAG CTGVSQQEIE QSSSQSMIKK LVVRGGKTET RASLIGELDP
     DQINKFLIEA ETDPSPIQYK FEPIWTILKN RYVGTEHFAK AVNLEQFYKG FLHFGCSFLH
     TSNADNADVE IQKFDFAKTS DPDAPTYVCK VGPEGCQHHE DCHYRAAFWC ECGGPYDLAR
     TCLRYKTEKL NSGSTKRECY PNKESGFAWH GCQLHGLSCW CSAPNKNWEE TWSGEDTNNA
     LNDVHQVLME KKRRDQAK