ID   TX60A_PHYSE             Reviewed;         501 AA.
AC   P58911;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=DELTA-alicitoxin-Pse2a {ECO:0000303|PubMed:22683676};
DE            Short=DELTA-ALTX-Pse2a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=Toxin PsTX-60A {ECO:0000303|PubMed:12061771};
DE            Short=PTX60A {ECO:0000303|PubMed:12061771};
DE   Flags: Precursor;
OS   Phyllodiscus semoni (Night anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Nynantheae; Aliciidae; Phyllodiscus.
OX   NCBI_TaxID=163701;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-61, AND FUNCTION.
RC   TISSUE=Nematoblast;
RX   PubMed=12061771; DOI=10.1016/s0006-291x(02)00547-8;
RA   Nagai H., Oshiro N., Takuwa-Kuroda K., Iwanaga S., Nozaki M., Nakajima T.;
RT   "Novel proteinaceous toxins from the nematocyst venom of the Okinawan sea
RT   anemone Phyllodiscus semoni Kwietniewski.";
RL   Biochem. Biophys. Res. Commun. 294:760-763(2002).
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: Causes lethal toxicity to the shrimp Palaemon paucidence, and
CC       hemolytic activity toward sheep red blood cells.
CC       {ECO:0000269|PubMed:12061771}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Nematocyst.
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DR   EMBL; AB063315; BAC00946.1; -; mRNA.
DR   AlphaFoldDB; P58911; -.
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:12061771"
FT                   /id="PRO_0000034867"
FT   CHAIN           36..501
FT                   /note="DELTA-alicitoxin-Pse2a"
FT                   /id="PRO_0000034868"
FT   DOMAIN          23..359
FT                   /note="MACPF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT   DOMAIN          388..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   501 AA;  56035 MW;  7C566F6132142E98 CRC64;
     MSPYFKLSSA LIFLAITMEA LCSPIENTST SNKDNDKETE HIEISAKPSG ISRGALGQGF
     EIHREDLLSK QFEATGEKIF EDLPMDECTV TTTLGTIERD DSFYNSTESL YQSVASSTKI
     SGSLKGAYTL GVSVAAVTNN IASSEEEVQG LSLNLKAYSM SSILKKNCVN TKPLSKDLVS
     DFEALDSEIT KPWKLSSWKK YKVLLEKYGS RIVKESISGS SIYQYVFAKS SQKFNHRSFT
     VKACVSLAGP TKVGKLSFSG CTGVSQQEIE QSSSQSMIKK LVVRGGKTET RASLIGELDP
     DQINKFLIEA ETDPSPIQYK FEPIWTILKT RYVGTEHFAK AVNLEQFYKG FLHFGCSYLH
     TTSAENKVAE MQKFDFAKTS DPDAPTYVCK VGPEGCQHHE DCHYRAAFWC ECGGPYDLAR
     TCFRHKFKKL KSGLTKKECY PNKESGFAWH GCRLHGLTCW CSAPNRSWEE SWSGEDTNNA
     LNDVHQVLME KKRRDNAQQQ Y