ID   JTX12_CHIFL             Reviewed;         462 AA.
AC   A7L036;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Toxin CfTX-2 {ECO:0000303|PubMed:17688901};
DE            Short=Toxin 2 {ECO:0000303|PubMed:17688901};
DE   Flags: Precursor;
OS   Chironex fleckeri (Australian box jellyfish).
OC   Eukaryota; Metazoa; Cnidaria; Cubozoa; Chirodropida; Chirodropidae;
OC   Chironex.
OX   NCBI_TaxID=45396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-32, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Nematoblast;
RX   PubMed=17688901; DOI=10.1016/j.toxicon.2007.06.016;
RA   Brinkman D., Burnell J.;
RT   "Identification, cloning and sequencing of two major venom proteins from
RT   the box jellyfish, Chironex fleckeri.";
RL   Toxicon 50:850-860(2007).
RN   [2]
RP   FUNCTION, AND FAMILY.
RC   TISSUE=Tentacle;
RX   PubMed=24403082; DOI=10.1074/jbc.m113.534149;
RA   Brinkman D.L., Konstantakopoulos N., McInerney B.V., Mulvenna J.,
RA   Seymour J.E., Isbister G.K., Hodgson W.C.;
RT   "Chironex fleckeri (box jellyfish) venom proteins: expansion of a cnidarian
RT   toxin family that elicits variable cytolytic and cardiovascular effects.";
RL   J. Biol. Chem. 289:4798-4812(2014).
RN   [3]
RP   IDENTIFICATION IN TRANSCRIPTOME AND PROTEOME, AND SUBCELLULAR LOCATION.
RC   TISSUE=Tentacle;
RX   PubMed=25793725; DOI=10.3390/toxins7030936;
RA   Jouiaei M., Casewell N.R., Yanagihara A.A., Nouwens A., Cribb B.W.,
RA   Whitehead D., Jackson T.N., Ali S.A., Wagstaff S.C., Koludarov I.,
RA   Alewood P., Hansen J., Fry B.G.;
RT   "Firing the sting: chemically induced discharge of cnidae reveals novel
RT   proteins and peptides from box jellyfish (Chironex fleckeri) venom.";
RL   Toxins 7:936-950(2015).
CC   -!- FUNCTION: May cause profound effects on the cardiovascular system of
CC       anesthetized rats (at 25 ug/kg), since the fraction containing this
CC       toxin and CfTX-1 produces an initial increase in mean arterial
CC       pressure, followed by cardiovascular collapse in all animals within 1
CC       minute of injection (PubMed:24403082). To note, the same fraction does
CC       not induce significant change in heart rate (PubMed:24403082). Has weak
CC       hemolytic activity (PubMed:24403082). Is lethal to crayfish (By
CC       similarity). Causes cutaneous inflammation in humans (By similarity).
CC       May act as a pore-forming toxin, disrupting normal transmembrane ion
CC       concentration gradients in susceptible cells (By similarity).
CC       {ECO:0000250|UniProtKB:Q9GV72, ECO:0000269|PubMed:24403082}.
CC   -!- SUBUNIT: Oligomer. {ECO:0000305|PubMed:24403082}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17688901,
CC       ECO:0000269|PubMed:25793725}. Nematocyst {ECO:0000269|PubMed:17688901,
CC       ECO:0000269|PubMed:25793725}. Target cell membrane {ECO:0000250}.
CC       Note=Forms a membrane channel in the prey. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Nematocytes. {ECO:0000305}.
CC   -!- PTM: Contains disulfide bonds. {ECO:0000305}.
CC   -!- MISCELLANEOUS: The fraction containing this toxin and CfTX-1 does not
CC       cross-react with CfTX-A and CfTX-B antibodies.
CC       {ECO:0000269|PubMed:24403082}.
CC   -!- MISCELLANEOUS: Surprisingly, only found after chemical disruption of
CC       nematocysts, and not also after pressure disruption of nematocysts.
CC       {ECO:0000269|PubMed:25793725}.
CC   -!- SIMILARITY: Belongs to the jellyfish toxin family. Type I subfamily.
CC       {ECO:0000305|PubMed:24403082}.
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DR   EMBL; EF636903; ABS30941.1; -; mRNA.
DR   AlphaFoldDB; A7L036; -.
DR   PRIDE; A7L036; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cardiotoxin; Direct protein sequencing; Disulfide bond; Ion transport;
KW   Membrane; Nematocyst; Secreted; Signal; Target cell membrane;
KW   Target membrane; Toxin; Transmembrane; Transport.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:17688901"
FT   CHAIN           18..462
FT                   /note="Toxin CfTX-2"
FT                   /evidence="ECO:0000305|PubMed:17688901"
FT                   /id="PRO_0000311593"
FT   CONFLICT        25
FT                   /note="L -> I (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  51684 MW;  677AEB64DC61A99F CRC64;
     MILVSLLPLL FMTGIASEST ISSGLASLKA KIDIKKPTGK QLFDKVKSME QALENKFSDD
     DERAKVMGAI GSLGTAIGKF QSGDPASIAS GCLDILVGIS SVLKDFAKFS PVFSILSLVV
     GLFSGTKAEE SVSSVVTKAI QEQSDQELQE ALYGVKREFA VSKAFLDGVR NEESDLRPTE
     VSALAANIPV YQGVRFIAMV VQRIKYIKPK TESEIKRMLT MLELFTDLCS IRDLILLDLH
     QLIATPGHSP NIASGIKEVT SLGREEYQRV FEDLLKTDDE ETFLFLSYLY PKEKNEQSRK
     IFKFFDLIEV KYDDRFKLDL SGGQALSTLQ WPNYYLCPHN DYLANNCHDL RVGLKLEKLS
     DGFYTIKTYG RDPRTCYWTD DYVKISSTSN GELEKFSFVP VQVKGQKAYL LSTKKWPHNF
     AYSQKTANGL LSILKDVPSK LGYGNQGFFT ISTYSNPKNR HA