ID   JTX11_CHIFL             Reviewed;         456 AA.
AC   A7L035;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Toxin CfTX-1 {ECO:0000303|PubMed:17688901};
DE            Short=Toxin 1 {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 21-42; 167-173; 199-206;
RP   221-235; 307-314 AND 393-405, AND SUBCELLULAR 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-2 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-2 does not
CC       cross-react with CfTX-A and CfTX-B antibodies.
CC       {ECO:0000269|PubMed:24403082}.
CC   -!- MISCELLANEOUS: Found after both pressure and chemical disruption of
CC       nematocysts. {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; EF636902; ABS30940.1; -; mRNA.
DR   AlphaFoldDB; A7L035; -.
DR   TCDB; 1.C.112.1.4; the cubozoan protein toxin (cpt) family.
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..20
FT                   /evidence="ECO:0000269|PubMed:17688901"
FT   CHAIN           21..456
FT                   /note="Toxin CfTX-1"
FT                   /evidence="ECO:0000305|PubMed:17688901"
FT                   /id="PRO_0000311592"
FT   CONFLICT        33
FT                   /note="T -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="S -> T (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221..223
FT                   /note="MLT -> VLS (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   456 AA;  51390 MW;  38751295A11D7D64 CRC64;
     MVKMLFFAFL PLLFMTGIAA ESTISSGLNS LKTKIDAKMP SGKQLFDKVV EMQKQIDAKF
     SNDDERAKVM GAIGSLSTAV GKFQSGDPAK IASGCLDILV GISSVLKDFA KFSPIFSILS
     LVVGLFSGTK AEESVGSVVK KAVQEQSDQE LQEALYGVKR EYAVSKAFLD GVRNETSDLS
     PTEVSALAAN VPIYQGVRFI AMVVQRIKYI KPKTESEIKR MLTMLELFTD LCSLRDLILL
     DLYQLVATPG HSPNIASGIK EVSNLGREEY KKVFEDLLKN DDKETYLFLS YLYPREKNEQ
     SRKIFNFFDL MKVKYDDRLK QDLTGVKIFS NVHWPNYFMC SSNDYLALIC TKPYGSLKLD
     KLNDGYYSIK TTQHDPKICH RYGNYILFTH KRNDDLEKFN FVPVKLEKRE IYLLSSKESP
     NKFAYVPQNA DGALFFVDGI PSKVGYGNQG YFTLVE