ID   JTX2A_CHIFL             Reviewed;         454 AA.
AC   T1PRE3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Toxin CfTX-A {ECO:0000303|PubMed:24403082};
DE   AltName: Full=Toxin A {ECO:0000312|EMBL:AFQ00676.1};
DE            Short=TX-A {ECO:0000312|EMBL:AFQ00676.1};
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 26-45; 53-64 AND 314-322,
RP   SUBCELLULAR LOCATION, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP   SUBUNIT, AND 3D-STRUCTURE MODELING.
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   [2]
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: The fraction containing this toxin and CfTX-A shows potent
CC       hemolytic activity (PubMed:24403082). This fraction causes minor
CC       effects on the cardiovascular system of anesthetized rats (at 25
CC       ug/kg), since it has no significant effects on heart rate but produces
CC       relatively small increases in mean arterial pressure (PubMed:24403082).
CC       {ECO:0000269|PubMed:24403082}.
CC   -!- SUBUNIT: Oligomer. {ECO:0000305|PubMed:24403082}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24403082,
CC       ECO:0000269|PubMed:25793725}. Nematocyst {ECO:0000269|PubMed:24403082,
CC       ECO:0000269|PubMed:25793725}. Target cell membrane
CC       {ECO:0000305|PubMed:24403082}. Note=Forms a membrane channel in the
CC       prey. {ECO:0000305|PubMed:24403082}.
CC   -!- TISSUE SPECIFICITY: Nematocytes. {ECO:0000305}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000305}.
CC   -!- MISCELLANEOUS: The fraction containing this toxin and CfTX-B does not
CC       cross-react with CfTX-1 and CfTX-2 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 II subfamily.
CC       {ECO:0000305|PubMed:24403082}.
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DR   EMBL; JN695597; AFQ00676.1; -; mRNA.
DR   TCDB; 1.C.112.1.2; the cubozoan protein toxin (cpt) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Coiled coil; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; Hemolysis; Membrane; Nematocyst;
KW   Secreted; Signal; Target cell membrane; Target membrane; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..25
FT                   /evidence="ECO:0000305|PubMed:24403082"
FT                   /id="PRO_0000453745"
FT   CHAIN           26..454
FT                   /note="Toxin CfTX-A"
FT                   /evidence="ECO:0000305|PubMed:24403082"
FT                   /id="PRO_5004583032"
FT   COILED          27..61
FT                   /evidence="ECO:0000255"
FT   CONFLICT        33
FT                   /note="G -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  50485 MW;  F928845A2A9C387F CRC64;
     MDYAFIVFLV CFVSGTLGNR RRAKRDVDEV TSGINQLVNQ LNNVQQDTAA IKSALEELKT
     EVSASPSTVS QVSEVVNTVG SSLTKFTSGD AFNIVSGCLD LLSTVASTFG GPYGIAISAV
     ISLVSSILSL FAGDGFDSAT RKVIEEAFKT HRDQELRDSV NGARRTFNDV IAFLKGASKH
     GNVTEQELEV ISKGVPLTKL SDTLGILESR INRGSTSTDA AEAERTVEFI FLYLQLATMR
     DTLITNFILI LKQVPAADTY ANAVSISLDA NKESVRETID FLHNMEAKNA VCGAYYYPIY
     HSEMTKSILS FAKFFGLPDP PRNTFGGVYR VQNRYWPTWY ICKESYMGNH MFRGCSNVRS
     PSVQIRALEN GYQKINLRGK NMYITKHAQG WAWGTADNDP GEQGYFVFVP LKSGYYMIST
     KKWPNYFVYM ESSASGYIRS WNHNPGLQGH WRIL