ID   JTX2B_CHIFL             Reviewed;         461 AA.
AC   T1PQV6;
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-B {ECO:0000303|PubMed:24403082};
DE   AltName: Full=Toxin B {ECO:0000312|EMBL:AFQ00677.1};
DE            Short=TX-B {ECO:0000312|EMBL:AFQ00677.1};
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 32-46 AND 148-156,
RP   SUBCELLULAR LOCATION, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   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-B 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-A 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; JN695598; AFQ00677.1; -; mRNA.
DR   SMR; T1PQV6; -.
DR   TCDB; 1.C.112.1.5; 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.
DR   Gene3D; 1.20.190.10; -; 1.
DR   InterPro; IPR036716; Pest_crys_N_sf.
DR   SUPFAM; SSF56849; SSF56849; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; Hemolysis; Membrane; Nematocyst; Secreted; Signal;
KW   Target cell membrane; Target membrane; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..31
FT                   /evidence="ECO:0000305|PubMed:24403082"
FT                   /id="PRO_0000453746"
FT   CHAIN           32..461
FT                   /note="Toxin CfTX-B"
FT                   /evidence="ECO:0000305|PubMed:24403082"
FT                   /id="PRO_5004583417"
SQ   SEQUENCE   461 AA;  51117 MW;  83E84DB8E192BF2A CRC64;
     MDPRISSRLR ALALLVFVIS ITDGIPNRAK RSSSEINAEI DGLIQQLTTV DADTKGIQET
     LTELKTTVSA NPSRISQVSA VVKSVGSSLA KFKTGDPYNI VSGCLDILSS IATTYNGPYG
     VGLGAVASLL SSVIGLFAQD GFKNSLKSIV DEAFKRYRDE ELQGQLKGAS RTFNDVIGTL
     KNLTDKDTAV TDLEFSLATS SVSVSQFSNM LGIIESRINT GSTTTDLAEA KRTVDFIFLY
     LELAVMRETL LTQLILFTKK LGKFENYANG ISASIDANKQ AVHDTILFLH QMEPKNAVCG
     AYYYPVHHSD VSEGIFTFTR YFGLPDPPRN TFQGVYRVEN RYWPAWHICK ESYMGNHMFR
     GCSYIKSAGV HISALDNGYL KLNLKGKNMY ITKHAQGWAW GTADNDPGEQ GYFIFVPLKS
     GYYMISTKKW PNYFVYMESS ASGYIRSWHN NPGLQGHWKL T