NAU1A_EXADI
ID NAU1A_EXADI Reviewed; 90 AA.
AC E3P6S4;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Delta-aiptatoxin-Adi1a {ECO:0000305};
DE Short=Delta-ATTX-Adi1a {ECO:0000305};
DE AltName: Full=Ion channel modifier Ade-1 {ECO:0000303|PubMed:23356888};
DE Short=Ade1 {ECO:0000312|EMBL:ACQ83467.1};
DE Flags: Precursor;
OS Exaiptasia diaphana (Tropical sea anemone) (Aiptasia pulchella).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Aiptasiidae; Exaiptasia.
OX NCBI_TaxID=2652724;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-76, FUNCTION, TOXIC
RP DOSE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND 3D-STRUCTURE MODELING.
RX PubMed=23356888; DOI=10.1042/bj20121623;
RA Nesher N., Shapira E., Sher D., Moran Y., Tsveyer L., Turchetti-Maia A.L.,
RA Horowitz M., Hochner B., Zlotkin E.;
RT "AdE-1, a new inotropic Na(+) channel toxin from Aiptasia diaphana, is
RT similar to, yet distinct from, known anemone Na(+) channel toxins.";
RL Biochem. J. 451:81-90(2013).
RN [2]
RP FUNCTION.
RX PubMed=24749540; DOI=10.1042/bj20131454;
RA Nesher N., Zlotkin E., Hochner B.;
RT "The sea anemone toxin AdE-1 modifies both sodium and potassium currents of
RT rat cardiomyocytes.";
RL Biochem. J. 461:51-59(2014).
CC -!- FUNCTION: Cardioactive peptide that acts on voltage-gated sodium
CC channels (hNav1.5/SCN5A) and voltage-gated potassium channels (Kv)
CC (PubMed:23356888, PubMed:24749540). The activity on sodium channels
CC consists of inhibition on sodium current inactivation with no
CC significant effect on current activation. This effect may be caused by
CC direct interaction of the toxin with sodium channel site-3
CC (PubMed:23356888, PubMed:24749540). The activity on potassium channels
CC consists of a significant increase of the amplitude of the transient
CC component of the potassium current, shifting the current threshold to
CC more negative membrane potentials. These effects are concentration-
CC dependent and reversible and may be due to a direct interaction between
CC the toxin and the voltage-sensing domain of the channel
CC (PubMed:24749540). Physiologically, this toxin increases the amplitude
CC of cardiomyocyte contraction and slows the late phase of the twitch
CC relaxation velocity with no induction of spontaneous twitching. It
CC increases action potential duration of cardiomyocytes with no effect on
CC its threshold and on the cell resting potential. On insects, it shows
CC neurotoxic activity to the blowfly larvae S.falculaty, causing an
CC immediate spasm that progressed to body contraction and paralysis.
CC {ECO:0000269|PubMed:23356888, ECO:0000269|PubMed:24749540}.
CC -!- SUBCELLULAR LOCATION: Secreted. Nematocyst
CC {ECO:0000269|PubMed:23356888}.
CC -!- MASS SPECTROMETRY: Mass=4907; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23356888};
CC -!- TOXIC DOSE: PD(50) is 16.91 +-5.78 ug/kg into blowfly larvae
CC (S.falculata). {ECO:0000269|PubMed:23356888}.
CC -!- MISCELLANEOUS: Has no hemolytic activity on human erythrocytes. Has no
CC effect on the shape, color and configuration of cardiomyocytes
CC (PubMed:23356888). Does not show significant effect on the calcium
CC currents (PubMed:24749540). {ECO:0000269|PubMed:23356888}.
CC -!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin
CC family. {ECO:0000305}.
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DR EMBL; FJ418889; ACQ83467.1; -; mRNA.
DR AlphaFoldDB; E3P6S4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 2.20.20.10; -; 1.
DR InterPro; IPR023355; Myo_ane_neurotoxin_sf.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Myotoxin; Nematocyst;
KW Neurotoxin; Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..44
FT /evidence="ECO:0000269|PubMed:23356888"
FT /id="PRO_0000434449"
FT CHAIN 47..90
FT /note="Delta-aiptatoxin-Adi1a"
FT /id="PRO_0000434450"
FT DISULFID 50..86
FT /evidence="ECO:0000250|UniProtKB:P01528"
FT DISULFID 52..77
FT /evidence="ECO:0000250|UniProtKB:P01528"
FT DISULFID 70..87
FT /evidence="ECO:0000250|UniProtKB:P01528"
SQ SEQUENCE 90 AA; 9929 MW; E115745D5BFAD7A0 CRC64;
MKTAMLIAVL GFCAALCFVE SSHEEEREAA VYLTDLVSKA ESAIKRGIPC RCDKNSDELN
GEQSYMNGNC GDGWKKCRSV NAIFNCCQRV
