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Delta-actitoxin-Axm1b (Delta-AITX-Axm1b) (Anthopleurin-B) (AP-B) (ApB)

 NA1B_ANTXA              Reviewed;          49 AA.
P01531; V9GZA1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
20-DEC-2017, entry version 96.
RecName: Full=Delta-actitoxin-Axm1b {ECO:0000303|PubMed:22683676};
Short=Delta-AITX-Axm1b {ECO:0000303|PubMed:22683676};
AltName: Full=Anthopleurin-B {ECO:0000303|PubMed:6108877};
Short=AP-B {ECO:0000303|PubMed:6108877};
Short=ApB {ECO:0000303|PubMed:8621610};
Anthopleura xanthogrammica (Giant green sea anemone) (Actinia
xanthogrammica).
Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
Actiniidae; Anthopleura.
NCBI_TaxID=6112;
[1]
PROTEIN SEQUENCE.
TISSUE=Nematoblast;
PubMed=4019448;
Reimer N.S., Yasunobu C.L., Yasunobu K.T., Norton T.R.;
"Amino acid sequence of the Anthopleura xanthogrammica heart
stimulant, anthopleurin-B.";
J. Biol. Chem. 260:8690-8693(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1629194;
Gallagher M.J., Blumenthal K.M.;
"Cloning and expression of wild-type and mutant forms of the
cardiotonic polypeptide anthopleurin B.";
J. Biol. Chem. 267:13958-13963(1992).
[3]
PROTEIN SEQUENCE OF 1-28.
PubMed=6108877;
Norton T.R.;
"Cardiotonic polypeptides from Anthopleura xanthogrammica (Brandt) and
A. elegantissima (Brandt).";
Fed. Proc. 40:21-25(1981).
[4]
FUNCTION, MUTAGENESIS OF ARG-12 AND LYS-49, AND SITES ARG-12 AND
LYS-49.
PubMed=8276803;
Gallagher M.J., Blumenthal K.M.;
"Importance of the unique cationic residues arginine 12 and lysine 49
in the activity of the cardiotonic polypeptide anthopleurin B.";
J. Biol. Chem. 269:254-259(1994).
[5]
MUTAGENESIS OF ARG-14 AND LYS-48, AND SITES ARG-14 AND LYS-48.
PubMed=8288644;
Khera P.K., Blumenthal K.M.;
"Role of the cationic residues arginine 14 and lysine 48 in the
function of the cardiotonic polypeptide anthopleurin B.";
J. Biol. Chem. 269:921-925(1994).
[6]
FUNCTION, AND MUTAGENESIS OF ARG-12; ARG-14; LYS-48 AND LYS-49.
PubMed=7612595; DOI=10.1021/bi00027a003;
Khera P.K., Benzinger G.R., Lipkind G., Drum C.L., Hanck D.A.,
Blumenthal K.M.;
"Multiple cationic residues of anthopleurin B that determine high
affinity and channel isoform discrimination.";
Biochemistry 34:8533-8541(1995).
[7]
MUTAGENESIS OF ASP-7; ASP-9; HIS-34; LYS-37 AND HIS-39, AND SITES
ASP-7; ASP-9; LYS-34; LYS-37 AND LYS-39.
PubMed=8639500; DOI=10.1021/bi9528457;
Khera P.K., Blumenthal K.M.;
"Importance of highly conserved anionic residues and electrostatic
interactions in the activity and structure of the cardiotonic
polypeptide anthopleurin B.";
Biochemistry 35:3503-3507(1996).
[8]
MUTAGENESIS OF PRO-3; ARG-12; PRO-13; ILE-21; PHE-24; ASN-42 AND
LYS-49, AND SITE PRO-13.
PubMed=8916901; DOI=10.1021/bi961584d;
Kelso G.J., Drum C.L., Hanck D.A., Blumenthal K.M.;
"Role for Pro-13 in directing high-affinity binding of anthopleurin B
to the voltage-sensitive sodium channel.";
Biochemistry 35:14157-14164(1996).
[9]
MUTAGENESIS OF LEU-18 AND ILE-43, AND SITES LEU-18 AND ILE-43.
PubMed=8621610; DOI=10.1074/jbc.271.16.9422;
Dias-Kadambi B.L., Drum C.L., Hanck D.A., Blumenthal K.M.;
"Leucine 18, a hydrophobic residue essential for high affinity binding
of anthopleurin B to the voltage-sensitive sodium channel.";
J. Biol. Chem. 271:9422-9428(1996).
[10]
MUTAGENESIS OF TRP-33 AND TRP-45, AND SITES TRP-33 AND TRP-45.
PubMed=8798612; DOI=10.1074/jbc.271.39.23828;
Dias-Kadambi B.L., Combs K.A., Drum C.L., Hanck D.A., Blumenthal K.M.;
"The role of exposed tryptophan residues in the activity of the
cardiotonic polypeptide anthopleurin B.";
J. Biol. Chem. 271:23828-23835(1996).
[11]
FUNCTION ON CHANNEL DOMAIN 1-DOMAIN 4 INTERFACE.
PubMed=9306007; DOI=10.1007/s004240050460;
Benzinger G.R., Drum C.L., Chen L.Q., Kallen R.G., Hanck D.A.,
Hanck D.;
"Differences in the binding sites of two site-3 sodium channel
toxins.";
Pflugers Arch. 434:742-749(1997).
[12]
MUTAGENESIS OF LYS-37; HIS-39 AND TRP-45, AND SITES LYS-37; HIS-39 AND
TRP-45.
PubMed=9417050; DOI=10.1074/jbc.273.1.80;
Benzinger G.R., Kyle J.W., Blumenthal K.M., Hanck D.A.;
"A specific interaction between the cardiac sodium channel and site-3
toxin anthopleurin B.";
J. Biol. Chem. 273:80-84(1998).
[13]
MUTAGENESIS OF GLY-10; GLY-15 AND GLY-20, AND SITES GLY-10; GLY-15 AND
GLY-20.
PubMed=14661964; DOI=10.1021/bi035291d;
Seibert A.L., Liu J., Hanck D.A., Blumenthal K.M.;
"Arg-14 loop of site 3 anemone toxins: effects of glycine replacement
on toxin affinity.";
Biochemistry 42:14515-14521(2003).
[14]
MUTAGENESIS OF ASN-16; THR-17 AND SER-19, AND SITES ASN-16; THR-17 AND
SER-19.
PubMed=15170345; DOI=10.1021/bi0496135;
Seibert A.L., Liu J., Hanck D.A., Blumenthal K.M.;
"Role of Asn-16 and Ser-19 in anthopleurin B binding. Implications for
the electrostatic nature of Na(V) site 3.";
Biochemistry 43:7082-7089(2004).
[15]
PHOSPHOLIPID-BINDING ACTIVITY.
PubMed=15632158; DOI=10.1074/jbc.M412552200;
Smith J.J., Alphy S., Seibert A.L., Blumenthal K.M.;
"Differential phospholipid binding by site 3 and site 4 toxins.
Implications for structural variability between voltage-sensitive
sodium channel domains.";
J. Biol. Chem. 280:11127-11133(2005).
[16]
FUNCTION.
PubMed=24898004; DOI=10.1124/mol.114.092338;
Xiao Y., Blumenthal K., Cummins T.R.;
"Gating-pore currents demonstrate selective and specific modulation of
individual sodium channel voltage-sensors by biological toxins.";
Mol. Pharmacol. 86:159-167(2014).
[17]
REVIEW.
PubMed=17092528; DOI=10.1016/j.toxicon.2006.09.017;
Hanck D.A., Sheets M.F.;
"Site-3 toxins and cardiac sodium channels.";
Toxicon 49:181-193(2007).
[18]
NOMENCLATURE.
PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
Oliveira J.S., Fuentes-Silva D., King G.F.;
"Development of a rational nomenclature for naming peptide and protein
toxins from sea anemones.";
Toxicon 60:539-550(2012).
[19]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=7582896; DOI=10.1016/S0969-2126(01)00214-3;
Monks S.A., Pallaghy P.K., Scanlon M.J., Norton R.S.;
"Solution structure of the cardiostimulant polypeptide anthopleurin-B
and comparison with anthopleurin-A.";
Structure 3:791-803(1995).
-!- FUNCTION: Binds specifically to voltage-gated sodium channels
(Nav) (site 3), thereby delaying their inactivation. This toxin
has the highest affinity of all anemone toxins for the mammalian
sodium channel, whereas its paralog Anthopleurin-A retains the
greatest capacity to discriminate between cardiac (Nav1.5/SCN5A)
and neuronal sodium channels (PubMed:8916901). When tested
electrophysiologically, this toxin exhibits a high affinity for
multiple sodium channels with a 50-fold preference for rat cardiac
(Nav1.5/SCN5A) over neuronal channels (0.1 nM versus 5 nM). When
tested by ion flux, the affinities are similar and appear to have
higher affinity (9 nM versus 22 nM) (PubMed:8276803,
PubMed:7612595). The residue Lys-37 of this toxin has been shown
to interact with channel Nav1.5 (residue Asp-1612 in rat and Asp-
1610 in human), which is located in the DIV S3-S4 linker
(corresponding to channel site 3) (PubMed:9417050,
PubMed:24898004). Selectively modifies sodium channel inactivation
from the open state with little effect on channel activation or on
inactivation from closed states (By similarity). Does not display
phospholipid-binding activities, suggesting that the domain IV S3-
S4 linker is located at the extracellular surface and not buried
in the phospholipid bilayer (PubMed:15632158).
{ECO:0000250|UniProtKB:P01530, ECO:0000269|PubMed:15632158,
ECO:0000269|PubMed:24898004, ECO:0000269|PubMed:7612595,
ECO:0000269|PubMed:8276803, ECO:0000269|PubMed:8916901,
ECO:0000269|PubMed:9306007, ECO:0000269|PubMed:9417050}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst
{ECO:0000305}.
-!- SIMILARITY: Belongs to the sea anemone sodium channel inhibitory
toxin family. Type I subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA27737.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia;
URL="https://en.wikipedia.org/wiki/Anthopleurin";
-----------------------------------------------------------------------
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EMBL; M90675; AAA27737.1; ALT_INIT; mRNA.
PIR; A92547; NAXAB.
PDB; 1APF; NMR; -; A=1-49.
PDBsum; 1APF; -.
ProteinModelPortal; P01531; -.
SMR; P01531; -.
EvolutionaryTrace; P01531; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
Gene3D; 2.20.20.10; -; 1.
InterPro; IPR000693; Anenome_toxin.
InterPro; IPR023355; Myo_ane_neurotoxin_sf.
Pfam; PF00706; Toxin_4; 1.
PIRSF; PIRSF001905; Anenome_toxin; 1.
1: Evidence at protein level;
3D-structure; Cardiotoxin; Direct protein sequencing; Disulfide bond;
Ion channel impairing toxin; Nematocyst; Neurotoxin; Secreted; Toxin;
Voltage-gated sodium channel impairing toxin.
CHAIN 1 49 Delta-actitoxin-Axm1b.
{ECO:0000269|PubMed:4019448}.
/FTId=PRO_0000221516.
REGION 1 7 Well-structured region.
{ECO:0000305|PubMed:14661964,
ECO:0000305|PubMed:15170345}.
REGION 8 17 Arg-14 loop (non-well-structured region).
{ECO:0000305|PubMed:14661964,
ECO:0000305|PubMed:15170345}.
REGION 18 49 Well-structured region.
{ECO:0000305|PubMed:14661964,
ECO:0000305|PubMed:15170345}.
SITE 7 7 Structurally important.
{ECO:0000305|PubMed:8639500}.
SITE 9 9 Important for sodium channel affinity and
for toxin structure.
{ECO:0000305|PubMed:8639500}.
SITE 10 10 Important for affinity to sodium channel,
probably due to the flexibility this
residue gives to the Arg-14 loop.
{ECO:0000305|PubMed:14661964}.
SITE 12 12 Key residue for binding both cardiac and
neuronal sodium channels.
{ECO:0000305|PubMed:8276803}.
SITE 13 13 Important for sodium channel affinity.
{ECO:0000305|PubMed:8916901}.
SITE 14 14 Not essential for sodium channel
affinity. {ECO:0000305|PubMed:8288644}.
SITE 15 15 Important for affinity to sodium channel,
probably due to the flexibility this
residue gives to the Arg-14 loop.
{ECO:0000305|PubMed:14661964}.
SITE 16 16 Binds to sodium channel.
{ECO:0000305|PubMed:15170345}.
SITE 17 17 Has its side chain oriented away from the
channel in the binary complex.
{ECO:0000305|PubMed:15170345}.
SITE 18 18 Important for high affinity to sodium
channel. {ECO:0000305|PubMed:8621610}.
SITE 19 19 Binds to sodium channel.
{ECO:0000305|PubMed:15170345}.
SITE 20 20 Structurally important.
{ECO:0000305|PubMed:14661964}.
SITE 33 33 Important for channel affinity.
{ECO:0000305|PubMed:8798612}.
SITE 34 34 Not important for channel affinity and
toxin structure.
{ECO:0000305|PubMed:8639500}.
SITE 37 37 Important for channel affinity (interacts
with rat Nav1.5 channel residue Asp-
1612). {ECO:0000305|PubMed:8639500,
ECO:0000305|PubMed:9417050}.
SITE 39 39 Not important for channel affinity and
toxin structure.
{ECO:0000305|PubMed:8639500}.
SITE 43 43 Structurally important.
{ECO:0000305|PubMed:8621610}.
SITE 45 45 Does not affect binding, but may affect
the stabilization of the cardiac channel
open conformation.
{ECO:0000305|PubMed:8798612}.
SITE 48 48 Binds to sodium channel.
{ECO:0000305|PubMed:8288644}.
SITE 49 49 Important for most of the cardiac
specificity.
{ECO:0000305|PubMed:8276803}.
DISULFID 4 46 {ECO:0000269|PubMed:7582896}.
DISULFID 6 36 {ECO:0000269|PubMed:7582896}.
DISULFID 29 47 {ECO:0000269|PubMed:7582896}.
MUTAGEN 3 3 P->S: Minor decrease in affinity for
sodium channels (4.7-fold on neuronal and
2-fold on cardiac (Nav1.5) channels).
{ECO:0000269|PubMed:8916901}.
MUTAGEN 7 7 D->A,N: Incorrect folding or very limited
amount of mutant obtained.
{ECO:0000269|PubMed:8639500}.
MUTAGEN 7 7 D->K: Incorrect folding; when associated
with D-37. {ECO:0000269|PubMed:8639500}.
MUTAGEN 7 7 D->N: Small decrease in affinity (4-6-
fold), and very limited amount of mutant
obtained. {ECO:0000269|PubMed:8639500}.
MUTAGEN 9 9 D->A: Major decrease in affinity for both
cardiac (Nav1.5) (300-fold) and neuronal
(100-fold) channels.
{ECO:0000269|PubMed:8639500}.
MUTAGEN 9 9 D->N: Decrease in affinity for both
cardiac (Nav1.5) (10-fold) and neuronal
(8-fold) channels.
{ECO:0000269|PubMed:8639500}.
MUTAGEN 10 10 G->A: Decrease in affinity for both
cardiac (Nav1.5) (15-fold) and neuronal
(450-fold) channels, as well as a 30-fold
increase in discrimination for Nav1.5.
Decrease in affinity for cardiac (Nav1.5)
(600-fold); when associated with A-15.
Not correctly folded; when associated
with A-20. {ECO:0000269|PubMed:14661964}.
MUTAGEN 12 12 R->A: Major decrease in affinity for both
cardiac (Nav1.5) and neuronal sodium
channels. {ECO:0000269|PubMed:8276803}.
MUTAGEN 12 12 R->K: Minor effect on toxicity.
{ECO:0000269|PubMed:8276803}.
MUTAGEN 12 12 R->S: Minor effect on toxicity. Decrease
in affinity for both cardiac (Nav1.5) (5-
fold) and neuronal (37-fold) channels;
when associated with Q-49 (tested by ion
flux studies). Loss of discrimination
between cardiac and neuronal channels;
when associated with Val-13 and Q-49.
{ECO:0000269|PubMed:7612595,
ECO:0000269|PubMed:8276803,
ECO:0000269|PubMed:8916901}.
MUTAGEN 13 13 P->V: Decrease in affinity for both
cardiac (Nav1.5) (9-fold) and neuronal
channels (9-fold). Loss of discrimination
between cardiac and neuronal channels;
when associated with S-12 and Q-49.
{ECO:0000269|PubMed:8916901}.
MUTAGEN 14 14 R->A: Minor effect on toxicity.
{ECO:0000269|PubMed:8288644}.
MUTAGEN 14 14 R->K: Minor effect on toxicity.
{ECO:0000269|PubMed:8288644}.
MUTAGEN 14 14 R->Q: Minor effect on toxicity. Decrease
in affinity for both cardiac (Nav1.5)
(56-fold) and neuronal (72-fold)
channels; when associated with S-12
(tested by ion flux studies). Decrease in
affinity for both cardiac (Nav1.5) (13-
fold) and neuronal (27-fold) channels;
when associated with A-48 (tested by ion
flux studies).
{ECO:0000269|PubMed:7612595,
ECO:0000269|PubMed:8288644}.
MUTAGEN 15 15 G->A: Decrease in affinity for both
cardiac (Nav1.5) (13-fold) and neuronal
(600-fold) channels, as well as a 50-fold
increase in discrimination for Nav1.5.
Decrease in affinity for cardiac (Nav1.5)
(600-fold); when associated with A-10.
{ECO:0000269|PubMed:14661964}.
MUTAGEN 16 16 N->A: Decrease in affinity for cardiac
(Nav1.5) (8-fold) channels.
{ECO:0000269|PubMed:15170345}.
MUTAGEN 16 16 N->D: Decrease in affinity for both
cardiac (Nav1.5) (500-fold) and neuronal
(3600-fold) channels.
{ECO:0000269|PubMed:15170345}.
MUTAGEN 16 16 N->R: Decrease in affinity for both
cardiac (Nav1.5) (5-fold) and neuronal
(56-fold) channels.
{ECO:0000269|PubMed:15170345}.
MUTAGEN 17 17 T->A,D: No change in activity.
{ECO:0000269|PubMed:15170345}.
MUTAGEN 18 18 L->A: Major decrease in affinity for both
cardiac (Nav1.5) (330-fold) and neuronal
(34-fold) channels, as well as a 9.5-fold
decrease in discrimination for Nav1.5.
{ECO:0000269|PubMed:8621610}.
MUTAGEN 18 18 L->V: Decrease in affinity for both
cardiac (Nav1.5) and neuronal channels.
{ECO:0000269|PubMed:8621610}.
MUTAGEN 19 19 S->A: Decrease in affinity for cardiac
(Nav1.5) (5.6-fold) channels.
{ECO:0000269|PubMed:15170345}.
MUTAGEN 19 19 S->D: Major decrease in affinity for both
cardiac (Nav1.5) (85-fold) and neuronal
(653-fold) channels.
{ECO:0000269|PubMed:15170345}.
MUTAGEN 19 19 S->R: Decrease in affinity for both
cardiac (Nav1.5) (5.7-fold) and neuronal
(27-fold) channels.
{ECO:0000269|PubMed:15170345}.
MUTAGEN 20 20 G->A: Incorrect folding. Incorrect
folding; when associated with A-10.
{ECO:0000269|PubMed:14661964}.
MUTAGEN 21 21 I->T: Minor decrease in affinity for
sodium channels (2.2-fold on neuronal and
2.9-fold on cardiac (Nav1.5) channels).
{ECO:0000269|PubMed:8916901}.
MUTAGEN 24 24 F->L: Minor decrease in affinity for
sodium channels (4.8-fold on neuronal and
2.4-fold on cardiac (Nav1.5) channels).
{ECO:0000269|PubMed:8916901}.
MUTAGEN 33 33 W->A: No mutant obtained.
{ECO:0000269|PubMed:8798612}.
MUTAGEN 33 33 W->F: Major decrease in affinity for both
cardiac (Nav1.5) (31-fold) and neuronal
(50-fold) channels (tested by ion flux
studies). This mutant is the first ApB
mutant that displays a significantly
altered association rate (K(on)).
{ECO:0000269|PubMed:8798612}.
MUTAGEN 33 33 W->S: No mutant obtained.
{ECO:0000269|PubMed:8798612}.
MUTAGEN 33 33 W->Y: Minor decrease in affinity for both
cardiac (Nav1.5) (5.6-fold) and neuronal
(5-fold) channels.
{ECO:0000269|PubMed:8798612}.
MUTAGEN 34 34 H->A: Minor decrease in affinity.
{ECO:0000269|PubMed:8639500}.
MUTAGEN 37 37 K->A: Decrease in affinity for both
cardiac (Nav1.5) (11-fold) and neuronal
(7-fold) channels.
{ECO:0000269|PubMed:8639500}.
MUTAGEN 37 37 K->A: Decrease in affinity for cardiac
(Nav1.5) channels (13-fold) (with
decrease in K(on) and increase in
K(off)). {ECO:0000269|PubMed:9417050}.
MUTAGEN 37 37 K->D: Incorrect folding; when associated
with K-7. {ECO:0000269|PubMed:8639500}.
MUTAGEN 39 39 H->A: No change in activity.
{ECO:0000269|PubMed:8639500}.
MUTAGEN 39 39 H->A: Small decrease in affinity for
cardiac (Nav1.5) channels (1.1-fold)
(with increase in both K(on) and K(off)).
{ECO:0000269|PubMed:9417050}.
MUTAGEN 42 42 N->T: Minor decrease in affinity for
sodium channels (1.1-fold on neuronal and
3.4-fold on cardiac (Nav1.5) channels).
{ECO:0000269|PubMed:8916901}.
MUTAGEN 43 43 I->A,G,F: Incorrect folding.
{ECO:0000269|PubMed:8621610}.
MUTAGEN 43 43 I->L,V: Small decrease in apparent
binding affinity for both neuronal and
cardiac (Nav1.5) channels (tested by ion
flux studies).
{ECO:0000269|PubMed:8621610}.
MUTAGEN 45 45 W->A: Minor decrease in affinity for both
cardiac (Nav1.5) (7.7-fold) and neuronal
(4-fold) channels (tested by ion flux
studies). {ECO:0000269|PubMed:8798612}.
MUTAGEN 45 45 W->F: Minor decrease in affinity for both
cardiac (Nav1.5) (2-4-fold) (with
decrease in K(on) and increase in K(off))
and neuronal (5-fold) channels (tested by
ion flux studies).
{ECO:0000269|PubMed:8798612,
ECO:0000269|PubMed:9417050}.
MUTAGEN 45 45 W->S: Minor decrease in affinity for both
cardiac (Nav1.5) (3.3-fold) and neuronal
(7-fold) channels (tested by ion flux
studies). {ECO:0000269|PubMed:8798612}.
MUTAGEN 48 48 K->A: Minor effect on toxicity. Decrease
in affinity for both cardiac (Nav1.5)
(13-fold) and neuronal (27-fold)
channels; when associated with Q-14
(tested by ion flux studies).
{ECO:0000269|PubMed:7612595,
ECO:0000269|PubMed:8288644}.
MUTAGEN 48 48 K->Q: Minor effect on toxicity.
{ECO:0000269|PubMed:8288644}.
MUTAGEN 48 48 K->R: Minor effect on toxicity.
{ECO:0000269|PubMed:8288644}.
MUTAGEN 49 49 K->A: Minor effect on toxicity.
{ECO:0000269|PubMed:8276803}.
MUTAGEN 49 49 K->Q: Minor effect on toxicity. Decrease
in affinity for both cardiac (Nav1.5) (5-
fold) and neuronal (37-fold) channels;
when associated with S-12 (tested by ion
flux studies). Loss of discrimination
between cardiac and neuronal channels;
when associated with S-12 and V-13.
{ECO:0000269|PubMed:7612595,
ECO:0000269|PubMed:8276803,
ECO:0000269|PubMed:8916901}.
MUTAGEN 49 49 K->R: Minor effect on toxicity.
{ECO:0000269|PubMed:8276803}.
CONFLICT 12 13 RP -> PN (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 25 25 Y -> A (in Ref. 3; AA sequence).
{ECO:0000305}.
TURN 14 17 {ECO:0000244|PDB:1APF}.
STRAND 20 23 {ECO:0000244|PDB:1APF}.
STRAND 42 47 {ECO:0000244|PDB:1APF}.
SEQUENCE 49 AA; 5274 MW; 7BD237179065AE90 CRC64;
GVPCLCDSDG PRPRGNTLSG ILWFYPSGCP SGWHNCKAHG PNIGWCCKK


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EIAAB31450 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4,Homo sapiens,hPLCD4,Human,Phosphoinositide phospholipase C-delta-4,Phospholipase C-delta-4,PLCD4,PLC-delta-4
EIAAB40071 Rat,Rattus norvegicus,Signal sequence receptor subunit delta,Ssr4,SSR-delta,Translocon-associated protein subunit delta,TRAP-delta
EIAAB31447 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4,Mouse,Mus musculus,Phosphoinositide phospholipase C-delta-4,Phospholipase C-delta-4,Plcd,Plcd4,PLC-delta-4
EIAAB31445 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3,Kiaa1964,Mouse,Mus musculus,Phosphoinositide phospholipase C-delta-3,Phospholipase C-delta-3,Plcd3,PLC-delta-3
EIAAB31442 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1,Mouse,Mus musculus,Phosphoinositide phospholipase C-delta-1,Phospholipase C-delta-1,Plcd,Plcd1,PLC-delta-1
15-288-22845 Translocon-associated protein subunit delta - TRAP-delta; Signal sequence receptor subunit delta; SSR-delta Polyclonal 0.1 mg
15-288-22845 Translocon-associated protein subunit delta - TRAP-delta; Signal sequence receptor subunit delta; SSR-delta Polyclonal 0.05 mg
EIAAB31448 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4,Phosphoinositide phospholipase C-delta-4,Phospholipase C-delta-4,Plcd4,PLC-delta-4,Rat,Rattus norvegicus
EIAAB12331 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase,Cholestenol Delta-isomerase,D8-D7 sterol isomerase,Delta(8)-Delta(7) sterol isomerase,EBP,Emopamil-binding protein,Homo sapiens,Human
EIAAB31449 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4,Phosphoinositide phospholipase C-delta-4,Phospholipase C-delta-4,Pig,PLCD4,PLC-delta-4,Sus scrofa
EIAAB12332 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase,Cholestenol Delta-isomerase,D8-D7 sterol isomerase,Delta(8)-Delta(7) sterol isomerase,Ebp,Emopamil-binding protein,Mouse,Msi,Mus musculus
EIAAB31446 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4,Bos taurus,Bovine,Phosphoinositide phospholipase C-delta-4,Phospholipase C-delta-2,Phospholipase C-delta-4,PLC-85,PLCD2,PLCD4,PLC-delt
EIAAB37638 Amiloride-sensitive sodium channel subunit delta,Delta-ENaC,Delta-NaCH,DNACH,ENaCD,Epithelial Na(+) channel subunit delta,Homo sapiens,Human,Nonvoltage-gated sodium channel 1 subunit delta,SCNED,SCNN1
EIAAB31441 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1,Homo sapiens,Human,Phosphoinositide phospholipase C-delta-1,Phospholipase C-delta-1,Phospholipase C-III,PLCD1,PLC-delta-1,PLC-III
EIAAB31440 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1,Phosphoinositide phospholipase C-delta-1,Phospholipase C-delta-1,Phospholipase C-III,Plcd1,PLC-delta-1,PLC-III,Rat,Rattus norvegicus
EIAAB31443 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1,Bos taurus,Bovine,Phosphoinositide phospholipase C-delta-1,Phospholipase C-delta-1,Phospholipase C-III,PLCD1,PLC-delta-1,PLC-III
EIAAB12333 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase,Cholestenol Delta-isomerase,D8-D7 sterol isomerase,Delta(8)-Delta(7) sterol isomerase,Ebp,Emopamil-binding protein,Rat,Rattus norvegicus,Rsi,Sterol 8-
EIAAB11418 Delta3,Delta-like protein 3,Dll3,Drosophila Delta homolog 3,M-Delta-3,Mouse,Mus musculus
EIAAB41750 A45,Cct4,Cctd,CCT-delta,Mouse,Mus musculus,T-complex protein 1 subunit delta,TCP-1-delta
EIAAB11413 Delta1,Delta-like protein 1,DLL1,Drosophila Delta homolog 1,H-Delta-1,Homo sapiens,Human,UNQ146_PRO172
EIAAB08601 Archain,Arcn1,Coatomer subunit delta,Copd,Delta-coat protein,Delta-COP,Mouse,Mus musculus


 

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