TX9A_ANTMC
ID TX9A_ANTMC Reviewed; 233 AA.
AC P69929; Q5R215;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Delta-actitoxin-Amc1a {ECO:0000303|PubMed:22683676};
DE Short=Delta-AITX-Amc1a {ECO:0000303|PubMed:22683676};
DE AltName: Full=AnmTX Ama 9a-1 {ECO:0000303|PubMed:23801332};
DE AltName: Full=Peptide toxins Am I {ECO:0000303|PubMed:15581681};
DE AltName: Full=Peptide toxins Am-1 {ECO:0000305};
DE Flags: Precursor;
OS Antheopsis maculata (Sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Antheopsis.
OX NCBI_TaxID=280228;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, HYDROXYLATION AT PRO-39;
RP PRO-73; PRO-107; PRO-141; PRO-175 AND PRO-209, AND TOXIC DOSE.
RX PubMed=15581681; DOI=10.1016/j.toxicon.2004.09.013;
RA Honma T., Hasegawa Y., Ishida M., Nagai H., Nagashima Y., Shiomi K.;
RT "Isolation and molecular cloning of novel peptide toxins from the sea
RT anemone Antheopsis maculata.";
RL Toxicon 45:33-41(2005).
RN [2]
RP NOMENCLATURE.
RX PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA Oliveira J.S., Fuentes-Silva D., King G.F.;
RT "Development of a rational nomenclature for naming peptide and protein
RT toxins from sea anemones.";
RL Toxicon 60:539-550(2012).
RN [3]
RP NOMENCLATURE.
RX PubMed=23801332; DOI=10.1074/jbc.m113.485516;
RA Osmakov D.I., Kozlov S.A., Andreev Y.A., Koshelev S.G., Sanamyan N.P.,
RA Sanamyan K.E., Dyachenko I.A., Bondarenko D.A., Murashev A.N., Mineev K.S.,
RA Arseniev A.S., Grishin E.V.;
RT "Sea anemone peptide with uncommon beta-hairpin structure inhibits acid-
RT sensing ion channel 3 (ASIC3) and reveals analgesic activity.";
RL J. Biol. Chem. 288:23116-23127(2013).
CC -!- FUNCTION: May inhibit voltage-gated sodium channels (Nav).
CC {ECO:0000305|PubMed:15581681}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- PTM: Each Am I peptide may contain 2 disulfide bonds. {ECO:0000305}.
CC -!- PTM: The precursor protein seems to be processed in the following
CC sequence: release of the signal peptide and of the propeptide,
CC production of six identical 34-residue peptides by cleavage between Arg
CC and Glu, release of four N-terminal and three C-terminal residues from
CC each peptide and hydroxylation of each Pro in position 6 of the
CC resulting 27-residue peptides. {ECO:0000269|PubMed:15581681}.
CC -!- MASS SPECTROMETRY: Mass=2814.5; Method=MALDI; Note=The measured mass is
CC that of any peptide toxin Am-1.;
CC Evidence={ECO:0000269|PubMed:15581681};
CC -!- TOXIC DOSE: LD(50) is 830 ug/kg into crabs.
CC {ECO:0000269|PubMed:15581681}.
CC -!- SIMILARITY: Belongs to the sea anemone structural class 9a family.
CC {ECO:0000305|PubMed:23801332}.
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DR EMBL; AB180685; BAD74021.1; -; mRNA.
DR AlphaFoldDB; P69929; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Disulfide bond; Hydroxylation;
KW Ion channel impairing toxin; Nematocyst; Repeat; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..29
FT /id="PRO_0000034842"
FT PROPEP 30..33
FT /id="PRO_0000034843"
FT PEPTIDE 34..60
FT /note="Delta-actitoxin-Amc1a"
FT /id="PRO_0000034844"
FT PROPEP 61..63
FT /id="PRO_0000034845"
FT PROPEP 64..67
FT /id="PRO_0000034846"
FT PEPTIDE 68..94
FT /note="Delta-actitoxin-Amc1a"
FT /id="PRO_0000034847"
FT PROPEP 95..97
FT /id="PRO_0000034848"
FT PROPEP 98..101
FT /id="PRO_0000034849"
FT PEPTIDE 102..128
FT /note="Delta-actitoxin-Amc1a"
FT /id="PRO_0000034850"
FT PROPEP 129..131
FT /id="PRO_0000034851"
FT PROPEP 132..135
FT /id="PRO_0000034852"
FT PEPTIDE 136..162
FT /note="Delta-actitoxin-Amc1a"
FT /id="PRO_0000034853"
FT PROPEP 163..165
FT /id="PRO_0000034854"
FT PROPEP 166..169
FT /id="PRO_0000034855"
FT PEPTIDE 170..196
FT /note="Delta-actitoxin-Amc1a"
FT /id="PRO_0000034856"
FT PROPEP 197..199
FT /id="PRO_0000034857"
FT PROPEP 200..203
FT /id="PRO_0000034858"
FT PEPTIDE 204..230
FT /note="Delta-actitoxin-Amc1a"
FT /id="PRO_0000034859"
FT PROPEP 231..233
FT /id="PRO_0000034860"
FT SITE 29..30
FT /note="Cleavage"
FT SITE 63..64
FT /note="Cleavage"
FT SITE 97..98
FT /note="Cleavage"
FT SITE 131..132
FT /note="Cleavage"
FT SITE 165..166
FT /note="Cleavage"
FT SITE 199..200
FT /note="Cleavage"
FT MOD_RES 39
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:15581681"
FT MOD_RES 73
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:15581681"
FT MOD_RES 107
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:15581681"
FT MOD_RES 141
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:15581681"
FT MOD_RES 175
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:15581681"
FT MOD_RES 209
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:15581681"
FT DISULFID 40..51
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 43..58
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 74..85
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 77..92
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 108..119
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 111..126
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 142..153
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 145..160
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 176..187
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 179..194
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 210..221
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
FT DISULFID 213..228
FT /evidence="ECO:0000250|UniProtKB:R4ZCU1"
SQ SEQUENCE 233 AA; 25355 MW; 8BD59FCA01380C1D CRC64;
MKRIFIVALL FATCLVNAKP SINDADIKRE PEPNVAVPPC GDCYQQVGNT CVRVPSLCPS
RKREPEPNVA VPPCGDCYQQ VGNTCVRVPS LCPSRKREPE PNVAVPPCGD CYQQVGNTCV
RVPSLCPSRK REPEPNVAVP PCGDCYQQVG NTCVRVPSLC PSRKREPEPN VAVPPCGDCY
QQVGNTCVRV PSLCPSRKRE PEPNVAVPPC GDCYQQVGNT CVRVPSLCPS RKR
