TX35_ACAPA
ID TX35_ACAPA Reviewed; 103 AA.
AC P0DV32;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=Omega toxin Ap5 {ECO:0000303|PubMed:34363923};
DE Contains:
DE RecName: Full=Omega toxin Ap3 {ECO:0000303|PubMed:34363923};
DE Flags: Precursor;
OS Acanthoscurria paulensis (Brazilian giant black tarantula spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Acanthoscurria.
OX NCBI_TaxID=1264770;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=34363923; DOI=10.1016/j.peptides.2021.170622;
RA Tibery D.V., de Souza A.C.B., Mourao C.B.F., do Nascimento J.M.,
RA Schwartz E.F.;
RT "Purification and characterization of peptides Ap2, Ap3 and Ap5 (omega-
RT toxins) from the venom of the Brazilian tarantula Acanthoscurria
RT paulensis.";
RL Peptides 145:170622-170622(2021).
CC -!- FUNCTION: [Omega toxin Ap3]: Shows a weak inhibition on the voltage-
CC gated calcium channel Cav2.1/CACNA1A and some voltage-gated sodium
CC channels (with 1 uM toxin tested: 22.08% inhibition on Cav2.1/CACNA1A,
CC 6.6% on Nav1.1/SCN1A, 4.2% on Nav1.5, and 16% on Nav1.7).
CC {ECO:0000269|PubMed:34363923}.
CC -!- FUNCTION: [Omega toxin Ap5]: Shows a weak inhibition on the voltage-
CC gated calcium channel Cav2.1/CACNA1A (28.06% at 1 uM).
CC {ECO:0000269|PubMed:34363923}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34363923}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:34363923}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: [Omega toxin Ap3]: Mass=4883.7; Method=MALDI;
CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:34363923};
CC -!- MASS SPECTROMETRY: [Omega toxin Ap5]: Mass=5454.7; Method=MALDI;
CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:34363923};
CC -!- MISCELLANEOUS: [Omega toxin Ap3]: Does not show activity on
CC Cav1.2/CACNA1C, and Cav2.2/CACNA1B. {ECO:0000269|PubMed:34363923}.
CC -!- MISCELLANEOUS: [Omega toxin Ap5]: Does not show activity on
CC Nav1.1/SCN1A, Nav1.5/SCN5A, Nav1.7/SCN9A, Cav1.2/CACNA1C, and
CC Cav2.2/CACNA1B. {ECO:0000269|PubMed:34363923}.
CC -!- SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. 08 (Ltx-4)
CC subfamily. {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR012627; Toxin_22.
DR Pfam; PF08092; Toxin_22; 1.
PE 1: Evidence at protein level;
KW Calcium channel impairing toxin; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Secreted; Signal; Toxin; Voltage-gated calcium channel impairing toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..57
FT /evidence="ECO:0000305|PubMed:34363923"
FT /id="PRO_0000454753"
FT CHAIN 58..103
FT /note="Omega toxin Ap5"
FT /evidence="ECO:0000305|PubMed:34363923"
FT /id="PRO_0000454754"
FT CHAIN 58..98
FT /note="Omega toxin Ap3"
FT /evidence="ECO:0000305|PubMed:34363923"
FT /id="PRO_0000454755"
FT DISULFID 58..73
FT /evidence="ECO:0000305|PubMed:34363923"
FT DISULFID 65..78
FT /evidence="ECO:0000305|PubMed:34363923"
FT DISULFID 72..93
FT /evidence="ECO:0000305|PubMed:34363923"
SQ SEQUENCE 103 AA; 11834 MW; 4FB795BD7D629C76 CRC64;
MNTIQVILFA VVLVLTVTVG QADEDSAETS LLRKLEEAEA SMFGQYLEES KNSREKRCAV
ENVPCDKDRP GCCREYECLK PTGYGWWYGS YYCYKKKERL IST