ID   TX2_ACAPA               Reviewed;         100 AA.
AC   P0DV31;
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 Ap2 {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, SUBCELLULAR LOCATION, AND AMIDATION AT SER-99.
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: Inhibits 31.17% of Cav2.1/CACNA1A current at 1 uM
CC       concentration. {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: Mass=4886.3; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:34363923};
CC   -!- MISCELLANEOUS: Does not show activity on Nav1.1/SCN1A, Nav1.5/SCN5A,
CC       Nav1.7/SCN9A, Cav1.2/CACNA1C, and Cav2.2/CACNA1B.
CC       {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   Amidation; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..57
FT                   /evidence="ECO:0000305|PubMed:34363923"
FT                   /id="PRO_0000454751"
FT   CHAIN           58..99
FT                   /note="Omega toxin Ap2"
FT                   /evidence="ECO:0000305|PubMed:34363923"
FT                   /id="PRO_0000454752"
FT   MOD_RES         99
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000269|PubMed:34363923"
FT   DISULFID        58..74
FT                   /evidence="ECO:0000305|PubMed:34363923"
FT   DISULFID        65..79
FT                   /evidence="ECO:0000305|PubMed:34363923"
FT   DISULFID        73..94
FT                   /evidence="ECO:0000305|PubMed:34363923"
SQ   SEQUENCE   100 AA;  11253 MW;  AE34CD5F4C37AD70 CRC64;
     MNTTQVILFA VVLVLTVTVG QADEDSAETS LLRKLEEAEA SMFGQYLEES KNSPEQRCAG
     ENVPCDKDRP GDCCSRYECL KPTGYGWWYA SYYCYKKKSG