TOG1A_AGEAP
ID TOG1A_AGEAP Reviewed; 112 AA.
AC P15969;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Omega-agatoxin-1A;
DE AltName: Full=Omega-agatoxin IA;
DE Short=Omega-Aga-IA;
DE Contains:
DE RecName: Full=Omega-agatoxin-1A major chain;
DE Contains:
DE RecName: Full=Omega-agatoxin-1A minor chain;
DE Flags: Precursor;
OS Agelenopsis aperta (North American funnel-web spider) (Agelenopsis
OS gertschi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Agelenidae; Agelenopsis.
OX NCBI_TaxID=6908;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=1383207; DOI=10.1016/s0021-9258(19)36742-0;
RA Santos A.D., Imperial J.S., Chaudhary T., Beavis R.C., Chait B.T.,
RA Hunsperger J.P., Olivera B.M., Adams M.E., Hillyard D.R.;
RT "Heterodimeric structure of the spider toxin omega-agatoxin IA revealed by
RT precursor analysis and mass spectrometry.";
RL J. Biol. Chem. 267:20701-20705(1992).
RN [2]
RP PROTEIN SEQUENCE OF 37-102, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=2295621; DOI=10.1016/s0021-9258(19)40129-4;
RA Adams M.E., Bindokas V.P., Hasegawa L., Venema V.J.;
RT "Omega-agatoxins: novel calcium channel antagonists of two subtypes from
RT funnel web spider (Agelenopsis aperta) venom.";
RL J. Biol. Chem. 265:861-867(1990).
RN [3]
RP FUNCTION.
RX PubMed=1685511; DOI=10.1152/jn.1991.66.2.590;
RA Bindokas V.P., Venema V.J., Adams M.E.;
RT "Differential antagonism of transmitter release by subtypes of omega-
RT agatoxins.";
RL J. Neurophysiol. 66:590-601(1991).
CC -!- FUNCTION: Omega-agatoxins are antagonists of voltage-gated calcium
CC channels. They block insect neuromuscular transmission presynaptically.
CC This toxin is a blocker of L-type calcium channels (Cav/CACNA1).
CC {ECO:0000269|PubMed:1685511}.
CC -!- SUBUNIT: Heterodimer of two subunits, a major chain and a minor chain,
CC linked by a disulfide bond.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1383207,
CC ECO:0000269|PubMed:2295621}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:1383207, ECO:0000305|PubMed:2295621}.
CC -!- PTM: Proteolytically processed to yield the major and the minor chains.
CC -!- MASS SPECTROMETRY: Mass=7791.4; Method=Plasma desorption; Note=The
CC measured ranges are 37-102, 110-112.;
CC Evidence={ECO:0000269|PubMed:1383207};
CC -!- SIMILARITY: Belongs to the neurotoxin 04 (omega-agtx) family. 01 (type
CC I omega-agtx) subfamily. {ECO:0000305}.
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DR EMBL; M95540; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A45069; A45069.
DR AlphaFoldDB; P15969; -.
DR ArachnoServer; AS000175; omega-agatoxin-Aa1a.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR013605; Toxin_34.
DR Pfam; PF08396; Toxin_34; 1.
PE 1: Evidence at protein level;
KW Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Presynaptic neurotoxin; Secreted;
KW Signal; Toxin; Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..36
FT /evidence="ECO:0000269|PubMed:2295621"
FT /id="PRO_0000035486"
FT CHAIN 37..102
FT /note="Omega-agatoxin-1A major chain"
FT /evidence="ECO:0000269|PubMed:2295621"
FT /id="PRO_0000035487"
FT PROPEP 103..109
FT /note="Glu-rich"
FT /id="PRO_0000035488"
FT CHAIN 110..112
FT /note="Omega-agatoxin-1A minor chain"
FT /id="PRO_0000035489"
FT CONFLICT 101
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 112 AA; 12808 MW; ACC0ED776E49DF23 CRC64;
MMKFVVFLAC LFVAAHSFAV EGEEEYFEAE VPELERAKAL PPGSVCDGNE SDCKCYGKWH
KCRCPWKWHF TGEGPCTCEK GMKHTCITKL HCPNKAEWGL DWRSEESERS PC