TXO1A_PELMU
ID TXO1A_PELMU Reviewed; 84 AA.
AC D5J6X1; D5J6X4;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Omega-theraphotoxin-Pm1a {ECO:0000305};
DE Short=Omega-TRTX-Pm1a {ECO:0000305};
DE AltName: Full=Omega-theraphotoxin-Cc1a {ECO:0000303|PubMed:24561180};
DE Short=Omega-TRTX-Cc1a {ECO:0000303|PubMed:24561180};
DE AltName: Full=Toxin-like GVDKE {ECO:0000303|PubMed:20372963};
DE Flags: Precursor;
OS Pelinobius muticus (King baboon spider) (Citharischius crawshayi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Pelinobius.
OX NCBI_TaxID=753628;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=20372963; DOI=10.1007/s00018-010-0359-x;
RA Diego-Garcia E., Peigneur S., Waelkens E., Debaveye S., Tytgat J.;
RT "Venom components from Citharischius crawshayi spider (Family
RT Theraphosidae): exploring transcriptome, venomics, and function.";
RL Cell. Mol. Life Sci. 67:2799-2813(2010).
RN [2]
RP PROTEIN SEQUENCE OF 46-84, MASS SPECTROMETRY, FUNCTION, SYNTHESIS OF 46-84,
RP MUTAGENESIS OF 46-GLY--GLU-50 AND 80-TRP--VAL-84, SUBCELLULAR LOCATION, AND
RP DOMAIN.
RC TISSUE=Venom;
RX PubMed=24561180; DOI=10.1016/j.bcp.2014.02.008;
RA Klint J.K., Berecki G., Durek T., Mobli M., Knapp O., King G.F.,
RA Adams D.J., Alewood P.F., Rash L.D.;
RT "Isolation, synthesis and characterization of omega-TRTX-Cc1a, a novel
RT tarantula venom peptide that selectively targets L-type Cav channels.";
RL Biochem. Pharmacol. 89:276-286(2014).
CC -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC block voltage-gated calcium channels (Cav). This toxin inhibits barium
CC currents (IBa) mediated by L-type voltage-gated calcium channels
CC Cav1.2/CACNA1C (IC(50)=825 nM) and Cav1.3/CACNA1C (IC(50)=2240 nM)
CC (PubMed:24561180). {ECO:0000269|PubMed:24561180}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20372963,
CC ECO:0000269|PubMed:24561180}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000269|PubMed:24561180}.
CC -!- MASS SPECTROMETRY: Mass=4267.85; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20372963};
CC -!- MASS SPECTROMETRY: Mass=4266.27; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:24561180};
CC -!- MISCELLANEOUS: This toxin exhibits weak activity on Nav1.5/SCN5A and
CC Nav1.7/SCN9A voltage-gated sodium channel (at 3 uM, reduces by 39% and
CC 17% the peak amplitude and slows inactivation) (PubMed:24561180). In
CC addition, this toxin shows a little inhibition on Cav2.2/CACNA1B (20%
CC at 3 uM), but does not inhibit Cav2.1/CACNA1A and Cav2.3/CACNA1E
CC (PubMed:24561180). {ECO:0000269|PubMed:24561180}.
CC -!- MISCELLANEOUS: This toxin exists as two stable, slowly interconverting
CC isomers. {ECO:0000269|PubMed:24561180}.
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 41 (Jztx-36)
CC subfamily. {ECO:0000305}.
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DR EMBL; GU170866; ADF28492.1; -; mRNA.
DR EMBL; GU170867; ADF28493.1; -; mRNA.
DR EMBL; GU170868; ADF28494.1; -; mRNA.
DR EMBL; GU170869; ADF28495.1; -; mRNA.
DR AlphaFoldDB; D5J6X1; -.
DR SMR; D5J6X1; -.
DR ArachnoServer; AS001640; U1-theraphotoxin-Pm1a.
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:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR011696; Huwentoxin-1.
DR Pfam; PF07740; Toxin_12; 1.
PE 1: Evidence at protein level;
KW Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..45
FT /evidence="ECO:0000269|PubMed:20372963"
FT /id="PRO_0000431733"
FT CHAIN 46..84
FT /note="Omega-theraphotoxin-Pm1a"
FT /evidence="ECO:0000269|PubMed:24561180"
FT /id="PRO_0000431734"
FT DISULFID 52..66
FT /evidence="ECO:0000250|UniProtKB:B1P1E3"
FT DISULFID 59..71
FT /evidence="ECO:0000250|UniProtKB:B1P1E3"
FT DISULFID 65..78
FT /evidence="ECO:0000250|UniProtKB:B1P1E3"
FT MUTAGEN 46..50
FT /note="Missing: Small decrease in inhibition of
FT Cav1.2/CACNA1C."
FT /evidence="ECO:0000269|PubMed:24561180"
FT MUTAGEN 80..84
FT /note="Missing: Important decrease in inhibition of
FT Cav1.2/CACNA1C."
FT /evidence="ECO:0000269|PubMed:24561180"
FT CONFLICT 36
FT /note="V -> A (in Ref. 1; ADF28495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 84 AA; 9195 MW; EA9CA26A985C66DB CRC64;
MKTSMLAVFV ALPLAFVLTA ATEERAHPNE LVNSLVELVK LDAERGVDKE GCKYMFGSCG
KSDDCCPKLA CKRTFNYCAW DGSV
