TLCOA_ALOMR
ID TLCOA_ALOMR Reviewed; 87 AA.
AC P85079; A9XDF9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Omega-lycotoxin-Gsp2671a;
DE Short=Omega-LCTX-Gsp2671a;
DE AltName: Full=Lsp-1;
DE AltName: Full=Omega-Lsp-IA;
DE Flags: Precursor;
OS Alopecosa marikovskyi (Wolf spider) (Lycosa kazakhstanicus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Lycosoidea; Lycosidae; Alopecosa.
OX NCBI_TaxID=2066572;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 41-87, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY OF 41-87.
RC TISSUE=Venom, and Venom gland;
RX PubMed=17888477; DOI=10.1016/j.toxicon.2007.07.004;
RA Pluzhnikov K.A., Vassilevski A., Korolkova Y., Fisyunov A., Iegorova O.,
RA Krishtal O., Grishin E.;
RT "Omega-Lsp-IA, a novel modulator of P-type Ca(2+) channels.";
RL Toxicon 50:993-1004(2007).
RN [2]
RP FUNCTION.
RX PubMed=15590128; DOI=10.1016/j.tox.2004.09.005;
RA Fisyunov A., Pluzhnikov K.A., Molyavka A., Grishin E.V., Lozovaya N.,
RA Krishtal O.;
RT "Novel spider toxin slows down the activation kinetics of P-type Ca2+
RT channels in Purkinje neurons of rat.";
RL Toxicology 207:129-136(2005).
CC -!- FUNCTION: Modulates P-type voltage-gated calcium channels
CC (Cav2.1/CACNA1A) in rat cerebellar Purkinje cells and hippocampal CA1-
CC CA3 neurons. At saturating concentrations (>10 nM) the toxin
CC decelerates activation kinetics and slightly increases peak amplitude
CC without affecting deactivation kinetics. {ECO:0000269|PubMed:15590128,
CC ECO:0000269|PubMed:17888477}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17888477}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:17888477}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- PTM: Contains 4 disulfide bonds.
CC -!- MASS SPECTROMETRY: Mass=5623.7; Mass_error=0.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17888477};
CC -!- SIMILARITY: Belongs to the neurotoxin (omega-lctx) family.
CC {ECO:0000305}.
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DR EMBL; EF187331; ABP68825.1; -; mRNA.
DR AlphaFoldDB; P85079; -.
DR TCDB; 8.B.19.2.4; the sea anemone k+ channel blocker toxin, bcstx3 (bcstx3) family.
DR ArachnoServer; AS000625; omega-lycotoxin-Gsp2671a.
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.
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..17
FT /evidence="ECO:0000255"
FT PROPEP 18..40
FT /evidence="ECO:0000269|PubMed:17888477"
FT /id="PRO_0000388999"
FT CHAIN 41..87
FT /note="Omega-lycotoxin-Gsp2671a"
FT /id="PRO_0000306389"
FT DISULFID 44..59
FT /evidence="ECO:0000250"
FT DISULFID 51..64
FT /evidence="ECO:0000250"
FT DISULFID 58..84
FT /evidence="ECO:0000250"
FT DISULFID 66..82
FT /evidence="ECO:0000250"
SQ SEQUENCE 87 AA; 10298 MW; 2A82D8DA55B47603 CRC64;
MKLSIFFVLF FIAIAYCQPE FLDDEEDEVE ETLPVAEEGR EKSCITWRNS CMHNDKGCCF
PWSCVCWSQT VSRNSSRKEK KCQCRLW
