3NX1_MICMP
ID 3NX1_MICMP Reviewed; 64 AA.
AC C0HJR1;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Micrurotoxin 1 {ECO:0000303|PubMed:25675485};
DE Short=MmTX1 {ECO:0000303|PubMed:25675485};
OS Micrurus mipartitus (Red-tailed coral snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=430902;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, MASS
RP SPECTROMETRY, TOXIC DOSE, AND BIOASSAY.
RC TISSUE=Venom;
RX PubMed=25675485; DOI=10.1073/pnas.1415488112;
RA Rosso J.P., Schwarz J.R., Diaz-Bustamante M., Ceard B., Gutierrez J.M.,
RA Kneussel M., Pongs O., Bosmans F., Bougis P.E.;
RT "MmTX1 and MmTX2 from coral snake venom potently modulate GABAA receptor
RT activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E891-900(2015).
CC -!- FUNCTION: Allosteric modulator of the GABA(A) receptor (GABR), possibly
CC increasing receptor affinity for the agonist, thus enhancing receptor
CC opening and macroscopic desensitization. In vivo,
CC intracerebroventricular injection into mice results in periods of
CC reduced basal activity, followed by bursts of intense seizures and
CC death. {ECO:0000269|PubMed:25675485}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25675485}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:25675485}.
CC -!- MASS SPECTROMETRY: Mass=7205; Mass_error=1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:25675485};
CC -!- TOXIC DOSE: LD(50) is 0.013-0.027 mg/kg by intracerebroventricular
CC injection into mice. {ECO:0000269|PubMed:25675485}.
CC -!- MISCELLANEOUS: Does not bind to nicotinic acetylcholine receptors
CC (nAChR), muscarinic acetylcholine receptors (mAChR),
CC acetylcholinesterase (AChE) or to receptors for glycine and glutamate.
CC {ECO:0000250|UniProtKB:C0HJR2}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HJR1; -.
DR SMR; C0HJR1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00206; snake_toxin; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR003571; Snake_3FTx.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
KW Chloride channel impairing toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Toxin.
FT CHAIN 1..64
FT /note="Micrurotoxin 1"
FT /evidence="ECO:0000269|PubMed:25675485"
FT /id="PRO_0000432830"
FT DISULFID 3..24
FT /evidence="ECO:0000250|UniProtKB:P81783"
FT DISULFID 6..11
FT /evidence="ECO:0000250|UniProtKB:P81783"
FT DISULFID 17..41
FT /evidence="ECO:0000250|UniProtKB:P81783"
FT DISULFID 45..57
FT /evidence="ECO:0000250|UniProtKB:P81783"
FT DISULFID 58..63
FT /evidence="ECO:0000250|UniProtKB:P81783"
SQ SEQUENCE 64 AA; 7215 MW; DE19370213C67AB1 CRC64;
LTCKTCPFTT CPNSESCPGG QSICYQRKWE EHRGERIERR CVANCPAFGS HDTSLLCCTR
DNCN