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CANA_CONIM
ID   CANA_CONIM              Reviewed;          72 AA.
AC   D0PX84;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Conotoxin im23a {ECO:0000303|PubMed:22399292};
DE   AltName: Full=Im23.1 {ECO:0000303|PubMed:22399292};
DE   AltName: Full=U1-CTX-Ci1a;
DE   Flags: Precursor;
OS   Conus imperialis (Imperial cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Stephanoconus.
OX   NCBI_TaxID=35631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, DISULFIDE
RP   BONDS, MASS SPECTROMETRY, STRUCTURE BY NMR, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=22399292; DOI=10.1074/jbc.m111.334615;
RA   Ye M., Khoo K.K., Xu S., Zhou M., Boonyalai N., Perugini M.A., Shao X.,
RA   Chi C., Galea C.A., Wang C., Norton R.S.;
RT   "A helical conotoxin from Conus imperialis has a novel cysteine framework
RT   and defines a new superfamily.";
RL   J. Biol. Chem. 287:14973-14983(2012).
CC   -!- FUNCTION: Neurotoxin that induces excitatory symptoms in mice following
CC       intracranial administration. No symptoms are observed after
CC       intraperitoneal and intravenous (tail vein) injections.
CC       {ECO:0000269|PubMed:22399292}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22399292}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:22399292}.
CC   -!- DOMAIN: The cysteine framework is XXIII (C-C-C-CC-C). {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=4823.0; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:22399292};
CC   -!- MISCELLANEOUS: Does not affect (up to 50 uM) the Nav1.7/SCN9A channel,
CC       Drosophila Shaker channel and rat KCa1.1/KCNMA1 channel expressed in
CC       HEK293 cell, as well as on whole cell current of neurons from neonatal
CC       rat hippocampus and prefrontal cortex. In addition, no detectable
CC       effect is observed on either action potential amplitude and duration or
CC       Na(+) and Ca(2+) current amplitude and kinetics when im23a is tested on
CC       action potentials and depolarization-activated Na(+) and Ca(2+)
CC       currents in rat DRG neurons (PubMed:22399292).
CC       {ECO:0000305|PubMed:22399292}.
CC   -!- SIMILARITY: Belongs to the conotoxin K superfamily. {ECO:0000305}.
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DR   EMBL; FJ375238; ACQ65998.1; -; mRNA.
DR   PDB; 2LMZ; NMR; -; A=31-72.
DR   PDBsum; 2LMZ; -.
DR   AlphaFoldDB; D0PX84; -.
DR   BMRB; D0PX84; -.
DR   SMR; D0PX84; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..28
FT                   /id="PRO_0000417032"
FT   CHAIN           31..72
FT                   /note="Conotoxin im23a"
FT                   /id="PRO_5000825649"
FT   DISULFID        34..41
FT                   /evidence="ECO:0000269|PubMed:22399292,
FT                   ECO:0000312|PDB:2LMZ"
FT   DISULFID        45..55
FT                   /evidence="ECO:0000269|PubMed:22399292,
FT                   ECO:0000312|PDB:2LMZ"
FT   DISULFID        56..71
FT                   /evidence="ECO:0000269|PubMed:22399292,
FT                   ECO:0000312|PDB:2LMZ"
FT   HELIX           38..47
FT                   /evidence="ECO:0007829|PDB:2LMZ"
FT   HELIX           52..61
FT                   /evidence="ECO:0007829|PDB:2LMZ"
FT   TURN            68..70
FT                   /evidence="ECO:0007829|PDB:2LMZ"
SQ   SEQUENCE   72 AA;  8040 MW;  F906BE740065B2C4 CRC64;
     MIMRMTLTLF VLVVMTAASA SGDALTEAKR IPYCGQTGAE CYSWCIKQDL SKDWCCDFVK
     DIRMNPPADK CP
 
 
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