CA11B_CONAH
ID CA11B_CONAH Reviewed; 64 AA.
AC P0CAQ5; A1X8B5; A3DT43; A6M932; A6M933;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Alpha-conotoxin-like Ac1.1b;
DE Flags: Precursor;
OS Conus achatinus (Little frog cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX NCBI_TaxID=369967;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Venom duct;
RX PubMed=17400270; DOI=10.1016/j.toxicon.2007.02.011;
RA Yuan D.-D., Han Y.-H., Wang C.-G., Chi C.-W.;
RT "From the identification of gene organization of alpha conotoxins to the
RT cloning of novel toxins.";
RL Toxicon 49:1135-1149(2007).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha3/5 pattern.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ359139; ABD48790.1; -; mRNA.
DR EMBL; DQ311055; ABD33847.1; -; Genomic_DNA.
DR AlphaFoldDB; P0CAQ5; -.
DR ConoServer; 545; Ac1.1b precursor.
DR ConoServer; 571; Ac1.1b precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR009958; Conotoxin_a-typ.
DR InterPro; IPR018072; Conotoxin_a-typ_CS.
DR Pfam; PF07365; Toxin_8; 1.
DR PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
PE 2: Evidence at transcript level;
KW Acetylcholine receptor inhibiting toxin; Amidation;
KW Cleavage on pair of basic residues; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..47
FT /evidence="ECO:0000250"
FT /id="PRO_0000376848"
FT PEPTIDE 48..62
FT /note="Alpha-conotoxin-like Ac1.1b"
FT /id="PRO_0000376849"
FT REGION 23..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Cysteine amide"
FT /evidence="ECO:0000250"
FT DISULFID 51..56
FT /evidence="ECO:0000250|UniProtKB:P01519"
FT DISULFID 52..62
FT /evidence="ECO:0000250|UniProtKB:P01519"
FT CONFLICT 9
FT /note="L -> V (in Ref. 1; ABD33847)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="F -> Y (in Ref. 1; ABD33847)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="K -> E (in Ref. 1; ABD33847)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 64 AA; 7181 MW; C4F719D02BF22F6E CRC64;
MGMRMMFTLF LLVVLTTTVV SFPSDSASDG RDDEAKDERS DMYKSKRNGR CCHPACGKHF
SCGR
