位置:首页 > 蛋白库 > CA1A_CONVR
CA1A_CONVR
ID   CA1A_CONVR              Reviewed;          62 AA.
AC   F5C0A0;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Alpha-conotoxin ViIA {ECO:0000303|PubMed:26511093};
DE   AltName: Full=ViIA-II {ECO:0000303|PubMed:26511093};
DE   Flags: Precursor;
OS   Conus virgo (Virgin cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Virgiconus.
OX   NCBI_TaxID=89427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 46-61, MUTAGENESIS OF ARG-46;
RP   ASP-47; HIS-56 AND CYS-61, AND DISULFIDE BOND.
RC   TISSUE=Venom duct;
RX   PubMed=26511093; DOI=10.1093/abbs/gmv105;
RA   Li L., Liu N., Ding R., Wang S., Liu Z., Li H., Zheng X., Dai Q.;
RT   "A novel 4/6-type alpha-conotoxin ViIA selectively inhibits nAchR
RT   alpha3beta2 subtype.";
RL   Acta Biochim. Biophys. Sin. 47:1023-1028(2015).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC       This toxin selectively inhibits nicotinic acetylcholine receptor
CC       (nAChR) alpha-3-beta-2 subtype (IC(50)=845.5 nM).
CC       {ECO:0000269|PubMed:26511093}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26511093}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:26511093}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/6 pattern.
CC       {ECO:0000305|PubMed:26511093}.
CC   -!- PTM: The toxin is inactive on the alpha-3-beta-2 nAChR when the
CC       disulfide bond connectivity is C1-C4 and C2-C3 (ViIA-I) (IC(50)>10000
CC       nM). {ECO:0000269|PubMed:26511093}.
CC   -!- MISCELLANEOUS: This toxin does not inhibit alpha-2-beta-2, alpha-2-
CC       beta-4, alpha-3-beta-4, alpha-4-beta-2, alpha-4-beta-4, alpha-7 and
CC       alpha-9-alpha-10 (PubMed:26511093). In addition, it does not target
CC       dorsal root ganglion sodium (Nav), potassium (Kv) and calcium (Cav) ion
CC       channels (PubMed:26511093). {ECO:0000269|PubMed:26511093}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily.
CC       {ECO:0000305|PubMed:26511093}.
CC   -!- CAUTION: Authors of PubMed:26511093 indicate an amidation at Cys-61.
CC       This amidation is improbable since no Gly follows the mature peptide
CC       region. This PTM is therefore not indicated here and we assume that
CC       electrophysiological results are obtained with an unamidated synthetic
CC       peptide. {ECO:0000305|PubMed:26511093}.
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; JF436964; ADZ99320.1; -; mRNA.
DR   AlphaFoldDB; F5C0A0; -.
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: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   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..45
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000439627"
FT   PEPTIDE         46..61
FT                   /note="Alpha-conotoxin ViIA"
FT                   /evidence="ECO:0000305|PubMed:26511093"
FT                   /id="PRO_5003322255"
FT   DISULFID        48..54
FT                   /evidence="ECO:0000305|PubMed:26511093"
FT   DISULFID        49..61
FT                   /evidence="ECO:0000305|PubMed:26511093"
FT   MUTAGEN         46
FT                   /note="R->A: 1.6-fold more potent in inhibition of rat
FT                   alpha-3-beta-2 nAChR."
FT                   /evidence="ECO:0000269|PubMed:26511093"
FT   MUTAGEN         47
FT                   /note="D->A: No change in inhibition of rat alpha-3-beta-2
FT                   nAChR."
FT                   /evidence="ECO:0000269|PubMed:26511093"
FT   MUTAGEN         56
FT                   /note="H->A: Complete loss of effect on rat alpha-3-beta-2
FT                   nAChR."
FT                   /evidence="ECO:0000269|PubMed:26511093"
FT   MUTAGEN         61
FT                   /note="C->CL: 13.6-fold more potent in inhibition of rat
FT                   alpha-3-beta-2 nAChR."
FT                   /evidence="ECO:0000269|PubMed:26511093"
SQ   SEQUENCE   62 AA;  6810 MW;  AE9764FFD3813190 CRC64;
     MGMRMMFVVF LLVVFASSVT LDRASYGRYA SPVDRASALI AQAILRDCCS NPPCAHNNPD
     CR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024