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CM31_CONAE
ID   CM31_CONAE              Reviewed;          67 AA.
AC   Q9BPH3;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Conotoxin ArMLKM-01;
DE   Flags: Precursor;
OS   Conus arenatus (Sand-dusted cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
OX   NCBI_TaxID=89451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA   Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT   "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL   Mol. Biol. Evol. 18:120-131(2001).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:11158371}.
CC   -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC       1 branch, since 1 residue stands between the fourth and the fifth
CC       cysteine residues. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; AF214952; AAG60380.1; -; mRNA.
DR   AlphaFoldDB; Q9BPH3; -.
DR   ConoServer; 639; Ar3.1 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   Pfam; PF02950; Conotoxin; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..51
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000404876"
FT   PEPTIDE         54..67
FT                   /note="Conotoxin ArMLKM-01"
FT                   /id="PRO_0000404877"
FT   DISULFID        54..65
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        55..63
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        58..66
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
SQ   SEQUENCE   67 AA;  7770 MW;  E51BC34A0EB8CDDF CRC64;
     MLKMEVVLFT FLVLFPLSTL QLETDQPVER YVENKQDLNP DESRNFMLPI VKKCCTACRM
     PPCKCCA
 
 
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