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CA168_CONPO
ID   CA168_CONPO             Reviewed;          62 AA.
AC   D9IWN7;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   23-FEB-2022, entry version 28.
DE   RecName: Full=Conotoxin Pl168 {ECO:0000303|PubMed:32443665};
DE   AltName: Full=Alpha-conotoxin Vt1.24 {ECO:0000312|EMBL:ADJ67510.1};
DE   Flags: Precursor;
OS   Conus planorbis (Planorbis cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Strategoconus.
OX   NCBI_TaxID=97183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sun T., Liu Z., Dai Q.;
RT   "A new alpha-conotoxin Vt1.24 precursor.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-62, PROTEIN SEQUENCE OF 41-62,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=26506909; DOI=10.1002/pmic.201500220;
RA   Jin A.H., Vetter I., Himaya S.W., Alewood P.F., Lewis R.J., Dutertre S.;
RT   "Transcriptome and proteome of Conus planorbis identify the nicotinic
RT   receptors as primary target for the defensive venom.";
RL   Proteomics 15:4030-4040(2015).
RN   [3]
RP   FUNCTION, SYNTHESIS OF 41-62, AND STRUCTURE BY NMR OF 41-62.
RX   PubMed=32443665; DOI=10.3390/biomedicines8050128;
RA   Wilson D.T., Bansal P.S., Carter D.A., Vetter I., Nicke A., Dutertre S.,
RA   Daly N.L.;
RT   "Characterisation of a novel A-superfamily conotoxin.";
RL   Biomedicines 8:0-0(2020).
CC   -!- FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion
CC       channels. {ECO:0000305|PubMed:32443665}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26506909}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:26506909}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/8 pattern.
CC       {ECO:0000305}.
CC   -!- PTM: Both Pro-53 and Pro-62 are not in cis/trans isomerization.
CC       {ECO:0000305|PubMed:32443665}.
CC   -!- MISCELLANEOUS: Does not show activity on a range of nAChRs (alpha-3-
CC       beta-2/CHRNA3-CHRNB2, alpha-4-beta-2/CHRNA4-CHRNB2, and alpha-
CC       7/CHRNA7), calcium and sodium channels. {ECO:0000305|PubMed:32443665}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
CC   -!- CAUTION: Shows a different disulfide-stabilized fold, despite
CC       containing the conserved cysteine framework and disulfide connectivity
CC       of classical alpha-conotoxins. {ECO:0000305|PubMed:32443665}.
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DR   EMBL; HM211181; ADJ67510.1; -; mRNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:InterPro.
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   Pfam; PF07365; Toxin_8; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..40
FT                   /evidence="ECO:0000305|PubMed:32443665"
FT                   /id="PRO_0000453213"
FT   PEPTIDE         41..62
FT                   /note="Conotoxin Pl168"
FT                   /evidence="ECO:0000269|PubMed:26506909"
FT                   /id="PRO_5003125753"
FT   DISULFID        46..52
FT                   /evidence="ECO:0000305|PubMed:32443665"
FT   DISULFID        47..61
FT                   /evidence="ECO:0000305|PubMed:32443665"
SQ   SEQUENCE   62 AA;  6829 MW;  5F7F8A8A843028FA CRC64;
     MGMRMMFTVF LLVVLATTVV SFTLDRASDG ANAAADLVAR GIRGNCCMFH TCPIDYSRFY
     CP
 
 
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