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O163_CONAA
ID   O163_CONAA              Reviewed;          76 AA.
AC   A0A3G3C7S6;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Conotoxin Am6.3 {ECO:0000305};
DE   Flags: Precursor;
OS   Conus amadis (Amadis cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Leptoconus.
OX   NCBI_TaxID=198732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-76, SUBCELLULAR
RP   LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=30593932; DOI=10.1016/j.jprot.2018.12.028;
RA   Vijayasarathy M., Balaram P.;
RT   "Cone snail prolyl-4-hydroxylase alpha-subunit sequences derived from
RT   transcriptomic data and mass spectrometric analysis of variable proline
RT   hydroxylation in C. amadis venom.";
RL   J. Proteomics 194:37-48(2019).
CC   -!- FUNCTION: Probable toxin that inhibits ion channels. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30593932}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:30593932}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- PTM: Is not hydroxylated. {ECO:0000269|PubMed:30593932}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   EMBL; MH282823; AYP73030.1; -; mRNA.
DR   SMR; A0A3G3C7S6; -.
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   InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR   Pfam; PF02950; Conotoxin; 1.
DR   PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Knottin; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..76
FT                   /note="Conotoxin Am6.3"
FT                   /evidence="ECO:0000269|PubMed:30593932"
FT                   /id="PRO_5018290338"
FT   DISULFID        52..67
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        59..71
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        66..75
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   76 AA;  8452 MW;  35D1278373F25788 CRC64;
     MKLTCMMIIA VLFLTAWTFA TADDSGNGLE NLFSKAHHEM KNPEASKLNK RCLAKGDFCN
     LITQDCCDGI CFIFCP
 
 
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