O27A_CONTE
ID O27A_CONTE Reviewed; 76 AA.
AC P24160; Q9BPB5; Q9BPB6;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 3.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Gamma-conotoxin-like TxVIIA {ECO:0000303|PubMed:8868490};
DE AltName: Full=TxIIA {ECO:0000303|PubMed:1761058};
DE Flags: Precursor;
OS Conus textile (Cloth-of-gold cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX NCBI_TaxID=6494;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [2]
RP PROTEIN SEQUENCE OF 49-75, GAMMA-CARBOXYGLUTAMATION AT GLU-57 AND GLU-61,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=Neovicarius; TISSUE=Venom;
RX PubMed=1761058; DOI=10.1111/j.1432-1033.1991.tb16412.x;
RA Fainzilber M., Gordon D., Hasson A., Spira M.E., Zlotkin E.;
RT "Mollusc-specific toxins from the venom of Conus textile neovicarius.";
RL Eur. J. Biochem. 202:589-595(1991).
RN [3]
RP SEQUENCE REVISION TO 49; 75 AND 76, AMIDATION AT PHE-75, AND MASS
RP SPECTROMETRY.
RX PubMed=8868490; DOI=10.1002/pro.5560050315;
RA Nakamura T., Yu Z., Fainzilber M., Burlingame A.L.;
RT "Mass spectrometric-based revision of the structure of a cysteine-rich
RT peptide toxin with gamma-carboxyglutamic acid, TxVIIA, from the sea snail,
RT Conus textile.";
RL Protein Sci. 5:524-530(1996).
CC -!- FUNCTION: Gamma-conotoxins may act on voltage-gated non-specific cation
CC pacemaker channels (HCN) (By similarity). Potent neurotoxin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1761058}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:1761058}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=3088.9; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8868490};
CC -!- SIMILARITY: Belongs to the conotoxin O2 superfamily. {ECO:0000305}.
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DR EMBL; AF215019; AAG60447.1; -; mRNA.
DR EMBL; AF215020; AAG60448.1; -; mRNA.
DR PIR; A58175; A58175.
DR AlphaFoldDB; P24160; -.
DR ConoServer; 1517; TxVIIA.
DR ConoServer; 706; TxVIIA precursor.
DR ConoServer; 707; TxVIIA 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 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Gamma-carboxyglutamic acid; Ion channel impairing toxin;
KW Knottin; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..46
FT /evidence="ECO:0000269|PubMed:1761058"
FT /id="PRO_0000392713"
FT PEPTIDE 49..75
FT /note="Gamma-conotoxin-like TxVIIA"
FT /evidence="ECO:0000269|PubMed:1761058"
FT /id="PRO_0000044485"
FT MOD_RES 57
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:1761058"
FT MOD_RES 61
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:1761058"
FT MOD_RES 75
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:8868490"
FT DISULFID 49..63
FT /evidence="ECO:0000250"
FT DISULFID 56..67
FT /evidence="ECO:0000250"
FT DISULFID 62..72
FT /evidence="ECO:0000250"
FT CONFLICT 23..25
FT /note="Missing (in Ref. 1; AAG60448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 76 AA; 8529 MW; 197F229C146A475B CRC64;
MEKLTILLLV AAVLMSTQAM FQGDGEKSRK AEINFSETRK LARNKQKRCG GYSTYCEVDS
ECCSDNCVRS YCTLFG