O27A_CONPE
ID O27A_CONPE Reviewed; 80 AA.
AC P56711; Q9BPA8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Gamma-conotoxin PnVIIA;
DE AltName: Full=PnMEKL-011;
DE Flags: Precursor;
OS Conus pennaceus (Feathered cone) (Conus episcopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Darioconus.
OX NCBI_TaxID=37335;
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 46-77, FUNCTION, HYDROXYLATION AT PRO-76,
RP GAMMA-CARBOXYGLUTAMATION AT GLU-59 AND GLU-71, SUBCELLULAR LOCATION, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=9484216; DOI=10.1021/bi971571f;
RA Fainzilber M., Nakamura T., Lodder J.C., Zlotkin E., Kits K.S.,
RA Burlingame A.L.;
RT "Gamma-conotoxin-PnVIIA, a gamma-carboxyglutamate-containing peptide
RT agonist of neuronal pacemaker cation currents.";
RL Biochemistry 37:1470-1477(1998).
CC -!- FUNCTION: Gamma-conotoxins may act on voltage-gated non-specific cation
CC pacemaker channels (HCN). Triggers depolarization and firing of action
CC potential bursts in the caudodorsal neurons of lymnaea. This effect is
CC due to activation or enhancement of a slow inward cation current that
CC may underlie endogenous bursting activity of these neurons.
CC {ECO:0000269|PubMed:9484216}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9484216}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:9484216}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=3718.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9484216};
CC -!- SIMILARITY: Belongs to the conotoxin O2 superfamily. {ECO:0000305}.
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DR EMBL; AF215029; AAG60457.1; -; mRNA.
DR AlphaFoldDB; P56711; -.
DR SMR; P56711; -.
DR TCDB; 8.B.16.2.1; the maurocalcine (maca) family.
DR ConoServer; 1636; PnVIIA.
DR ConoServer; 716; PnVIIA 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 Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Gamma-carboxyglutamic acid; Hydroxylation;
KW Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..43
FT /evidence="ECO:0000305|PubMed:9484216"
FT /id="PRO_0000392707"
FT PEPTIDE 46..77
FT /note="Gamma-conotoxin PnVIIA"
FT /evidence="ECO:0000269|PubMed:9484216"
FT /id="PRO_0000044877"
FT PROPEP 78..80
FT /evidence="ECO:0000305|PubMed:9484216"
FT /id="PRO_0000392708"
FT MOD_RES 59
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:9484216"
FT MOD_RES 71
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:9484216"
FT MOD_RES 76
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:9484216"
FT DISULFID 47..61
FT /evidence="ECO:0000250"
FT DISULFID 54..65
FT /evidence="ECO:0000250"
FT DISULFID 60..70
FT /evidence="ECO:0000250"
SQ SEQUENCE 80 AA; 9189 MW; 758ACDD9692E18D7 CRC64;
MEKLTILLLV AAVLMSTQAQ NQEQRQQAKI NFLSKRKPSA ERWRRDCTSW FGRCTVNSEC
CSNSCDQTYC ELYAFPSFGA