ID   O27A_CONPG              Reviewed;          25 AA.
AC   P0DOW6;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-JAN-2017, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Gamma-conotoxin PiVIIA {ECO:0000303|PubMed:26861393};
OS   Conus princeps (Prince cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Ductoconus.
OX   NCBI_TaxID=101311;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, HYDROXYLATION AT PRO-4,
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-13 AND GLU-20, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=26861393; DOI=10.3390/toxins8020039;
RA   Bernaldez J., Jimenez S., Gonzalez L.J., Ferro J.N., Soto E., Salceda E.,
RA   Chavez D., Aguilar M.B., Licea-Navarro A.;
RT   "A new member of gamma-conotoxin family isolated from Conus princeps
RT   displays a novel molecular target.";
RL   Toxins 8:1-18(2016).
CC   -!- FUNCTION: Micromolar concentrations of PiVIIA increase the magnitude of
CC       the macroscopic calcium current in DRG neurons from rat. An increase,
CC       even modest of the calcium current, may have a significant impact in
CC       the excitability and electrical activity of neurons, and may set up
CC       PiVIIA as a member of the pharmacological family of the gamma-
CC       conotoxins. {ECO:0000250|UniProtKB:P56711,
CC       ECO:0000269|PubMed:26861393}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26861393}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
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=3094.95; Method=Electrospray; Note=Monoisotopic
CC       mass.; Evidence={ECO:0000269|PubMed:26861393};
CC   -!- MISCELLANEOUS: Does not modify sodium, potassium and acid sensing ionic
CC       channel (ASIC) currents. {ECO:0000269|PubMed:26861393}.
CC   -!- SIMILARITY: Belongs to the conotoxin O2 superfamily.
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DR   AlphaFoldDB; P0DOW6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Hydroxylation; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..25
FT                   /note="Gamma-conotoxin PiVIIA"
FT                   /evidence="ECO:0000269|PubMed:26861393"
FT                   /id="PRO_0000438813"
FT   MOD_RES         4
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:26861393"
FT   MOD_RES         13
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:26861393"
FT   MOD_RES         20
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:26861393"
FT   DISULFID        1..15
FT                   /evidence="ECO:0000250"
FT   DISULFID        8..19
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..24
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   25 AA;  2999 MW;  0B415AABF05447FC CRC64;
     CDAPTHYCTN YWECCSGYCE HSHCW