ID   CT5A_CONCN              Reviewed;          14 AA.
AC   P0DJL6;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2013, sequence version 1.
DT   29-SEP-2021, entry version 16.
DE   RecName: Full=Tau-conotoxin CnVA {ECO:0000305|PubMed:23567999};
DE   AltName: Full=Tau-CnVA {ECO:0000303|PubMed:23567999};
OS   Conus consors (Singed cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=101297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS, FUNCTION, STRUCTURE BY NMR OF THE
RP   SYNTHETIC PEPTIDE, AND AMIDATION AT VAL-14.
RC   TISSUE=Venom duct;
RX   PubMed=23567999; DOI=10.1016/j.bcp.2013.03.019;
RA   Petrel C., Hocking H.G., Reynaud M., Upert G., Favreau P., Biass D.,
RA   Paolini-Bertrand M., Peigneur S., Tytgat J., Gilles N., Hartley O.,
RA   Boelens R., Stocklin R., Servent D.;
RT   "Identification, structural and pharmacological characterization of tau-
RT   CnVA, a conopeptide that selectively interacts with somatostatin sst
RT   receptor.";
RL   Biochem. Pharmacol. 85:1663-1671(2013).
CC   -!- FUNCTION: Interacts selectively with the G-coupled somatostatin sst3
CC       receptor (SSTR3). It displays antagonist property for SSTR3 (Ki=1.5
CC       uM). Other somatostatin receptors are also affected, but with a lower
CC       selectivity: SSTR5 (Ki=80.2 uM), SSTR1 (Ki=169 uM), SSTR2 (KI=159 uM),
CC       SSTR4 (Ki>100 uM). {ECO:0000269|PubMed:23567999}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23567999}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:23567999}.
CC   -!- DOMAIN: The cysteine framework is V (CC-CC). {ECO:0000305}.
CC   -!- PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or
CC       'C1-C4, C2-C3', since these disulfide connectivities have been observed
CC       for conotoxins with cysteine framework V (for examples, see AC P0DQQ7
CC       and AC P81755). {ECO:0000305}.
CC   -!- MISCELLANEOUS: 5-10 uM of the toxin does not have activity on 30
CC       different class A receptors of GPCR, voltage-gated sodium channels
CC       (Nav1.2, 1.3, 1.4, 1.5, 1.6, 1.8 and the insect channel BgNaV1),
CC       voltage-gated potassium channels (Kv1.1, 1.2, 1.3, 1.4 1.5, 1.6, Kv2.1,
CC       hERG and the insect channel Shaker IR), muscular and neuronal nicotinic
CC       acetylcholine receptors (4 subtypes) and neurotransmitter transporters
CC       (3 subfamilies). {ECO:0000305|PubMed:23567999}.
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
CC   -!- CAUTION: Due to the lack of the signal sequence, the classification of
CC       this peptide as a T-superfamily member is not definitively established.
CC       {ECO:0000305}.
CC   -!- CAUTION: According to established conopeptide and toxin nomenclature,
CC       Greek letters are used to indicate pharmacological targets of toxins.
CC       The Greek letter 'tau' has already been attributed to toxins that
CC       target transient receptor potential (TRP) channels which is why it is
CC       indicated here only as an alternative name (PubMed:18619481).
CC       {ECO:0000305}.
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DR   SMR; P0DJL6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Disulfide bond; G-protein coupled receptor impairing toxin;
KW   Secreted; Toxin.
FT   PEPTIDE         1..14
FT                   /note="Tau-conotoxin CnVA"
FT                   /evidence="ECO:0000305|PubMed:23567999"
FT                   /id="PRO_0000422696"
FT   MOD_RES         14
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000305|PubMed:23567999"
SQ   SEQUENCE   14 AA;  1723 MW;  5ADB153DF364A627 CRC64;
     ECCHRQLLCC LRFV