CMAT_CONPO
ID CMAT_CONPO Reviewed; 14 AA.
AC P0C260;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 22-APR-2020, entry version 24.
DE RecName: Full=Conomap-Vt;
DE Short=Conp-Vt;
OS Conus planorbis (Planorbis cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Strategoconus.
OX NCBI_TaxID=97183;
RN [1]
RP PROTEIN SEQUENCE, SYNTHESIS, D-AMINO ACID AT PHE-2, AMIDATION AT TYR-14,
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=16797543; DOI=10.1016/j.febslet.2006.06.011;
RA Dutertre S., Lumsden N.G., Alewood P.F., Lewis R.J.;
RT "Isolation and characterisation of conomap-Vt, a D-amino acid containing
RT excitatory peptide from the venom of a vermivorous cone snail.";
RL FEBS Lett. 580:3860-3866(2006).
CC -!- FUNCTION: Is a potent and mollusk specific excitatory peptide. Most
CC potent excitatory effect are observed on the buccal mass. It interacts
CC with non-cholinergic receptors. As this peptide is a major component of
CC the venom, it may play an important role in prey capture.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16797543}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=1488.86; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:16797543};
CC -!- MISCELLANEOUS: The mature peptide does not contain cysteine residue.
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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; D-amino acid; Direct protein sequencing; Neurotoxin; Secreted;
KW Toxin.
FT PEPTIDE 1..14
FT /note="Conomap-Vt"
FT /id="PRO_0000262691"
FT MOD_RES 2
FT /note="D-phenylalanine"
FT /evidence="ECO:0000269|PubMed:16797543"
FT MOD_RES 14
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:16797543"
SQ SEQUENCE 14 AA; 1491 MW; C8D0B2081A5A13DD CRC64;
AFVKGSAQRV AHGY