ID   TU3A_UNEBI              Reviewed;          17 AA.
AC   C0HKK6;
DT   31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Turripeptide ubi3a {ECO:0000303|PubMed:29090914};
OS   Unedogemmula bisaya (Sea snail) (Lophiotoma bisaya).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Turridae; Unedogemmula.
OX   NCBI_TaxID=746885 {ECO:0000303|PubMed:29090914};
RN   [1] {ECO:0000305}
RP   STRUCTURE BY NMR OF 1-17, PROTEIN SEQUENCE, MASS SPECTROMETRY, FUNCTION,
RP   HYDROXYLATION AT PRO-4 AND PRO-6, AMIDATION AT CYS-17, AND DISULFIDE BOND.
RX   PubMed=29090914; DOI=10.1021/acs.biochem.7b00485;
RA   Omaga C.A., Carpio L.D., Imperial J.S., Daly N.L., Gajewiak J.,
RA   Flores M.S., Espino S.S., Christensen S., Filchakova O.M., Lopez-Vera E.,
RA   Raghuraman S., Olivera B.M., Concepcion G.P.;
RT   "Structure and Biological Activity of a Turripeptide from Unedogemmula
RT   bisaya Venom.";
RL   Biochemistry 56:6051-6060(2017).
CC   -!- FUNCTION: This toxin elicits excitatory activity in two subsets of the
CC       mouse dorsal root ganglion neurons; the medium diameter isolectin B4-
CC       expressing neurons and the small diameter CGRP-expressing neurons.
CC       Intracranial injection into mice causes strong tremors and impaired
CC       locomotion for around 3 hours after administration. Displays low
CC       inhibition of the human alpha-9-alpha-10 nAChR (IC(50)=10200 nM).
CC       {ECO:0000269|PubMed:29090914}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29090914}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:29090914}.
CC   -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC       3 branch, since 3 residues stand between the fourth and the fifth
CC       cysteine residues. This peptide has a cysteine scaffold similar to the
CC       M superfamily of conotoxins, but it displays a disulfide pattern
CC       previously unknown in native cone snail peptides.
CC       {ECO:0000305|PubMed:29090914}.
CC   -!- MASS SPECTROMETRY: Mass=1798.52; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29090914};
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DR   AlphaFoldDB; C0HKK6; -.
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; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..17
FT                   /note="Turripeptide ubi3a"
FT                   /evidence="ECO:0000269|PubMed:29090914"
FT                   /id="PRO_0000442850"
FT   MOD_RES         4
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:29090914"
FT   MOD_RES         6
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:29090914"
FT   MOD_RES         17
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:29090914"
FT   DISULFID        2..12
FT                   /evidence="ECO:0000269|PubMed:29090914"
FT   DISULFID        3..17
FT                   /evidence="ECO:0000269|PubMed:29090914"
FT   DISULFID        5..16
FT                   /evidence="ECO:0000269|PubMed:29090914"
SQ   SEQUENCE   17 AA;  1775 MW;  70CDB69996C4E6CF CRC64;
     DCCPCPAGAV RCRFACC