CLEA_CONVL
ID CLEA_CONVL Reviewed; 117 AA.
AC P84704; A0A3G1VU89;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Conotoxin vil14a {ECO:0000303|PubMed:16331958, ECO:0000303|PubMed:30040981};
DE AltName: Full=Conotoxin vil14.1 {ECO:0000303|PubMed:30040981};
DE Flags: Precursor;
OS Conus villepinii (Villepin's cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Dauciconus.
OX NCBI_TaxID=257347;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], STRUCTURE BY NMR OF 91-117, DISULFIDE BOND, AND
RP SYNTHESIS OF 91-117.
RC TISSUE=Venom, and Venom duct;
RX PubMed=30040981; DOI=10.1016/j.peptides.2018.06.002;
RA Moeller C., Dovell S., Melaun C., Mari F.;
RT "Definition of the R-superfamily of conotoxins: structural convergence of
RT helix-loop-helix peptidic scaffolds.";
RL Peptides 107:75-82(2018).
RN [2]
RP PROTEIN SEQUENCE OF 91-117, FUNCTION, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=16331958; DOI=10.1021/bi0511181;
RA Moller C., Rahmankhah S., Lauer-Fields J., Bubis J., Fields G.B., Mari F.;
RT "A novel conotoxin framework with a helix-loop-helix (Cs alpha/alpha)
RT fold.";
RL Biochemistry 44:15986-15996(2005).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16331958}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:16331958}.
CC -!- DOMAIN: The cysteine framework is XIV (C-C-C-C). {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=2872.5; Mass_error=0.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16331958};
CC -!- MISCELLANEOUS: Very weakly inhibits potassium channels in PC12 cells.
CC Very weekly and reversibly inhibits Kv1.3/KCNA3 in HEK293 cells
CC (Ki=12.1 uM). Does not inhibit Kv1.1/KCNA1, Kv1.2/KCNA2 and Kv1.3/KCNA3
CC when expressed in oocytes (tested at 10 uM).
CC {ECO:0000269|PubMed:30040981}.
CC -!- SIMILARITY: Belongs to the conotoxin R superfamily. {ECO:0000305}.
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DR EMBL; MH750032; AYK27405.1; -; mRNA.
DR PDB; 6EFE; NMR; -; A=91-117.
DR PDBsum; 6EFE; -.
DR AlphaFoldDB; P84704; -.
DR SMR; P84704; -.
DR ConoServer; 1619; VilXIVA.
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 3D-structure; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Neurotoxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..90
FT /evidence="ECO:0000305"
FT /id="PRO_0000446988"
FT PEPTIDE 91..117
FT /note="Conotoxin vil14a"
FT /evidence="ECO:0000269|PubMed:16331958"
FT /id="PRO_0000044484"
FT REGION 53..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 96..116
FT /evidence="ECO:0000269|PubMed:16331958,
FT ECO:0000269|PubMed:30040981, ECO:0000312|PDB:6EFE"
FT DISULFID 100..112
FT /evidence="ECO:0000269|PubMed:16331958,
FT ECO:0000269|PubMed:30040981, ECO:0000312|PDB:6EFE"
FT CONFLICT 71
FT /note="M -> V (in Ref. 1; AYK27405)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="Missing (in Ref. 1; AYK27405 and 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:6EFE"
FT TURN 110..115
FT /evidence="ECO:0007829|PDB:6EFE"
SQ SEQUENCE 117 AA; 13143 MW; 6589C3C8D80A3FE1 CRC64;
MGFRVLVLVV MATTSALPFT FSEEPGRSPF RPALRSEEAQ ALRHGLTLLL ARRADGQPPD
MRQPEMRRPE MRRPEVRQPE FAETPVGQKR GGLGRCIYNC MNSGGGLSFI QCKTMCY
