CLEC_CONAW
ID CLEC_CONAW Reviewed; 122 AA.
AC P84707; A0A3G1VU88;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Conotoxin flf14c {ECO:0000303|PubMed:16331958, ECO:0000303|PubMed:30040981};
DE AltName: Full=Conotoxin flf14.1 {ECO:0000303|PubMed:30040981};
DE Flags: Precursor;
OS Conus anabathrum floridanus (Florida cone) (Conus floridanus floridensis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Dauciconus.
OX NCBI_TaxID=1520082;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=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 96-122, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP 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=3280.4; Mass_error=0.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16331958};
CC -!- SIMILARITY: Belongs to the conotoxin R superfamily. {ECO:0000305}.
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DR EMBL; MH750030; AYK27403.1; -; mRNA.
DR AlphaFoldDB; P84707; -.
DR SMR; P84707; -.
DR ConoServer; 1497; FlfXIVC.
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 Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..96
FT /evidence="ECO:0000305"
FT /id="PRO_0000446989"
FT PEPTIDE 96..122
FT /note="Conotoxin flf14c"
FT /evidence="ECO:0000269|PubMed:16331958"
FT /id="PRO_0000044517"
FT REGION 53..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 101..121
FT /evidence="ECO:0000269|PubMed:16331958"
FT DISULFID 105..117
FT /evidence="ECO:0000269|PubMed:16331958"
SQ SEQUENCE 122 AA; 14192 MW; 739EAEB0896BA6D7 CRC64;
MGFRVLVLIV MVTTSALPFT FSEESGRSPF RPALRSEEAQ ALRHGLTLLL ARRADGQTPD
MHQPEMRRPE MRRPEVRRPE VRQPEFAESP VGQKRWDAYD CIQFCMRPEM RHTYAQCLSI
CT