CM3F_CONPU
ID CM3F_CONPU Reviewed; 24 AA.
AC P60245;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Psi-conotoxin PIIIF;
OS Conus purpurascens (Purple cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Chelyconus.
OX NCBI_TaxID=41690;
RN [1]
RP PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, MASS SPECTROMETRY, STRUCTURE BY NMR,
RP HYDROXYLATION AT PRO-2; PRO-3 AND PRO-14, AMIDATION AT LYS-24, DISULFIDE
RP BONDS, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=12767216; DOI=10.1021/bi0272757;
RA Van Wagoner R.M., Jacobsen R.B., Olivera B.M., Ireland C.M.;
RT "Characterization and three-dimensional structure determination of psi-
RT conotoxin PIIIF, a novel noncompetitive antagonist of nicotinic
RT acetylcholine receptors.";
RL Biochemistry 42:6353-6362(2003).
CC -!- FUNCTION: Psi-conotoxins act on postsynaptic membranes, and act as non-
CC competitive antagonist of nicotinic acetylcholine receptors (nAChR). Is
CC less toxic than Psi-conotoxin PIIIE. {ECO:0000269|PubMed:12767216}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12767216}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:12767216}.
CC -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC 4 branch, since 4 residues stand between the fourth and the fifth
CC cysteine residues. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=2667.68; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12767216};
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR PDB; 1JLP; NMR; -; A=1-24.
DR PDBsum; 1JLP; -.
DR AlphaFoldDB; P60245; -.
DR SMR; P60245; -.
DR ConoServer; 1594; PIIIF.
DR EvolutionaryTrace; P60245; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
KW Direct protein sequencing; Disulfide bond; Hydroxylation;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Toxin.
FT PEPTIDE 1..24
FT /note="Psi-conotoxin PIIIF"
FT /evidence="ECO:0000269|PubMed:12767216"
FT /id="PRO_0000044498"
FT MOD_RES 2
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12767216"
FT MOD_RES 3
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12767216"
FT MOD_RES 14
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12767216"
FT MOD_RES 24
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:12767216"
FT DISULFID 4..16
FT /evidence="ECO:0000269|PubMed:12767216,
FT ECO:0007744|PDB:1JLP"
FT DISULFID 5..21
FT /evidence="ECO:0000269|PubMed:12767216,
FT ECO:0007744|PDB:1JLP"
FT DISULFID 10..22
FT /evidence="ECO:0000269|PubMed:12767216,
FT ECO:0007744|PDB:1JLP"
FT TURN 14..18
FT /evidence="ECO:0007829|PDB:1JLP"
SQ SEQUENCE 24 AA; 2609 MW; 6DE39416A9308C8A CRC64;
GPPCCLYGSC RPFPGCYNAL CCRK