CA1F_CONRE
ID CA1F_CONRE Reviewed; 13 AA.
AC P85012;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 23-FEB-2022, entry version 36.
DE RecName: Full=Alpha-conotoxin-like Reg1f {ECO:0000303|PubMed:17153339};
OS Conus regius (Crown cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Stephanoconus.
OX NCBI_TaxID=101314;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, HYDROXYLATION
RP AT PRO-7 AND PRO-8, AND AMIDATION AT CYS-13.
RC TISSUE=Venom;
RX PubMed=17153339; DOI=10.1007/978-3-540-30880-5_4;
RA Franco A., Pisarewicz K., Moller C., Mora D., Fields G.B., Mari F.;
RT "Hyperhydroxylation: a new strategy for neuronal targeting by venomous
RT marine molluscs.";
RL Prog. Mol. Subcell. Biol. 43:83-103(2006).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC {ECO:0000250|UniProtKB:P50983}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17153339}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000269|PubMed:17153339}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/3 pattern.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR ConoServer; 31; Reg1f.
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 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..13
FT /note="Alpha-conotoxin-like Reg1f"
FT /evidence="ECO:0000269|PubMed:17153339"
FT /id="PRO_0000259388"
FT MOD_RES 7
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:17153339"
FT MOD_RES 8
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:17153339"
FT MOD_RES 13
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:17153339"
FT DISULFID 3..9
FT /evidence="ECO:0000250|UniProtKB:P0C1D0"
FT DISULFID 4..13
FT /evidence="ECO:0000250|UniProtKB:P0C1D0"
SQ SEQUENCE 13 AA; 1543 MW; 73788AF087F37774 CRC64;
DYCCRRPPCT LIC
