CT51_CONVE
ID CT51_CONVE Reviewed; 60 AA.
AC Q9BPG5; Q9BPG4;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Conotoxin VnMRCL-012 {ECO:0000303|PubMed:11158371};
DE AltName: Full=VnMRCL-03 {ECO:0000303|PubMed:11158371};
DE Flags: Precursor;
OS Conus ventricosus (Mediterranean cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lautoconus.
OX NCBI_TaxID=117992;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VNMRCL-012 AND VNMRCL-03).
RX PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL Mol. Biol. Evol. 18:120-131(2001).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:11158371}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=VnMRCL-012;
CC IsoId=Q9BPG5-1; Sequence=Displayed;
CC Name=VnMRCL-03;
CC IsoId=Q9BPG5-2; Sequence=VSP_038850;
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:11158371}.
CC -!- DOMAIN: The cysteine framework is V (CC-CC). {ECO:0000305}.
CC -!- PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or
CC 'C1-C4, C2-C3', since these disulfide connectivities have been observed
CC for conotoxins with cysteine framework V (for examples, see AC P0DQQ7
CC and AC P81755). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR EMBL; AF214964; AAG60392.1; -; mRNA.
DR EMBL; AF214965; AAG60393.1; -; mRNA.
DR AlphaFoldDB; Q9BPG5; -.
DR ConoServer; 651; Vn5.1 precursor.
DR ConoServer; 652; Vn5.1 precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR031565; T-conotoxin.
DR Pfam; PF16981; Chi-conotoxin; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..50
FT /evidence="ECO:0000250"
FT /id="PRO_0000392723"
FT PEPTIDE 51..60
FT /note="Conotoxin VnMRCL-012"
FT /id="PRO_0000392724"
FT VAR_SEQ 22..36
FT /note="Missing (in isoform VnMRCL-03)"
FT /evidence="ECO:0000303|PubMed:11158371"
FT /id="VSP_038850"
SQ SEQUENCE 60 AA; 6802 MW; 17D28AB5BE67A88B CRC64;
MRCLPVFVIL LLLIASAPGV DAQPKTKYDV PLASRHDFAK KTPKRLSKPR DCCRRNFLCC