COW1_CONLT
ID COW1_CONLT Reviewed; 63 AA.
AC Q2I2P3; A0A1P8NVS4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Contryphan-Lt {ECO:0000303|PubMed:16908117};
DE Flags: Precursor;
OS Conus litteratus (Lettered cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Elisaconus.
OX NCBI_TaxID=89445;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=16908117; DOI=10.1016/j.ygeno.2006.06.014;
RA Pi C., Liu J., Peng C., Liu Y., Jiang X., Zhao Y., Tang S., Wang L.,
RA Dong M., Chen S., Xu A.;
RT "Diversity and evolution of conotoxins based on gene expression profiling
RT of Conus litteratus.";
RL Genomics 88:809-819(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-63.
RC TISSUE=Venom duct;
RX PubMed=28152596; DOI=10.1021/acs.jproteome.6b00776;
RA Vijayasarathy M., Basheer S.M., Franklin J.B., Balaram P.;
RT "Contryphan genes and mature peptides in the venom of nine cone snail
RT species by transcriptomic and mass spectrometric analysis.";
RL J. Proteome Res. 16:763-772(2017).
CC -!- FUNCTION: Its target is unknown, but this toxin may modulate voltage-
CC activated calcium channels (Cav) or calcium-dependent potassium
CC channels (KCa). {ECO:0000250|UniProtKB:P0C248,
CC ECO:0000250|UniProtKB:P0C250, ECO:0000250|UniProtKB:P62903,
CC ECO:0000250|UniProtKB:P83047}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16908117}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:16908117}.
CC -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC 56-Cys-hydroxyPro-57. The cis conformation is the major form.
CC {ECO:0000250|UniProtKB:P58787}.
CC -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC {ECO:0000305}.
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DR EMBL; DQ345389; ABC74997.1; -; mRNA.
DR EMBL; KX289883; APX52860.1; -; mRNA.
DR AlphaFoldDB; Q2I2P3; -.
DR ConoServer; 1175; Contryphan-Lt1 precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004214; Conotoxin.
DR InterPro; IPR011062; Contryphan_CS.
DR Pfam; PF02950; Conotoxin; 1.
DR PROSITE; PS60027; CONTRYPHAN; 1.
PE 3: Inferred from homology;
KW Amidation; D-amino acid; Disulfide bond; Hydroxylation;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..54
FT /evidence="ECO:0000305"
FT /id="PRO_0000262671"
FT PEPTIDE 55..62
FT /note="Contryphan-Lt"
FT /id="PRO_0000262672"
FT REGION 24..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P58786"
FT MOD_RES 58
FT /note="D-tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P58786"
FT MOD_RES 62
FT /note="Cysteine amide"
FT /evidence="ECO:0000250|UniProtKB:P58786"
FT DISULFID 56..62
FT /evidence="ECO:0000250|UniProtKB:P58786"
SQ SEQUENCE 63 AA; 6699 MW; A56C33FA79C415C8 CRC64;
MGKLTILLLV AAALLSTQVM VQGGGDQPAA RNAVPRDDNP DGMSGQFMNV LRRSGCPWEP
WCG
