ID   COW_CONLV               Reviewed;          58 AA.
AC   A0A0K8TU78;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Contryphan-Lnv {ECO:0000305};
DE   Flags: Precursor; Fragment;
OS   Conus lenavati (Cone snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Splinoconus.
OX   NCBI_TaxID=1519839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305|Ref.1}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC       51-Cys-hydroxyPro-52. 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; GCVH01000087; JAI17806.1; -; Transcribed_RNA.
DR   AlphaFoldDB; A0A0K8TU78; -.
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   2: Evidence at transcript level;
KW   Amidation; D-amino acid; Disulfide bond; Hydroxylation; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..47
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000445139"
FT   PEPTIDE         48..57
FT                   /note="Contryphan-Lnv"
FT                   /id="PRO_5005520251"
FT   MOD_RES         52
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
FT   MOD_RES         53
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
FT   MOD_RES         57
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
FT   DISULFID        51..57
FT                   /evidence="ECO:0000250|UniProtKB:P58786"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:JAI17806.1"
SQ   SEQUENCE   58 AA;  6369 MW;  C754FDBBF59415EB CRC64;
     ILLLVAAVLL STQVMVQGDG DQPAYRNAVP RDDNTGGASR KFLNVPRESE CPWRPWCG