ID   COW2_CONBL              Reviewed;          60 AA.
AC   A0A1P8NVU0;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Contryphan-Lo2 {ECO:0000305};
DE   AltName: Full=Lo1158 {ECO:0000305|PubMed:28152596};
DE   Flags: Precursor;
OS   Conus buxeus loroisii (Cone snail) (Conus loroisii).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Dendroconus.
OX   NCBI_TaxID=410709;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   AMIDATION AT CYS-59, D-AMINO ACID AT TRP-55 AND TRP-58, AND DISULFIDE BOND.
RC   TISSUE=Venom, and 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:0000269|PubMed:28152596}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:28152596}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1158.44; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:28152596};
CC   -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC       {ECO:0000305}.
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DR   EMBL; KX289885; APX52862.1; -; mRNA.
DR   AlphaFoldDB; A0A1P8NVU0; -.
DR   ConoServer; 9764; Contryphan-Lo2 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   1: Evidence at protein level;
KW   Amidation; D-amino acid; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..50
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000445134"
FT   PEPTIDE         51..59
FT                   /note="Contryphan-Lo2"
FT                   /evidence="ECO:0000269|PubMed:28152596"
FT                   /id="PRO_5012433346"
FT   REGION          25..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         55
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000305|PubMed:28152596"
FT   MOD_RES         58
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000305|PubMed:28152596"
FT   MOD_RES         59
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:28152596"
FT   DISULFID        53..59
FT                   /evidence="ECO:0000269|PubMed:28152596"
SQ   SEQUENCE   60 AA;  6598 MW;  FFBFDB803564D3E2 CRC64;
     MGKLTILVLV AAVLLSTQAM VQDQPADRNA VRRNDNPGGA SRKSINVLHR NECPWQPWCG