COW_CONIN
ID COW_CONIN Reviewed; 8 AA.
AC P0C249;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 23-FEB-2022, entry version 42.
DE RecName: Full=Contryphan-In {ECO:0000303|PubMed:16387709};
DE AltName: Full=Contryphan-In936 {ECO:0000303|PubMed:17902199, ECO:0000303|PubMed:24115170};
DE Contains:
DE RecName: Full=Contryphan-In880 {ECO:0000303|PubMed:17902199, ECO:0000303|PubMed:33732044};
DE AltName: Full=Contryphan-In896 {ECO:0000303|PubMed:33732044};
OS Conus inscriptus (Engraved cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Phasmoconus.
OX NCBI_TaxID=257329;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=16387709; DOI=10.1196/annals.1352.022;
RA Gowd K.H., Sabareesh V., Sudarslal S., Iengar P., Franklin B., Fernando A.,
RA Dewan K., Ramaswami M., Sarma S.P., Sikdar S., Balaram P., Krishnan K.S.;
RT "Novel peptides of therapeutic promise from Indian conidae.";
RL Ann. N. Y. Acad. Sci. 1056:462-473(2005).
RN [2]
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, SUBCELLULAR LOCATION, D-AMINO ACID AT
RP LEU-4, AND AMIDATION AT CYS-8.
RC TISSUE=Venom;
RX PubMed=17902199; DOI=10.1002/rcm.3225;
RA Thakur S.S., Balaram P.;
RT "Rapid mass spectral identification of contryphans. Detection of
RT characteristic peptide ions by fragmentation of intact disulfide-bonded
RT peptides in crude venom.";
RL Rapid Commun. Mass Spectrom. 21:3420-3426(2007).
RN [3]
RP PROTEIN SEQUENCE OF 2-7, SUBCELLULAR LOCATION, AMIDATION AT CYS-8,
RP HYDROXYLATION AT PRO-6, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=33732044; DOI=10.1016/j.sjbs.2020.12.032;
RA Jain R.P., Jayaseelan B.F., Wilson Alphonse C.R., Mahmoud A.H.,
RA Mohammed O.B., Ahmed Almunqedhi B.M., Rajaian Pushpabai R.;
RT "Mass spectrometric identification and denovo sequencing of novel
RT conotoxins from vermivorous cone snail (Conus inscriptus), and preliminary
RT screening of its venom for biological activities in vitro and in vivo.";
RL Saudi J. Biol. Sci. 28:1582-1595(2021).
RN [4]
RP STRUCTURE BY NMR, DISULFIDE BOND, SYNTHESIS, CIS-TRANS ISOMERIZATION, AND
RP MUTAGENESIS OF VAL-3 AND TYR-5.
RC TISSUE=Venom;
RX PubMed=24115170; DOI=10.1002/chem.201301722;
RA Sonti R., Gowd K.H., Rao K.N., Ragothama S., Rodriguez A., Perez J.J.,
RA Balaram P.;
RT "Conformational diversity in contryphans from Conus venom: cis-trans
RT isomerisation and aromatic/proline interactions in the 23-membered ring of
RT a 7-residue peptide disulfide loop.";
RL Chemistry 19:15175-15189(2013).
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:17902199}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:17902199}.
CC -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: [Contryphan-In]: Mass=937; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17902199};
CC -!- MASS SPECTROMETRY: [Contryphan-In880]: Mass=880; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17902199};
CC -!- MASS SPECTROMETRY: [Contryphan-In880]: Mass=879.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:33732044};
CC -!- MASS SPECTROMETRY: [Contryphan-In880]: Mass=895.3; Method=MALDI;
CC Note=with 6-HydroxyPro.; Evidence={ECO:0000269|PubMed:33732044};
CC -!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization at
CC 5-Tyr-Pro-6. {ECO:0000269|PubMed:24115170}.
CC -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC {ECO:0000305}.
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DR PDB; 2M6C; NMR; -; A=1-8.
DR PDB; 2M6D; NMR; -; A=1-8.
DR PDB; 2M6E; NMR; -; A=1-8.
DR PDB; 2M6F; NMR; -; A=1-8.
DR PDBsum; 2M6C; -.
DR PDBsum; 2M6D; -.
DR PDBsum; 2M6E; -.
DR PDBsum; 2M6F; -.
DR BMRB; P0C249; -.
DR ConoServer; 1271; Contryphan-In.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR011062; Contryphan_CS.
DR PROSITE; PS60027; CONTRYPHAN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; D-amino acid; Direct protein sequencing;
KW Disulfide bond; Hydroxylation; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Toxin.
FT PEPTIDE 1..8
FT /note="Contryphan-In"
FT /evidence="ECO:0000269|PubMed:16387709,
FT ECO:0000269|PubMed:17902199"
FT /id="PRO_0000262669"
FT PEPTIDE 2..8
FT /note="Contryphan-In880"
FT /evidence="ECO:0000269|PubMed:17902199"
FT /id="PRO_0000439693"
FT MOD_RES 4
FT /note="D-leucine"
FT /evidence="ECO:0000269|PubMed:17902199"
FT MOD_RES 6
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:33732044"
FT MOD_RES 8
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:17902199,
FT ECO:0000269|PubMed:33732044"
FT DISULFID 2..8
FT /evidence="ECO:0000269|PubMed:24115170,
FT ECO:0000312|PDB:2M6C, ECO:0000312|PDB:2M6D,
FT ECO:0000312|PDB:2M6E, ECO:0000312|PDB:2M6F"
FT MUTAGEN 3
FT /note="V->P: Permits a very slow conformation equilibrium
FT to occur."
FT /evidence="ECO:0000269|PubMed:24115170"
FT MUTAGEN 5
FT /note="Y->L: No change in chromatographic profile, there is
FT no slow conformation equilibrium."
FT /evidence="ECO:0000269|PubMed:24115170"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:2M6C"
SQ SEQUENCE 8 AA; 940 MW; 75A3677B5732CEB8 CRC64;
GCVLYPWC
