COW_CONRA
ID COW_CONRA Reviewed; 63 AA.
AC P58786;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Contryphan-R {ECO:0000303|PubMed:8910408};
DE AltName: Full=Bromocontryphan {ECO:0000303|PubMed:9033387};
DE Contains:
DE RecName: Full=[Des-Gly1]-contryphan-R {ECO:0000303|PubMed:8910408};
DE Flags: Precursor;
OS Conus radiatus (Rayed cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Phasmoconus.
OX NCBI_TaxID=61198;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 55-62, HYDROXYLATION AT
RP PRO-57, D-AMINO ACID AT TRP-58, BROMINATION AT TRP-61, AMIDATION AT CYS-62,
RP SYNTHESIS OF 55-62 (BROMOCONTRYPHAN), MASS SPECTROMETRY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom, and Venom duct;
RX PubMed=9033387; DOI=10.1021/bi962840p;
RA Jimenez E.C., Craig A.G., Watkins M., Hillyard D.R., Gray W.R., Gulyas J.,
RA Rivier J.E., Cruz L.J., Olivera B.M.;
RT "Bromocontryphan: post-translational bromination of tryptophan.";
RL Biochemistry 36:989-994(1997).
RN [2]
RP PROTEIN SEQUENCE OF 55-62, HYDROXYLATION AT PRO-57, D-AMINO ACID AT TRP-58,
RP AMIDATION AT CYS-62, SYNTHESIS OF 55-62 (CONTRYPHAN), MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8910408; DOI=10.1074/jbc.271.45.28002;
RA Jimenez E.C., Olivera B.M., Gray W.R., Cruz L.J.;
RT "Contryphan is a D-tryptophan-containing Conus peptide.";
RL J. Biol. Chem. 271:28002-28005(1996).
RN [3]
RP STRUCTURE BY NMR OF 55-62, DISULFIDE BONDS, AND CIS-TRANS ISOMERIZATION.
RX PubMed=10471307; DOI=10.1021/bi990685j;
RA Pallaghy P.K., Melnikova A.P., Jimenez E.C., Olivera B.M., Norton R.S.;
RT "Solution structure of contryphan-R, a naturally occurring disulfide-
RT bridged octapeptide containing D-tryptophan: comparison with protein
RT loops.";
RL Biochemistry 38:11553-11559(1999).
RN [4]
RP STRUCTURE BY NMR OF 56-62 (MAJOR (CIS) CONFORMER), DISULFIDE BONDS, AND
RP CIS-TRANS ISOMERIZATION.
RX PubMed=11041849; DOI=10.1021/bi0010930;
RA Pallaghy P.K., He W., Jimenez E.C., Olivera B.M., Norton R.S.;
RT "Structures of the contryphan family of cyclic peptides. Role of
RT electrostatic interactions in cis-trans isomerism.";
RL Biochemistry 39:12845-12852(2000).
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:8910408,
CC ECO:0000269|PubMed:9033387}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:8910408, ECO:0000305|PubMed:9033387}.
CC -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC -!- PTM: The differences between contryphan-R and bromocontryphan lies in
CC the state of bromination of Trp-61. {ECO:0000269|PubMed:9033387}.
CC -!- MASS SPECTROMETRY: [Contryphan-R]: Mass=990.3; Method=Electrospray;
CC Note=Contryphan-R.; Evidence={ECO:0000269|PubMed:8910408};
CC -!- MASS SPECTROMETRY: [[Des-Gly1]-contryphan-R]: Mass=933.3;
CC Method=Electrospray; Note=[Des-Gly1]contryphan-R.;
CC Evidence={ECO:0000269|PubMed:8910408};
CC -!- MASS SPECTROMETRY: [Contryphan-R]: Mass=1070.5; Method=MALDI;
CC Note=Bromocontryphan.; Evidence={ECO:0000269|PubMed:9033387};
CC -!- MISCELLANEOUS: Contryphan-R and [Des-Gly1]-contryphan-R exist in two
CC forms, due to cis-trans isomerization at 56-Cys-hydroxyPro-57.
CC {ECO:0000269|PubMed:10471307, ECO:0000269|PubMed:11041849}.
CC -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC {ECO:0000305}.
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DR PIR; A58511; A58511.
DR PDB; 1DG0; NMR; -; A=56-62.
DR PDB; 1QFB; NMR; -; A=55-62.
DR PDBsum; 1DG0; -.
DR PDBsum; 1QFB; -.
DR AlphaFoldDB; P58786; -.
DR BMRB; P58786; -.
DR SMR; P58786; -.
DR ConoServer; 1310; Contryphan-R precursor.
DR EvolutionaryTrace; P58786; -.
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 3D-structure; Amidation; Bromination; D-amino acid;
KW Direct protein sequencing; 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:0000269|PubMed:8910408,
FT ECO:0000269|PubMed:9033387"
FT /id="PRO_0000035070"
FT PEPTIDE 55..62
FT /note="Contryphan-R"
FT /evidence="ECO:0000269|PubMed:10471307,
FT ECO:0000269|PubMed:8910408, ECO:0000269|PubMed:9033387"
FT /id="PRO_0000035071"
FT PEPTIDE 56..62
FT /note="[Des-Gly1]-contryphan-R"
FT /evidence="ECO:0000269|PubMed:8910408"
FT /id="PRO_0000035072"
FT REGION 24..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:8910408,
FT ECO:0000269|PubMed:9033387"
FT MOD_RES 58
FT /note="D-tryptophan"
FT /evidence="ECO:0000269|PubMed:8910408,
FT ECO:0000269|PubMed:9033387"
FT MOD_RES 61
FT /note="6'-bromotryptophan; in form bromocontryphan"
FT /evidence="ECO:0000269|PubMed:9033387"
FT MOD_RES 62
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:8910408,
FT ECO:0000269|PubMed:9033387"
FT DISULFID 56..62
FT /evidence="ECO:0000269|PubMed:10471307,
FT ECO:0000269|PubMed:11041849, ECO:0000269|PubMed:9033387"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1QFB"
SQ SEQUENCE 63 AA; 6667 MW; 5FAE62CDB6B016B6 CRC64;
MGKLTILVLV AAVLLSAQVM VQGDGDQPAD RNAVPRDDNP GGASGKFMNV LRRSGCPWEP
WCG
