COW_CONMR
ID COW_CONMR Reviewed; 63 AA.
AC P62903;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Glacontryphan-M {ECO:0000303|PubMed:15155730, ECO:0000303|PubMed:15155731};
DE Flags: Precursor;
OS Conus marmoreus (Marble cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Conus.
OX NCBI_TaxID=42752;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-62, FUNCTION,
RP GAMMA-CARBOXYGLUTAMATION AT GLU-53 AND GLU-55, D-AMINO ACID AT TRP-58,
RP AMIDATION AT CYS-62, MASS SPECTROMETRY, SYNTHESIS OF 52-62, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom, and Venom duct;
RX PubMed=15155730; DOI=10.1074/jbc.m313825200;
RA Hansson K., Ma X., Eliasson L., Czerwiec E., Furie B., Furie B.C.,
RA Rorsman P., Stenflo J.;
RT "The first gamma-carboxyglutamic acid-containing contryphan. A selective L-
RT type calcium ion channel blocker isolated from the venom of Conus
RT marmoreus.";
RL J. Biol. Chem. 279:32453-32463(2004).
RN [2]
RP STRUCTURE BY NMR, CALCIUM-BINDING, CIS-TRANS ISOMERIZATION, AND DISULFIDE
RP BOND.
RX PubMed=15155731; DOI=10.1074/jbc.m313826200;
RA Grant M.A., Hansson K., Furie B.C., Furie B., Stenflo J., Rigby A.C.;
RT "The metal-free and calcium-bound structures of a gamma-carboxyglutamic
RT acid-containing contryphan from Conus marmoreus, glacontryphan-M.";
RL J. Biol. Chem. 279:32464-32473(2004).
CC -!- FUNCTION: Inhibits high (L-type) voltage-activated calcium channels
CC (Cav) in a calcium-dependent manner. {ECO:0000269|PubMed:15155730}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15155730}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:15155730}.
CC -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=1471.47; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15155730};
CC -!- MISCELLANEOUS: In contrast to the other contryphans, glacontryphan-M is
CC a single homogenous conformer exhibiting no cis to trans isomerization
CC of the Cys-Pro peptidyl bond in aqueous solution.
CC {ECO:0000269|PubMed:15155731}.
CC -!- SIMILARITY: Belongs to the O2 superfamily. Contryphan family.
CC {ECO:0000305}.
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DR EMBL; AY485226; AAS48587.1; -; mRNA.
DR AlphaFoldDB; P62903; -.
DR ConoServer; 1357; contryphan-M precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Calcium channel impairing toxin; D-amino acid;
KW Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW Ion channel impairing toxin; Metal-binding; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..51
FT /evidence="ECO:0000269|PubMed:15155730"
FT /id="PRO_0000035066"
FT PEPTIDE 52..62
FT /note="Glacontryphan-M"
FT /evidence="ECO:0000269|PubMed:15155730"
FT /id="PRO_0000035067"
FT REGION 23..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:15155731"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:15155731"
FT MOD_RES 53
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:15155730"
FT MOD_RES 55
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:15155730"
FT MOD_RES 58
FT /note="D-tryptophan"
FT /evidence="ECO:0000269|PubMed:15155730"
FT MOD_RES 62
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:15155730"
FT DISULFID 56..62
FT /evidence="ECO:0000269|PubMed:15155731"
SQ SEQUENCE 63 AA; 7097 MW; E7F51B5DBB2B1FE1 CRC64;
MGKLTILVLV AAVLLSTQVM VQGDRDQPAD RNAVPRDDNP GRARRKRMKV LNESECPWHP
WCG
