COMB_CONMA
ID COMB_CONMA Reviewed; 42 AA.
AC Q9TWL8;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 02-JUN-2021, entry version 47.
DE RecName: Full=Conodipine-M beta chain;
OS Conus magus (Magical cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX NCBI_TaxID=6492;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=7876086; DOI=10.1074/jbc.270.8.3518;
RA McIntosh J.M., Ghomashchi F., Gelb M.H., Dooley D.J., Stoehr S.J.,
RA Giordani A.B., Naisbitt S.R., Olivera B.M.;
RT "Conodipine-M, a novel phospholipase A2 isolated from the venom of the
RT marine snail Conus magus.";
RL J. Biol. Chem. 270:3518-3526(1995).
CC -!- FUNCTION: Heterodimer: conodipine-M catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. This
CC activity may be supported by the alpha chain. Conodipine-M inhibits the
CC binding of isradipine (a ligand specific for L-type calcium channel) to
CC L-type calcium channels. {ECO:0000269|PubMed:7876086}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chains; probably disulfide-
CC linked.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC -!- MASS SPECTROMETRY: Mass=5036; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7876086};
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DR ConoServer; 5540; Conodipine-M beta chain.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IDA:CACAO.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Secreted; Toxin.
FT CHAIN 1..42
FT /note="Conodipine-M beta chain"
FT /id="PRO_0000086875"
SQ SEQUENCE 42 AA; 4962 MW; F1132A5CEB974134 CRC64;
AATCTHWALI YFKTVQLFGW XHFNYQVDAT YCPQFQPCMP XX