COMA_CONMA
ID COMA_CONMA Reviewed; 77 AA.
AC Q9TWL9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 23-FEB-2022, entry version 71.
DE RecName: Full=Conodipine-M alpha chain {ECO:0000303|PubMed:7876086};
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A2;
DE Short=PLA2;
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, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, SUBUNIT, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP PYROGLUTAMATE FORMATION AT GLN-1.
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:0000305|PubMed:7876086}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:7876086};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:7876086};
CC -!- ACTIVITY REGULATION: Inhibited by linoleoyl amide and MG14.
CC {ECO:0000269|PubMed:7876086}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chains; probably disulfide-
CC linked. {ECO:0000269|PubMed:7876086}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7876086}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:7876086}.
CC -!- MASS SPECTROMETRY: Mass=8571; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7876086};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group IX subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR ConoServer; 5541; Conodipine-M alpha chain.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Pyrrolidone carboxylic acid; Secreted;
KW Toxin.
FT CHAIN 1..77
FT /note="Conodipine-M alpha chain"
FT /evidence="ECO:0000269|PubMed:7876086"
FT /id="PRO_0000086866"
FT ACT_SITE 36
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:7876086"
SQ SEQUENCE 77 AA; 8492 MW; 73861D7587479D8C CRC64;
QXPSTAELCK INSNACSVPF SXIPCQKXFL AACDRHDTCY HCGKHFGFKQ DDCDDAFFRD
MTALCAHGTD DEGXCPX
