PA2A1_MICDM
ID PA2A1_MICDM Reviewed; 117 AA.
AC C0HKB8;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Acidic phospholipase A2 {ECO:0000303|PubMed:28315380};
DE Short=MdumPLA2 {ECO:0000303|PubMed:28315380};
DE Short=svPLA2 {ECO:0000250|UniProtKB:P15445};
DE EC=3.1.1.4 {ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000269|PubMed:28315380};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P15445};
OS Micrurus dumerilii (Coral snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=1337871 {ECO:0000303|PubMed:28315380};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000303|PubMed:28315380};
RX PubMed=28315380; DOI=10.1016/j.biochi.2017.03.008;
RA Rey-Suarez P., Nunez V., Saldarriaga-Cordoba M., Lomonte B.;
RT "Primary structures and partial toxicological characterization of two
RT phospholipases A2 from Micrurus mipartitus and Micrurus dumerilii coral
RT snake venoms.";
RL Biochimie 137:88-98(2017).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows strong
CC myotoxicity and induces edema in mice. Shows no cytotoxicity in vitro.
CC Has a strong anticoagulant effect in vitro. PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:28315380}.
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:0000255|PROSITE-ProRule:PRU10035,
CC ECO:0000269|PubMed:28315380};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P15445};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15445};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28315380}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:28315380}.
CC -!- MASS SPECTROMETRY: Mass=13288; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:28315380};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HKB8; -.
DR SMR; C0HKB8; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted.
FT CHAIN 1..117
FT /note="Acidic phospholipase A2"
FT /evidence="ECO:0000269|PubMed:28315380"
FT /id="PRO_0000441096"
FT ACT_SITE 46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10036"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 11..70
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT DISULFID 25..116
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT DISULFID 27..43
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT DISULFID 42..98
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT DISULFID 49..91
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT DISULFID 59..84
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT DISULFID 77..89
FT /evidence="ECO:0000250|UniProtKB:P15445"
SQ SEQUENCE 117 AA; 13188 MW; C179E4185348D287 CRC64;
NLIDFKNMIK CTTKRSVLDF ADYGCYCGSG GSGTPVDDLD RCCKVHDDCY GEAEKVHGCW
PKWTLYSYDC SNGQLTCKDN NTKCKDFVCN CDRTAAICFA KAPYDDNNFM INNPRCQ
