PA2_MICLE
ID PA2_MICLE Reviewed; 32 AA.
AC C0HLB8;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Phospholipase A2 {ECO:0000303|Ref.1};
DE Short=MIPLA2-1 {ECO:0000303|Ref.1};
DE Short=svPLA2 {ECO:0000250|UniProtKB:P84736};
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:P84736};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P84736};
DE Flags: Fragment;
OS Micrurus lemniscatus (South American 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=129464 {ECO:0000303|Ref.1};
RN [1]
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom {ECO:0000303|Ref.1};
RA Guimaraes L., Santos J., Gouveia V., Borges M.;
RT "Purification and characterization of a MlPLA2 from Micrurus lemniscatus
RT snake venom.";
RL Submitted (MAY-2018) to UniProtKB.
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000250|UniProtKB:P84736}.
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:0000250|UniProtKB:P84736};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P84736};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P84736};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC -!- MASS SPECTROMETRY: Mass=13811; Method=MALDI;
CC Evidence={ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC {ECO:0000305}.
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DR AlphaFoldDB; C0HLB8; -.
DR SMR; C0HLB8; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
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; IPR001211; PLipase_A2.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SUPFAM; SSF48619; SSF48619; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Secreted.
FT CHAIN <1..>32
FT /note="Phospholipase A2"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000445265"
FT BINDING 16
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT DISULFID 15..?
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT DISULFID 17..?
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT DISULFID 32..?
FT /evidence="ECO:0000250|UniProtKB:P15445"
FT NON_TER 1
FT NON_TER 32
SQ SEQUENCE 32 AA; 3728 MW; 3DD1D733C62530D0 CRC64;
NRNNRDWWHF ADYGCYCGYG GSGTPVDELD RC
