PA2_SCOVI
ID PA2_SCOVI Reviewed; 147 AA.
AC C1JAR9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Phospholipase A2 Scol/Pla;
DE Short=PLA2;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:P0DPT8};
DE Flags: Precursor;
OS Scolopendra viridis (Giant centipede).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Scolopendromorpha; Scolopendridae; Scolopendra.
OX NCBI_TaxID=118503;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-53, MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=19285520; DOI=10.1016/j.toxicon.2009.03.003;
RA Gonzalez-Morales L., Diego-Garcia E., Segovia L., Gutierrez M.D.C.,
RA Possani L.D.;
RT "Venom from the centipede Scolopendra viridis Say: Purification, gene
RT cloning and phylogenetic analysis of a phospholipase A2.";
RL Toxicon 54:8-15(2009).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000250|UniProtKB:P0DPT8}.
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:P0DPT8};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19285520}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:19285520}.
CC -!- MASS SPECTROMETRY: Mass=13752; Method=Unknown; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:19285520};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; FJ491263; ACO50769.1; -; mRNA.
DR AlphaFoldDB; C1JAR9; -.
DR SMR; C1JAR9; -.
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 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; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..28
FT /evidence="ECO:0000305|PubMed:19285520"
FT /id="PRO_0000398341"
FT CHAIN 29..147
FT /note="Phospholipase A2 Scol/Pla"
FT /evidence="ECO:0000305|PubMed:19285520"
FT /id="PRO_5000456195"
FT ACT_SITE 74
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT ACT_SITE 124
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 55..71
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 70..130
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 77..123
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 86..116
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 109..121
FT /evidence="ECO:0000250|UniProtKB:P14555"
SQ SEQUENCE 147 AA; 16902 MW; 3B118A711D173D38 CRC64;
MSSKIPLLFI ISFGLYVSTT NSSPIERRSL WNFFFMTFIG GKRAPWKYDG YGNHCGIGGK
GSPVDSIDRC CQVHDRCYHE VNENECGSYK RNVKFIDYDW YMQDKQIVCD TTDTVCAQAI
CKCDKDIVEC LNQNDKDYNP KYNKAIG
