PA2A_MACLN
ID PA2A_MACLN Reviewed; 138 AA.
AC B5U6Z2;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Acidic phospholipase A2 MVL-PLA2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Macrovipera lebetina transmediterranea (Blunt-nosed viper) (Vipera lebetina
OS transmediterranea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX NCBI_TaxID=384075;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-34; 59-72; 83-93 AND
RP 100-112, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=19351557; DOI=10.1016/j.matbio.2009.03.007;
RA Bazaa A., Luis J., Srairi-Abid N., Kallech-Ziri O., Kessentini-Zouari R.,
RA Defilles C., Lissitzky J.C., El Ayeb M., Marrakchi N.;
RT "MVL-PLA2, a phospholipase A2 from Macrovipera lebetina transmediterranea
RT venom, inhibits tumor cells adhesion and migration.";
RL Matrix Biol. 28:188-193(2009).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that displays an
CC inhibitory effect, independent from its catalytic activity, on tumor
CC cell adhesion and migration. This effect is mediated via specific
CC inhibition of integrins alpha-5/beta-1 (ITGA5/ITGB1), alpha-v/beta-3
CC (ITGAV/ITGB3) and alpha-v/beta-6 (ITGAV/ITGB6). PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:19351557}.
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, ECO:0000255|PROSITE-
CC ProRule:PRU10036};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13626.64; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19351557};
CC -!- MISCELLANEOUS: Concentrations up to 2 uM during 4 days does not induce
CC detectable cytotoxicity on human melanoma and fibrosarcoma cell lines.
CC {ECO:0000305|PubMed:19351557}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; FM202092; CAR40186.1; -; mRNA.
DR AlphaFoldDB; B5U6Z2; -.
DR SMR; B5U6Z2; -.
DR BRENDA; 3.1.1.4; 11952.
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: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 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 Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:19351557"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 MVL-PLA2"
FT /id="PRO_0000419283"
FT MOTIF 86..88
FT /note="May inhibit integrin function (Atypical cell
FT attachment site)"
FT ACT_SITE 63
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 42..131
FT /evidence="ECO:0000250"
FT DISULFID 44..60
FT /evidence="ECO:0000250"
FT DISULFID 59..111
FT /evidence="ECO:0000250"
FT DISULFID 65..138
FT /evidence="ECO:0000250"
FT DISULFID 66..104
FT /evidence="ECO:0000250"
FT DISULFID 73..97
FT /evidence="ECO:0000250"
FT DISULFID 91..102
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 15399 MW; 8D801E95C09E9DE0 CRC64;
MRTLWIVAVC LMGVEGHLTQ FGDMINKKTG TFGLLSYVYY GCYCGLGGKG KPQDATDRCC
FVHDCCYGTV NGCDPKLSTY SYSFQNGDIV CGDDDPCLRA VCECDRVAAI CFGENMNTYD
KKYMLYSLFD CMEESEKC
