PA2A2_NAJNA
ID PA2A2_NAJNA Reviewed; 119 AA.
AC P15445; Q65ZF5;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Acidic phospholipase A2 2;
DE Short=PLA22;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Naja naja (Indian cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=35670;
RN [1]
RP PROTEIN SEQUENCE, AND CIRCULAR DICHROISM.
RC TISSUE=Venom;
RX PubMed=2294972; DOI=10.1016/0167-4838(90)90095-w;
RA Davidson F.F., Dennis E.A.;
RT "Amino acid sequence and circular dichroism of Indian cobra (Naja naja
RT naja) venom acidic phospholipase A2.";
RL Biochim. Biophys. Acta 1037:7-15(1990).
RN [2]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=2626425;
RA Shafqat J., Beg O.U., Joernvall H., Zaidi Z.H.;
RT "Phospholipase A2 from cobra (Naja naja naja) venom. Primary structure and
RT subspecies variation.";
RL Protein Seq. Data Anal. 2:451-452(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1730025; DOI=10.1016/0167-4838(92)90136-2;
RA Kelley M.J., Crowl R.M., Dennis E.A.;
RT "Renaturation of cobra venom phospholipase A2 expressed from a synthetic
RT gene in Escherichia coli.";
RL Biochim. Biophys. Acta 1118:107-115(1992).
RN [4]
RP PROTEIN SEQUENCE OF 1-20, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=20203422; DOI=10.2220/biomedres.31.71;
RA Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G.,
RA Athauda S.B., Moriyama A.;
RT "Molecular diversity in venom proteins of the Russell's viper (Daboia
RT russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka.";
RL Biomed. Res. 31:71-81(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALCIUM ION,
RP COFACTOR, DISULFIDE BONDS, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=8419939; DOI=10.1073/pnas.90.1.342;
RA Fremont D.H., Anderson D.H., Wilson I.A., Dennis E.A., Xuong N.-H.;
RT "Crystal structure of phospholipase A2 from Indian cobra reveals a trimeric
RT association.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:342-346(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), DISULFIDE BONDS, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=9636712; DOI=10.1006/jmbi.1998.1759;
RA Segelke B.W., Nguyen D., Chee R., Xuong N.H., Dennis E.A.;
RT "Structures of two novel crystal forms of Naja naja naja phospholipase A2
RT lacking Ca2+ reveal trimeric packing.";
RL J. Mol. Biol. 279:223-232(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH AN INHIBITOR, AND
RP DISULFIDE BONDS.
RX PubMed=20211188; DOI=10.1016/j.jmb.2010.02.049;
RA Dalm D., Palm G.J., Aleksandrov A., Simonson T., Hinrichs W.;
RT "Nonantibiotic properties of tetracyclines: structural basis for inhibition
RT of secretory phospholipase A2.";
RL J. Mol. Biol. 398:83-96(2010).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides.
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;
CC Evidence={ECO:0000305|PubMed:8419939};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305|PubMed:8419939};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:20211188,
CC ECO:0000269|PubMed:8419939, ECO:0000269|PubMed:9636712}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20203422}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20203422}.
CC -!- MISCELLANEOUS: Is not neurotoxic.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA45372.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X63947; CAA45372.1; ALT_INIT; Genomic_DNA.
DR PIR; S07528; S07528.
DR PDB; 1A3D; X-ray; 1.80 A; A=1-119.
DR PDB; 1A3F; X-ray; 2.65 A; A/B/C=1-119.
DR PDB; 1OWS; X-ray; 2.30 A; A=1-118, B=1-119.
DR PDB; 1PSH; X-ray; 2.30 A; A/B/C=1-119.
DR PDB; 2WQ5; X-ray; 1.65 A; A=1-119.
DR PDBsum; 1A3D; -.
DR PDBsum; 1A3F; -.
DR PDBsum; 1OWS; -.
DR PDBsum; 1PSH; -.
DR PDBsum; 2WQ5; -.
DR AlphaFoldDB; P15445; -.
DR SMR; P15445; -.
DR BindingDB; P15445; -.
DR ChEMBL; CHEMBL5584; -.
DR SwissLipids; SLP:000000937; -.
DR PRIDE; P15445; -.
DR BRENDA; 3.1.1.4; 3557.
DR EvolutionaryTrace; P15445; -.
DR Proteomes; UP000694559; Unplaced.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Reference proteome; Secreted.
FT CHAIN 1..119
FT /note="Acidic phospholipase A2 2"
FT /id="PRO_0000161669"
FT ACT_SITE 47
FT /evidence="ECO:0000305|PubMed:8419939"
FT ACT_SITE 93
FT /evidence="ECO:0000305|PubMed:8419939"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8419939,
FT ECO:0007744|PDB:1PSH"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8419939,
FT ECO:0007744|PDB:1PSH"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8419939,
FT ECO:0007744|PDB:1PSH"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8419939,
FT ECO:0007744|PDB:1PSH"
FT DISULFID 11..71
FT /evidence="ECO:0000269|PubMed:20211188,
FT ECO:0000269|PubMed:8419939, ECO:0000269|PubMed:9636712,
FT ECO:0007744|PDB:1A3D, ECO:0007744|PDB:1PSH,
FT ECO:0007744|PDB:2WQ5"
FT DISULFID 26..118
FT /evidence="ECO:0000269|PubMed:20211188,
FT ECO:0000269|PubMed:8419939, ECO:0000269|PubMed:9636712,
FT ECO:0007744|PDB:1A3D, ECO:0007744|PDB:1PSH,
FT ECO:0007744|PDB:2WQ5"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:20211188,
FT ECO:0000269|PubMed:8419939, ECO:0000269|PubMed:9636712,
FT ECO:0007744|PDB:1A3D, ECO:0007744|PDB:1PSH,
FT ECO:0007744|PDB:2WQ5"
FT DISULFID 43..99
FT /evidence="ECO:0000269|PubMed:20211188,
FT ECO:0000269|PubMed:8419939, ECO:0000269|PubMed:9636712,
FT ECO:0007744|PDB:1A3D, ECO:0007744|PDB:1PSH,
FT ECO:0007744|PDB:2WQ5"
FT DISULFID 50..92
FT /evidence="ECO:0000269|PubMed:20211188,
FT ECO:0000269|PubMed:8419939, ECO:0000269|PubMed:9636712,
FT ECO:0007744|PDB:1A3D, ECO:0007744|PDB:1PSH,
FT ECO:0007744|PDB:2WQ5"
FT DISULFID 60..85
FT /evidence="ECO:0000269|PubMed:20211188,
FT ECO:0000269|PubMed:8419939, ECO:0000269|PubMed:9636712,
FT ECO:0007744|PDB:1A3D, ECO:0007744|PDB:1PSH,
FT ECO:0007744|PDB:2WQ5"
FT DISULFID 78..90
FT /evidence="ECO:0000269|PubMed:20211188,
FT ECO:0000269|PubMed:8419939, ECO:0000269|PubMed:9636712,
FT ECO:0007744|PDB:1A3D, ECO:0007744|PDB:1PSH,
FT ECO:0007744|PDB:2WQ5"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:2WQ5"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:2WQ5"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2WQ5"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:2WQ5"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1A3D"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2WQ5"
FT HELIX 39..54
FT /evidence="ECO:0007829|PDB:2WQ5"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2WQ5"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2WQ5"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2WQ5"
FT HELIX 84..102
FT /evidence="ECO:0007829|PDB:2WQ5"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2WQ5"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2WQ5"
SQ SEQUENCE 119 AA; 13346 MW; B725291AAB522966 CRC64;
NLYQFKNMIK CTVPSRSWWD FADYGCYCGR GGSGTPVDDL DRCCQVHDNC YNEAEKISGC
WPYFKTYSYE CSQGTLTCKG DNNACAASVC DCDRLAAICF AGAPYNDNNY NIDLKARCQ
