PA2A3_NAJSG
ID PA2A3_NAJSG Reviewed; 126 AA.
AC P60045;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Acidic phospholipase A2 3;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor; Fragment;
OS Naja sagittifera (Andaman cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=195058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Paramasivam M., Hariprasad R.G., Saravanan K., Singh R.K., Sharma S.,
RA Singh T.P., Srinivasan A.;
RT "Phospholipase A2 isoform 3 from Indian cobra.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 8-126 IN COMPLEX WITH A PEPTIDE
RP INHIBITOR.
RX PubMed=14529280; DOI=10.1021/bi035076x;
RA Singh R.K., Vikram P., Makker J., Jabeen T., Sharma S., Dey S., Kaur P.,
RA Srinivasan A., Singh T.P.;
RT "Design of specific peptide inhibitors for group I phospholipase A2:
RT structure of a complex formed between phospholipase A2 from Naja naja
RT sagittifera (group I) and a designed peptide inhibitor Val-Ala-Phe-Arg-Ser
RT (VAFRS) at 1.9 A resolution reveals unique features.";
RL Biochemistry 42:11701-11706(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 8-125 IN COMPLEX WITH CALCIUM ION
RP AND ACETYLSALICYLIC ACID, COFACTOR, AND DISULFIDE BONDS.
RX PubMed=15823962; DOI=10.1080/10611860400024078;
RA Singh R.K., Ethayathulla A.S., Jabeen T., Sharma S., Kaur P., Singh T.P.;
RT "Aspirin induces its anti-inflammatory effects through its specific binding
RT to phospholipase A2: crystal structure of the complex formed between
RT phospholipase A2 and aspirin at 1.9 angstroms resolution.";
RL J. Drug. Target. 13:113-119(2005).
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:15823962};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:15823962};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AY433936; AAR08048.1; -; mRNA.
DR PDB; 1LN8; X-ray; 1.65 A; A=8-126.
DR PDB; 1MF4; X-ray; 1.90 A; A=8-126.
DR PDB; 1OXR; X-ray; 1.93 A; A=8-125.
DR PDB; 1SZ8; X-ray; 1.50 A; A=8-126.
DR PDB; 1T37; X-ray; 2.60 A; A=8-125.
DR PDB; 1TD7; X-ray; 2.50 A; A=8-126.
DR PDB; 1YXL; X-ray; 1.48 A; A=8-125.
DR PDB; 1ZM6; X-ray; 2.60 A; A=8-125.
DR PDB; 3GCI; X-ray; 2.04 A; A=8-126.
DR PDB; 3JQ5; X-ray; 2.03 A; A=8-126.
DR PDB; 3JQL; X-ray; 1.20 A; A=8-126.
DR PDB; 3JTI; X-ray; 1.80 A; A=8-126.
DR PDB; 3NJU; X-ray; 1.40 A; A=8-126.
DR PDB; 3OSH; X-ray; 1.50 A; A=8-126.
DR PDB; 3Q4Y; X-ray; 2.30 A; A=8-126.
DR PDBsum; 1LN8; -.
DR PDBsum; 1MF4; -.
DR PDBsum; 1OXR; -.
DR PDBsum; 1SZ8; -.
DR PDBsum; 1T37; -.
DR PDBsum; 1TD7; -.
DR PDBsum; 1YXL; -.
DR PDBsum; 1ZM6; -.
DR PDBsum; 3GCI; -.
DR PDBsum; 3JQ5; -.
DR PDBsum; 3JQL; -.
DR PDBsum; 3JTI; -.
DR PDBsum; 3NJU; -.
DR PDBsum; 3OSH; -.
DR PDBsum; 3Q4Y; -.
DR AlphaFoldDB; P60045; -.
DR SMR; P60045; -.
DR DrugCentral; P60045; -.
DR PRIDE; P60045; -.
DR TopDownProteomics; P60045; -.
DR EvolutionaryTrace; P60045; -.
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; Disulfide bond; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Secreted.
FT PROPEP <1..7
FT /id="PRO_0000022928"
FT CHAIN 8..126
FT /note="Acidic phospholipase A2 3"
FT /id="PRO_0000022929"
FT ACT_SITE 54
FT /evidence="ECO:0000305|PubMed:15823962"
FT ACT_SITE 100
FT /evidence="ECO:0000305|PubMed:15823962"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT DISULFID 18..78
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT DISULFID 33..125
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT DISULFID 35..51
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT DISULFID 50..106
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT DISULFID 57..99
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT DISULFID 67..92
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT DISULFID 85..97
FT /evidence="ECO:0000269|PubMed:15823962,
FT ECO:0007744|PDB:1OXR"
FT NON_TER 1
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:3JQL"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:3JQL"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3JQL"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:3JQL"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3JQL"
FT HELIX 46..61
FT /evidence="ECO:0007829|PDB:3JQL"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3JQL"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3JQL"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3JQL"
FT HELIX 91..109
FT /evidence="ECO:0007829|PDB:3JQL"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3JQL"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:3JQL"
SQ SEQUENCE 126 AA; 13969 MW; DA6CA9CB6A447EF3 CRC64;
SNRPMPLNLY QFKNMIQCTV PSRSWQDFAD YGCYCGKGGS GTPVDDLDRC CQVHDNCYNE
AENISGCRPY FKTYSYECTQ GTLTCKGDNN ACAASVCDCD RLAAICFAGA PYNDANYNID
LKARCN
