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Acidic phospholipase A2 3 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Fragment)

 PA2A3_NAJSG             Reviewed;         126 AA.
P60045;
21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
21-NOV-2003, sequence version 1.
25-OCT-2017, entry version 83.
RecName: Full=Acidic phospholipase A2 3;
Short=svPLA2;
EC=3.1.1.4;
AltName: Full=Phosphatidylcholine 2-acylhydrolase;
Flags: Precursor; Fragment;
Naja sagittifera (Andaman cobra).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
NCBI_TaxID=195058;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
Paramasivam M., Hariprasad R.G., Saravanan K., Singh R.K., Sharma S.,
Singh T.P., Srinivasan A.;
"Phospholipase A2 isoform 3 from Indian cobra.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[2]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 8-126 IN COMPLEX WITH A
PEPTIDE INHIBITOR.
PubMed=14529280; DOI=10.1021/bi035076x;
Singh R.K., Vikram P., Makker J., Jabeen T., Sharma S., Dey S.,
Kaur P., Srinivasan A., Singh T.P.;
"Design of specific peptide inhibitors for group I phospholipase A2:
structure of a complex formed between phospholipase A2 from Naja naja
sagittifera (group I) and a designed peptide inhibitor Val-Ala-Phe-
Arg-Ser (VAFRS) at 1.9 A resolution reveals unique features.";
Biochemistry 42:11701-11706(2003).
[3]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 8-125 IN COMPLEX WITH
CALCIUM ION AND ACETYLSALICYLIC ACID, COFACTOR, AND DISULFIDE BONDS.
PubMed=15823962; DOI=10.1080/10611860400024078;
Singh R.K., Ethayathulla A.S., Jabeen T., Sharma S., Kaur P.,
Singh T.P.;
"Aspirin induces its anti-inflammatory effects through its specific
binding to phospholipase A2: crystal structure of the complex formed
between phospholipase A2 and aspirin at 1.9 angstroms resolution.";
J. Drug. Target. 13:113-119(2005).
-!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the
2-acyl groups in 3-sn-phosphoglycerides.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000305|PubMed:15823962};
Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:15823962};
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group I
subfamily. D49 sub-subfamily. {ECO:0000305}.
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EMBL; AY433936; AAR08048.1; -; mRNA.
PDB; 1LN8; X-ray; 1.65 A; A=8-126.
PDB; 1MF4; X-ray; 1.90 A; A=8-126.
PDB; 1OXR; X-ray; 1.93 A; A=8-125.
PDB; 1SZ8; X-ray; 1.50 A; A=8-126.
PDB; 1T37; X-ray; 2.60 A; A=8-125.
PDB; 1TD7; X-ray; 2.50 A; A=8-126.
PDB; 1YXL; X-ray; 1.48 A; A=8-125.
PDB; 1ZM6; X-ray; 2.60 A; A=8-125.
PDB; 3GCI; X-ray; 2.04 A; A=8-126.
PDB; 3JQ5; X-ray; 2.03 A; A=8-126.
PDB; 3JQL; X-ray; 1.20 A; A=8-126.
PDB; 3JTI; X-ray; 1.80 A; A=8-126.
PDB; 3NJU; X-ray; 1.40 A; A=8-126.
PDB; 3OSH; X-ray; 1.50 A; A=8-126.
PDB; 3Q4Y; X-ray; 2.30 A; A=8-126.
PDBsum; 1LN8; -.
PDBsum; 1MF4; -.
PDBsum; 1OXR; -.
PDBsum; 1SZ8; -.
PDBsum; 1T37; -.
PDBsum; 1TD7; -.
PDBsum; 1YXL; -.
PDBsum; 1ZM6; -.
PDBsum; 3GCI; -.
PDBsum; 3JQ5; -.
PDBsum; 3JQL; -.
PDBsum; 3JTI; -.
PDBsum; 3NJU; -.
PDBsum; 3OSH; -.
PDBsum; 3Q4Y; -.
ProteinModelPortal; P60045; -.
SMR; P60045; -.
TopDownProteomics; P60045; -.
HOVERGEN; HBG008137; -.
EvolutionaryTrace; P60045; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
CDD; cd00125; PLA2c; 1.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR033112; PLipase_A2_Asp_AS.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
PANTHER; PTHR11716; PTHR11716; 1.
Pfam; PF00068; Phospholip_A2_1; 1.
PRINTS; PR00389; PHPHLIPASEA2.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00119; PA2_ASP; 1.
PROSITE; PS00118; PA2_HIS; 1.
1: Evidence at protein level;
3D-structure; Calcium; Disulfide bond; Hydrolase; Lipid degradation;
Lipid metabolism; Metal-binding; Secreted.
PROPEP <1 7
/FTId=PRO_0000022928.
CHAIN 8 126 Acidic phospholipase A2 3.
/FTId=PRO_0000022929.
ACT_SITE 54 54 {ECO:0000305|PubMed:15823962}.
ACT_SITE 100 100 {ECO:0000305|PubMed:15823962}.
METAL 34 34 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
METAL 36 36 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
METAL 38 38 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
METAL 55 55 Calcium. {ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
DISULFID 18 78 {ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
DISULFID 33 125 {ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
DISULFID 35 51 {ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
DISULFID 50 106 {ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
DISULFID 57 99 {ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
DISULFID 67 92 {ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
DISULFID 85 97 {ECO:0000244|PDB:1OXR,
ECO:0000269|PubMed:15823962}.
NON_TER 1 1
HELIX 9 19 {ECO:0000244|PDB:3JQL}.
HELIX 25 28 {ECO:0000244|PDB:3JQL}.
STRAND 29 31 {ECO:0000244|PDB:3JQL}.
TURN 32 34 {ECO:0000244|PDB:3JQL}.
STRAND 35 37 {ECO:0000244|PDB:3JQL}.
HELIX 46 61 {ECO:0000244|PDB:3JQL}.
TURN 69 71 {ECO:0000244|PDB:3JQL}.
STRAND 76 79 {ECO:0000244|PDB:3JQL}.
STRAND 82 85 {ECO:0000244|PDB:3JQL}.
HELIX 91 109 {ECO:0000244|PDB:3JQL}.
HELIX 114 116 {ECO:0000244|PDB:3JQL}.
HELIX 121 124 {ECO:0000244|PDB:3JQL}.
SEQUENCE 126 AA; 13969 MW; DA6CA9CB6A447EF3 CRC64;
SNRPMPLNLY QFKNMIQCTV PSRSWQDFAD YGCYCGKGGS GTPVDDLDRC CQVHDNCYNE
AENISGCRPY FKTYSYECTQ GTLTCKGDNN ACAASVCDCD RLAAICFAGA PYNDANYNID
LKARCN


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