PA2A6_NAJSG
ID PA2A6_NAJSG Reviewed; 125 AA.
AC Q5G290;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Acidic phospholipase A2 6;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A2 molecule B;
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], X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 8-125,
RP MASS SPECTROMETRY, SUBUNIT, AND DISULFIDE BONDS.
RC TISSUE=Venom, and Venom gland;
RX PubMed=16287060; DOI=10.1002/prot.20708;
RA Jabeen T., Singh N., Singh R.K., Jasti J., Sharma S., Kaur P.,
RA Srinivasan A., Singh T.P.;
RT "Crystal structure of a heterodimer of phospholipase A2 from Naja naja
RT sagittifera at 2.3 A resolution reveals the presence of a new PLA2-like
RT protein with a novel Cys 32-Cys 49 disulphide bridge with a bound sugar at
RT the substrate-binding site.";
RL Proteins 62:329-337(2006).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000250}.
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:0000250|UniProtKB:Q6T179};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:Q6T179};
CC -!- SUBUNIT: Heterodimer formed between isoform 5 and isoform 6 in presence
CC of zinc ion and monomer in absence of zinc ion.
CC {ECO:0000269|PubMed:16287060}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=12705.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16287060};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AY862400; AAW65726.1; -; mRNA.
DR PDB; 1Y75; X-ray; 2.30 A; B=8-125.
DR PDBsum; 1Y75; -.
DR AlphaFoldDB; Q5G290; -.
DR SMR; Q5G290; -.
DR PRIDE; Q5G290; -.
DR EvolutionaryTrace; Q5G290; -.
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; Signal; Zinc.
FT SIGNAL <1..1
FT /evidence="ECO:0000255"
FT PROPEP 2..7
FT /evidence="ECO:0000250"
FT /id="PRO_0000346753"
FT CHAIN 8..125
FT /note="Acidic phospholipase A2 6"
FT /id="PRO_5000094847"
FT ACT_SITE 53
FT /evidence="ECO:0000250|UniProtKB:Q6T179"
FT ACT_SITE 99
FT /evidence="ECO:0000250|UniProtKB:Q6T179"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:16287060,
FT ECO:0007744|PDB:1Y75"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q6T179"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q6T179"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q6T179"
FT DISULFID 18..77
FT /evidence="ECO:0000269|PubMed:16287060,
FT ECO:0007744|PDB:1Y75"
FT DISULFID 33..124
FT /evidence="ECO:0000269|PubMed:16287060,
FT ECO:0007744|PDB:1Y75"
FT DISULFID 35..50
FT /evidence="ECO:0000269|PubMed:16287060,
FT ECO:0007744|PDB:1Y75"
FT DISULFID 49..105
FT /evidence="ECO:0000269|PubMed:16287060,
FT ECO:0007744|PDB:1Y75"
FT DISULFID 56..98
FT /evidence="ECO:0000269|PubMed:16287060,
FT ECO:0007744|PDB:1Y75"
FT DISULFID 66..91
FT /evidence="ECO:0000269|PubMed:16287060,
FT ECO:0007744|PDB:1Y75"
FT DISULFID 84..96
FT /evidence="ECO:0000269|PubMed:16287060,
FT ECO:0007744|PDB:1Y75"
FT NON_TER 1
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:1Y75"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1Y75"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1Y75"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:1Y75"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1Y75"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1Y75"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1Y75"
FT HELIX 90..108
FT /evidence="ECO:0007829|PDB:1Y75"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1Y75"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1Y75"
SQ SEQUENCE 125 AA; 13501 MW; 2237D8FA493ED6AA CRC64;
SNRPMPLNIK QFNNMIQCTV PARSWWDFAD YGCYCGSGSG SPVDDLDRCC QVHDNCYNAG
GGVTGCAPKS KTYTYECSQG TLTCSGENSA CAATVCDCDR LAAICFAGAP YNDNNYNIDL
KSRCQ
