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PA2B1_NAJSG
ID   PA2B1_NAJSG             Reviewed;         126 AA.
AC   P60043;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Basic phospholipase A2 1;
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., Saravanan K., Hariprasad R.G., Jabeen T., Sharma S.,
RA   Singh T.P., Srinivasan A.;
RT   "Phospholipase A2 isoform from Indian cobra.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 8-126 IN COMPLEX WITH ISOFORM 2
RP   AND CALCIUM ION, COFACTOR, AND DISULFIDE BONDS.
RX   PubMed=15828003; DOI=10.1002/prot.20464;
RA   Jabeen T., Sharma S., Singh N., Singh R.K., Kaur P., Perbandt M.,
RA   Betzel C., Srinivasan A., Singh T.P.;
RT   "Crystal structure of a calcium-induced dimer of two isoforms of cobra
RT   phospholipase A2 at 1.6 A resolution.";
RL   Proteins 59:856-863(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:15828003};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:15828003};
CC   -!- SUBUNIT: Heterodimer formed between two homologous isoforms: isoform 1
CC       and isoform 2. {ECO:0000269|PubMed:15828003}.
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; AY422775; AAR00253.2; -; mRNA.
DR   PDB; 1MH2; X-ray; 2.70 A; A=8-126.
DR   PDB; 1MH7; X-ray; 2.00 A; A=8-126.
DR   PDB; 1MH8; X-ray; 1.86 A; A=8-126.
DR   PDB; 1S6B; X-ray; 1.60 A; A=8-126.
DR   PDB; 1XXW; X-ray; 2.70 A; A=8-125.
DR   PDB; 2RD4; X-ray; 2.97 A; A=8-126.
DR   PDBsum; 1MH2; -.
DR   PDBsum; 1MH7; -.
DR   PDBsum; 1MH8; -.
DR   PDBsum; 1S6B; -.
DR   PDBsum; 1XXW; -.
DR   PDBsum; 2RD4; -.
DR   AlphaFoldDB; P60043; -.
DR   SMR; P60043; -.
DR   PRIDE; P60043; -.
DR   EvolutionaryTrace; P60043; -.
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_0000022924"
FT   CHAIN           8..126
FT                   /note="Basic phospholipase A2 1"
FT                   /id="PRO_0000022925"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000250|UniProtKB:P14418"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000250|UniProtKB:P14418"
FT   BINDING         34
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   BINDING         36
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   BINDING         38
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   DISULFID        18..78
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   DISULFID        33..125
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   DISULFID        35..51
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   DISULFID        50..106
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   DISULFID        57..99
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   DISULFID        67..92
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   DISULFID        85..97
FT                   /evidence="ECO:0000269|PubMed:15828003,
FT                   ECO:0007744|PDB:1S6B"
FT   NON_TER         1
FT   HELIX           9..19
FT                   /evidence="ECO:0007829|PDB:1S6B"
FT   HELIX           26..29
FT                   /evidence="ECO:0007829|PDB:1S6B"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:1S6B"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1S6B"
FT   HELIX           46..61
FT                   /evidence="ECO:0007829|PDB:1S6B"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:1S6B"
FT   STRAND          76..79
FT                   /evidence="ECO:0007829|PDB:1S6B"
FT   STRAND          82..85
FT                   /evidence="ECO:0007829|PDB:1S6B"
FT   HELIX           91..109
FT                   /evidence="ECO:0007829|PDB:1S6B"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:1S6B"
FT   HELIX           121..124
FT                   /evidence="ECO:0007829|PDB:1S6B"
SQ   SEQUENCE   126 AA;  14003 MW;  07D0BFA119F6A8B2 CRC64;
     SNRPMPLNTY QFKNMIQCTV PKRSWWDFAD YGCYCGRGGS GTPIDDLDRC CQVHDNCYNS
     AREQGGCRPK QKTYSYECKA GTLSCSGSNN SCAATVCDCD RLAAICFAGA PYNDNNYNID
     LKARCQ
 
 
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