PA2A2_OPHHA
ID PA2A2_OPHHA Reviewed; 146 AA.
AC Q9DF33;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Acidic phospholipase A2 2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=APLA2-2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Wang Q.Y., Shu Y.Y.;
RT "Cloning and characterization of cDNAs encoding two acidic isoforms of
RT phospholipase A2 in Guangxi king cobra (Ophiophagus hannah).";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 28-146 IN COMPLEX WITH CALCIUM
RP ION, COFACTOR, AND DISULFIDE BONDS.
RX PubMed=12925787; DOI=10.1107/s0907444903014598;
RA Xu S., Gu L., Wang Q., Shu Y., Song S., Lin Z.;
RT "Structure of a king cobra phospholipase A2 determined from a hemihedrally
RT twinned crystal.";
RL Acta Crystallogr. D 59:1574-1581(2003).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that displays edema-
CC inducing and moderate anticoagulant activities. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC 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:12925787};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:12925787};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; AF302907; AAG23963.1; -; mRNA.
DR PDB; 1M8T; X-ray; 2.10 A; A/B/C/D/E/F=28-146.
DR PDBsum; 1M8T; -.
DR AlphaFoldDB; Q9DF33; -.
DR SMR; Q9DF33; -.
DR TopDownProteomics; Q9DF33; -.
DR EvolutionaryTrace; Q9DF33; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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; Blood coagulation cascade inhibiting toxin; Calcium;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..27
FT /evidence="ECO:0000255"
FT /id="PRO_0000022944"
FT CHAIN 28..146
FT /note="Acidic phospholipase A2 2"
FT /id="PRO_0000022945"
FT ACT_SITE 75
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 121
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT DISULFID 38..99
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT DISULFID 54..146
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT DISULFID 56..72
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT DISULFID 71..127
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT DISULFID 78..120
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT DISULFID 88..113
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT DISULFID 106..118
FT /evidence="ECO:0000269|PubMed:12925787,
FT ECO:0007744|PDB:1M8T"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1M8T"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1M8T"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1M8T"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1M8T"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1M8T"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:1M8T"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1M8T"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1M8T"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1M8T"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:1M8T"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1M8T"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:1M8T"
SQ SEQUENCE 146 AA; 15901 MW; 354F45F6B67690A7 CRC64;
MNPAHLLVLS AVCVSLLGAS SIPPQPLHLV QFNGMIRCTI PGSIPWWDYS DYGCYCGSGG
SGTPVDELDR CCQVHDNCYT QAQQLTECSP YSKRYSYDCS EGTLTCKADN DECAAFVCDC
DRVAAICFAG APYNKENINI DTTTRC
