PA2A1_OVOOK
ID PA2A1_OVOOK Reviewed; 139 AA.
AC P00625; P79836; Q92151;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Acidic phospholipase A2 DE-I;
DE Short=svPA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A2 Ook-E6;
DE AltName: Full=Phospholipase A2 PLA2-01;
DE Flags: Precursor;
OS Ovophis okinavensis (Ryukyu Island pit viper) (Trimeresurus okinavensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Ovophis.
OX NCBI_TaxID=8769;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver, and Venom gland;
RX PubMed=8682315; DOI=10.1016/0378-1119(96)00186-2;
RA Nobuhisa I., Nakashima K., Deshimaru M., Ogawa T., Shimohigashi Y.,
RA Fukumaki Y., Sakaki Y., Hattori S., Kihara H., Ohno M.;
RT "Accelerated evolution of Trimeresurus okinavensis venom gland
RT phospholipase A2 isozyme-encoding genes.";
RL Gene 172:267-272(1996).
RN [2]
RP PROTEIN SEQUENCE OF 17-139.
RC TISSUE=Venom;
RX PubMed=7275018; DOI=10.1515/bchm2.1981.362.2.997;
RA Joubert F.J., Haylett T.;
RT "Snake venoms. Purification, some properties and amino acid sequence of a
RT phospholipase A2 (DE-I) from Trimeresurus okinavensis (Hime-habu) venom.";
RL Hoppe-Seyler's Z. Physiol. Chem. 362:997-1006(1981).
RN [3]
RP PROTEIN SEQUENCE OF 17-45, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=22115990; DOI=10.1016/j.toxicon.2011.10.016;
RA Tsai I.-H., Tsai T.-S., Wang Y.-M., Tu M.-C., Chang H.-C.;
RT "Cloning and characterization of Trimeresurus gracilis venom phospholipases
RT A(2): comparison with Ovophis okinavensis venom and the systematic
RT implications.";
RL Toxicon 59:151-157(2012).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits the
CC ADP- and collagen-induced human platelet aggregation (By similarity).
CC Exhibits high hydrolytic activities and preferred the anionic micelles
CC to the zwitterionic micelles. PLA2 catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000250, ECO:0000269|PubMed:22115990}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13786; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22115990};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; D49388; BAA08383.1; -; mRNA.
DR EMBL; D49390; BAA08385.1; ALT_SEQ; Genomic_DNA.
DR PIR; JC4874; PSTV.
DR AlphaFoldDB; P00625; -.
DR SMR; P00625; -.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0043655; C:host extracellular space; TAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
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 Calcium; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:22115990,
FT ECO:0000269|PubMed:7275018"
FT CHAIN 17..139
FT /note="Acidic phospholipase A2 DE-I"
FT /id="PRO_0000022966"
FT ACT_SITE 63
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 42..132
FT /evidence="ECO:0000250"
FT DISULFID 44..60
FT /evidence="ECO:0000250"
FT DISULFID 59..111
FT /evidence="ECO:0000250"
FT DISULFID 65..139
FT /evidence="ECO:0000250"
FT DISULFID 66..104
FT /evidence="ECO:0000250"
FT DISULFID 73..97
FT /evidence="ECO:0000250"
FT DISULFID 91..102
FT /evidence="ECO:0000250"
FT CONFLICT 39..41
FT /note="Missing (in Ref. 1; BAA08385)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="N -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..95
FT /note="EN -> ND (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 135..136
FT /note="ES -> SE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 139 AA; 15584 MW; E0FBB7B688925137 CRC64;
MRTLWIMAVL LLGVEGHLMQ FETLIMKIAG RSGVWWYGSY GCYCGAGGQG RPQDPSDRCC
FVHDCCYGKV TGCNTKDEFY TYSEENGAIT CGGENPCLKE VCECDLAAAI CFRDNLDTYN
SKKYWMFPAK NCLEESEPC
