PA21_OXYSC
ID PA21_OXYSC Reviewed; 154 AA.
AC Q4VRI5; Q45Z52;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Phospholipase A2 OS1;
DE Short=PLA2;
DE EC=3.1.1.4;
DE AltName: Full=OS5;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX NCBI_TaxID=8667;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Welton R.E., Burnell J.N.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16261251; DOI=10.1007/s00018-005-5384-9;
RA St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.;
RT "Identification and analysis of venom gland-specific genes from the coastal
RT taipan (Oxyuranus scutellatus) and related species.";
RL Cell. Mol. Life Sci. 62:2679-2693(2005).
RN [3]
RP PROTEIN SEQUENCE OF 28-154.
RC TISSUE=Venom;
RX PubMed=7890672; DOI=10.1074/jbc.270.10.5534;
RA Lambeau G., Ancian P., Nicolas J.P., Beiboer S.H., Moinier D., Verheij H.,
RA Lazdunski M.;
RT "Structural elements of secretory phospholipases A2 involved in the binding
RT to M-type receptors.";
RL J. Biol. Chem. 270:5534-5540(1995).
RN [4]
RP FUNCTION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=2160984; DOI=10.1016/s0021-9258(19)38881-7;
RA Lambeau G., Schmid-Alliana A., Lazdunski M., Barhanin J.;
RT "Identification and purification of a very high affinity binding protein
RT for toxic phospholipases A2 in skeletal muscle.";
RL J. Biol. Chem. 265:9526-9532(1990).
RN [5]
RP FUNCTION, AND BIOASSAY.
RX PubMed=10548416; DOI=10.1016/s0304-3940(99)00709-0;
RA Kolko M., Bruhn T., Christensen T., Lazdunski M., Lambeau G., Bazan N.G.,
RA Diemer N.H.;
RT "Secretory phospholipase A2 potentiates glutamate-induced rat striatal
RT neuronal cell death in vivo.";
RL Neurosci. Lett. 274:167-170(1999).
RN [6]
RP FUNCTION IN CELL MIGRATION.
RX PubMed=11090064;
RA Rizzo M.T., Nguyen E., Aldo-Benson M., Lambeau G.;
RT "Secreted phospholipase A(2) induces vascular endothelial cell migration.";
RL Blood 96:3809-3815(2000).
RN [7]
RP FUNCTION, AND TOXIC DOSE.
RX PubMed=16669624; DOI=10.1021/bi060217r;
RA Rouault M., Rash L.D., Escoubas P., Boilard E., Bollinger J., Lomonte B.,
RA Maurin T., Guillaume C., Canaan S., Deregnaucourt C., Schrevel J.,
RA Doglio A., Gutierrez J.M., Lazdunski M., Gelb M.H., Lambeau G.;
RT "Neurotoxicity and other pharmacological activities of the snake venom
RT phospholipase A2 OS2: the N-terminal region is more important than
RT enzymatic activity.";
RL Biochemistry 45:5800-5816(2006).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has a low specific
CC activity on phospholipid substrates, and is neither neurotoxic, nor
CC myotoxic. Triggers cell migration (PubMed:11090064), has antimalarial
CC activity (PubMed:16669624), but is not able to potently inhibit HIV-1
CC replication (PubMed:16669624). Binds in a calcium-independent fashion
CC with very high affinity to a muscle-type (M-type) PLA2 receptor, but is
CC a very poor ligand for neuronal-type (N-type) receptors. PLA2 catalyzes
CC the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:10548416,
CC ECO:0000269|PubMed:11090064, ECO:0000269|PubMed:16669624,
CC ECO:0000269|PubMed:2160984}.
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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2160984}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- TOXIC DOSE: LD(100) is 3500 ug/kg by intracerebroventricular injection
CC into mice. {ECO:0000269|PubMed:16669624}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AY691660; AAY47069.1; -; mRNA.
DR EMBL; DQ085814; AAZ22632.1; -; mRNA.
DR AlphaFoldDB; Q4VRI5; -.
DR SMR; Q4VRI5; -.
DR PRIDE; Q4VRI5; -.
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 Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..154
FT /note="Phospholipase A2 OS1"
FT /id="PRO_5000140339"
FT ACT_SITE 75
FT /evidence="ECO:0000250"
FT ACT_SITE 126
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 38..104
FT /evidence="ECO:0000250"
FT DISULFID 54..153
FT /evidence="ECO:0000250"
FT DISULFID 56..72
FT /evidence="ECO:0000250"
FT DISULFID 71..132
FT /evidence="ECO:0000250"
FT DISULFID 78..125
FT /evidence="ECO:0000250"
FT DISULFID 88..118
FT /evidence="ECO:0000250"
FT DISULFID 111..123
FT /evidence="ECO:0000250"
SQ SEQUENCE 154 AA; 16898 MW; 26CF67BAE3852C46 CRC64;
MHPAHLLVLL AVCVSLLGAA RIPPLPLSLL NFANLIECAN HGTRSALAYA DYGCYCGKGG
RGTPLDDLDR CCHVHDDCYG EAEKLPACNY LMSSPYFNSY SYKCNEGKVT CTDDNDECKA
FICNCDRTAA ICFAGATYND ENFMISKKRN DICQ
