PA2A_GLOBL
ID PA2A_GLOBL Reviewed; 122 AA.
AC P20249;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Acidic phospholipase A2;
DE Short=PA2-II;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=242054;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=2914966; DOI=10.1016/s0021-9258(18)94114-1;
RA Tomoo K., Ohishi H., Ishida T., Inoue M., Ikeda K., Aoki Y., Samejima Y.;
RT "Revised amino acid sequence, crystallization, and preliminary X-ray
RT diffraction analysis of acidic phospholipase A2 from the venom of
RT Agkistrodon halys blomhoffii.";
RL J. Biol. Chem. 264:3636-3638(1989).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=4430362; DOI=10.1016/0014-5793(74)81045-8;
RA Samejima Y., Iwanaga S., Suzuki T.;
RT "Complete amino acid sequence of phospholipase A2-II isolated from
RT Agkistrodon halys blomhoffii venom.";
RL FEBS Lett. 47:348-351(1974).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCIUM ION,
RP COFACTOR, AND DISULFIDE BONDS.
RX PubMed=1567418; DOI=10.1016/0006-291x(92)91169-q;
RA Tomoo K., Ohishi H., Doi M., Ishida T., Inoue M., Ikeda K., Hata Y.,
RA Samejima Y.;
RT "Structure of acidic phospholipase A2 for the venom of Agkistrodon halys
RT blomhoffii at 2.8-A resolution.";
RL Biochem. Biophys. Res. Commun. 184:137-143(1992).
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:1567418};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000305|PubMed:1567418};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Is not neurotoxic.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P20249; -.
DR SMR; P20249; -.
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.
FT CHAIN 1..122
FT /note="Acidic phospholipase A2"
FT /evidence="ECO:0000269|PubMed:2914966"
FT /id="PRO_0000161596"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P06859"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1567418"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1567418"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:1567418"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1567418"
FT DISULFID 26..115
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 49..122
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:O42191"
SQ SEQUENCE 122 AA; 13664 MW; 9728BC3E27CC5474 CRC64;
SLMQFETLIM KIAGRSGIWY YGSYGCYCGA GGQGRPQDAS DRCCFVHDCC YGKVTGCDPK
LDVYTYTEEN GAIVCGGDDP CKKQICECDK DAAICFRDNI DTYDNKYWFF PAKNCQEESE
PC
