PA2A7_GLOHA
ID PA2A7_GLOHA Reviewed; 124 AA.
AC O42191;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Acidic phospholipase A2 A;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=8714;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=9690782; DOI=10.1016/s0041-0101(98)00013-0;
RA Pan H., Liu X.-L., Ou-Yang L.-L., Yang G.-Z., Zhou Y.-C., Li Z.-P.,
RA Wu X.-F.;
RT "Diversity of cDNAs encoding phospholipase A2 from Agkistrodon halys pallas
RT venom, and its expression in E. coli.";
RL Toxicon 36:1155-1163(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH CADMIUM IONS, AND
RP DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=12504079; DOI=10.1016/s0006-291x(02)02833-4;
RA Xu S., Gu L., Jiang T., Zhou Y., Lin Z.;
RT "Structures of cadmium-binding acidic phospholipase A2 from the venom of
RT Agkistrodon halys pallas at 1.9-A resolution.";
RL Biochem. Biophys. Res. Commun. 300:271-277(2003).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71848.1; Type=Miscellaneous discrepancy; Note=The sequence shown is that displayed in the paper.; Evidence={ECO:0000305|PubMed:9690782};
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DR EMBL; AF015246; AAB71848.1; ALT_SEQ; mRNA.
DR PDB; 1M8R; X-ray; 1.90 A; A=1-124.
DR PDB; 1M8S; X-ray; 1.90 A; A=1-124.
DR PDBsum; 1M8R; -.
DR PDBsum; 1M8S; -.
DR AlphaFoldDB; O42191; -.
DR SMR; O42191; -.
DR EvolutionaryTrace; O42191; -.
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 CHAIN 1..124
FT /note="Acidic phospholipase A2 A"
FT /id="PRO_0000161602"
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:0000305|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT DISULFID 26..116
FT /evidence="ECO:0000269|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT DISULFID 43..95
FT /evidence="ECO:0000269|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT DISULFID 49..124
FT /evidence="ECO:0000269|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT DISULFID 50..88
FT /evidence="ECO:0000269|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT DISULFID 57..81
FT /evidence="ECO:0000269|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT DISULFID 75..86
FT /evidence="ECO:0000269|PubMed:12504079,
FT ECO:0007744|PDB:1M8R"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:1M8R"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1M8R"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1M8R"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1M8R"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1M8R"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:1M8R"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1M8R"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1M8R"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1M8R"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:1M8R"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1M8R"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:1M8R"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1M8R"
SQ SEQUENCE 124 AA; 13927 MW; 3A1307DD25F50B5E CRC64;
SLLQFETLIM KVAKKSGMVW YSNYGCYCGW GGQGRPQDAT DRCCFVHDCC YGKVTGCDPK
MDVYSFSEEN GDIVCGGDDP CKKEICECDR AAAICFRDNL NTYNDKKYWA FGAKNCPQEE
SEPC
