PA2A_CROAT
ID PA2A_CROAT Reviewed; 138 AA.
AC P00624; Q8UVZ6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Acidic phospholipase A2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Crotalus atrox (Western diamondback rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8730;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Tsai I.-H., Chen Y.-H., Wang Y.-M., Tu A.T.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 17-138.
RC TISSUE=Venom;
RX PubMed=7061414; DOI=10.1016/s0021-9258(18)34899-3;
RA Randolph A., Heinrikson R.L.;
RT "Crotalus atrox phospholipase A2. Amino acid sequence and studies on the
RT function of the NH2-terminal region.";
RL J. Biol. Chem. 257:2155-2161(1982).
RN [3]
RP PROTEIN SEQUENCE OF 17-31; 38-69 AND 107-129, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19371136; DOI=10.1021/pr900249q;
RA Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.;
RT "Exploring the venom proteome of the western diamondback rattlesnake,
RT Crotalus atrox, via snake venomics and combinatorial peptide ligand library
RT approaches.";
RL J. Proteome Res. 8:3055-3067(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC TISSUE=Venom;
RX PubMed=7263673; DOI=10.1016/s0021-9258(19)68887-3;
RA Keith C., Feldman D.S., Deganello S., Glick J., Ward K.B., Jones E.O.,
RA Sigler P.B.;
RT "The 2.5 A crystal structure of a dimeric phospholipase A2 from the venom
RT of Crotalus atrox.";
RL J. Biol. Chem. 256:8602-8607(1981).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 17-138, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=4019493; DOI=10.1016/s0021-9258(17)39301-8;
RA Brunie S., Bolin J., Gewirth D., Sigler P.B.;
RT "The refined crystal structure of dimeric phospholipase A2 at 2.5 A. Access
RT to a shielded catalytic center.";
RL J. Biol. Chem. 260:9742-9749(1985).
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:0000250|UniProtKB:Q8AXY1};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8AXY1};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:4019493}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=13585; Method=Unknown; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:19371136};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF269131; AAL36974.1; -; mRNA.
DR PIR; A00764; PSRSAW.
DR PDB; 1PP2; X-ray; 2.50 A; L/R=17-138.
DR PDBsum; 1PP2; -.
DR AlphaFoldDB; P00624; -.
DR SMR; P00624; -.
DR EvolutionaryTrace; P00624; -.
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; Calcium; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:19371136,
FT ECO:0000269|PubMed:7061414"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2"
FT /id="PRO_0000022851"
FT ACT_SITE 63
FT /evidence="ECO:0000305|PubMed:4019493"
FT ACT_SITE 105
FT /evidence="ECO:0000305|PubMed:4019493"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 42..131
FT /evidence="ECO:0000269|PubMed:4019493,
FT ECO:0007744|PDB:1PP2"
FT DISULFID 44..60
FT /evidence="ECO:0000269|PubMed:4019493,
FT ECO:0007744|PDB:1PP2"
FT DISULFID 59..111
FT /evidence="ECO:0000269|PubMed:4019493,
FT ECO:0007744|PDB:1PP2"
FT DISULFID 65..138
FT /evidence="ECO:0000269|PubMed:4019493,
FT ECO:0007744|PDB:1PP2"
FT DISULFID 66..104
FT /evidence="ECO:0000269|PubMed:4019493,
FT ECO:0007744|PDB:1PP2"
FT DISULFID 73..97
FT /evidence="ECO:0000269|PubMed:4019493,
FT ECO:0007744|PDB:1PP2"
FT DISULFID 91..102
FT /evidence="ECO:0000269|PubMed:4019493,
FT ECO:0007744|PDB:1PP2"
FT CONFLICT 19
FT /note="V -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:1PP2"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1PP2"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1PP2"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1PP2"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1PP2"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1PP2"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:1PP2"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1PP2"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1PP2"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:1PP2"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:1PP2"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1PP2"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1PP2"
SQ SEQUENCE 138 AA; 15346 MW; 78A0034CA963A4E3 CRC64;
MRTLWIVAVL LLGVEGSLVQ FETLIMKIAG RSGLLWYSAY GCYCGWGGHG LPQDATDRCC
FVHDCCYGKA TDCNPKTVSY TYSEENGEII CGGDDPCGTQ ICECDKAAAI CFRDNIPSYD
NKYWLFPPKN CREEPEPC
