ID PA2A_CROAD Reviewed; 138 AA. AC P00623; F8S100; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 02-SEP-2026, entry version 115. DE RecName: Full=Acidic phospholipase A2 beta; DE Short=svPLA2; DE EC=3.1.1.4; DE AltName: Full=Phosphatidylcholine 2-acylhydrolase; DE Flags: Precursor; OS Crotalus adamanteus (Eastern 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=8729; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Venom gland; RX PubMed=21255598; DOI=10.1016/j.toxicon.2011.01.008; RA Rokyta D.R., Wray K.P., Lemmon A.R., Lemmon E.M., Caudle S.B.; RT "A high-throughput venom-gland transcriptome for the eastern diamondback RT rattlesnake (Crotalus adamanteus) and evidence for pervasive positive RT selection across toxin classes."; RL Toxicon 57:657-671(2011). RN [2] RP PROTEIN SEQUENCE OF 17-138, AND SUBUNIT. RC TISSUE=Venom; RX PubMed=873920; DOI=10.1016/s0021-9258(17)40140-2; RA Heinrikson R.L., Krueger E.T., Keim P.S.; RT "Amino acid sequence of phospholipase A2-alpha from the venom of Crotalus RT adamanteus. A new classification of phospholipases A2 based upon structural RT determinants."; RL J. Biol. Chem. 252:4913-4921(1977). 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; Evidence={ECO:0000250}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:873920}. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HQ414104; AEJ31982.1; -; mRNA. DR PIR; A00763; PSRSAE. DR SMR; P00623; -. DR BindingDB; P00623; -. DR ChEMBL; CHEMBL5711; -. DR CDD; cd00125; PLA2c; 1. DR FunFam; 1.20.90.10:FF:000001; Basic phospholipase A2 homolog; 1. DR Gene3D; 1.20.90.10; Phospholipase A2 domain; 1. DR InterPro; IPR001211; PLA2. DR InterPro; IPR016090; PLA2-like_dom. DR InterPro; IPR033112; PLA2_Asp_AS. DR InterPro; IPR033113; PLA2_histidine. DR InterPro; IPR036444; PLipase_A2_dom_sf. DR PANTHER; PTHR11716; PHOSPHOLIPASE A2 FAMILY MEMBER; 1. DR PANTHER; PTHR11716:SF9; PHOSPHOLIPASE A2, MEMBRANE ASSOCIATED; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1. DR PROSITE; PS00119; PA2_ASP; 1. DR PROSITE; PS00118; PA2_HIS; 1. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004623; F:A2-type glycerophospholipase activity; IEA:UniProtKB-EC. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter. DR GO; GO:0050482; P:arachidonate secretion; IEA:InterPro. DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro. DR GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:TreeGrafter. DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro. DR AlphaFoldDB; P00623; -. PE 1: Evidence at protein level; KW Calcium; Direct protein sequencing; Disulfide bond; Hydrolase; KW Lipid degradation; Lipid metabolism; Metal-binding; Secreted; Signal; KW Toxin. FT SIGNAL 1..16 FT /evidence="ECO:0000269|PubMed:873920" FT CHAIN 17..138 FT /note="Acidic phospholipase A2 beta" FT /id="PRO_0000161642" FT ACT_SITE 63 FT /evidence="ECO:0000250|UniProtKB:P06859" FT ACT_SITE 105 FT /evidence="ECO:0000250|UniProtKB:P06859" 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:0000250|UniProtKB:O42191" FT DISULFID 44..60 FT /evidence="ECO:0000250|UniProtKB:O42191" FT DISULFID 59..111 FT /evidence="ECO:0000250|UniProtKB:O42191" FT DISULFID 65..138 FT /evidence="ECO:0000250|UniProtKB:O42191" FT DISULFID 66..104 FT /evidence="ECO:0000250|UniProtKB:O42191" FT DISULFID 73..97 FT /evidence="ECO:0000250|UniProtKB:O42191" FT DISULFID 91..102 FT /evidence="ECO:0000250|UniProtKB:O42191" FT VARIANT 133 FT /note="E -> Q (in the alpha form)" FT CONFLICT 72 FT /note="D -> N (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="N -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 138 AA; 15433 MW; 71B48637E52C9E0A CRC64; MRTLWIVAVL LLGVEGSLVQ FETLIMKVAK RSGLLWYSAY GCYCGWGGHG RPQDATDRCC FVHDCCYGKA TDCNPKTVSY TYSEENGEIV CGGDDPCGTQ ICECDKAAAI CFRDNIPSYD NKYWLFPPKN CREEPEPC //