PA2A_CERCE
ID PA2A_CERCE Reviewed; 120 AA.
AC P21789;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Acidic phospholipase A2 Cc1-PLA2 {ECO:0000303|PubMed:30239061};
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Cerastes cerastes (Horned desert viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Cerastes.
OX NCBI_TaxID=8697;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=Baluchistan; TISSUE=Venom;
RX PubMed=1993470; DOI=10.1016/0014-5793(91)80072-b;
RA Siddiqi A.R., Shafqat J., Zaidi Z.H., Joernvall H.;
RT "Characterization of phospholipase A2 from the venom of Horned viper
RT (Cerastes cerastes).";
RL FEBS Lett. 278:14-16(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-31, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Tunisia; TISSUE=Venom;
RX PubMed=2402760; DOI=10.1016/0041-0101(90)90252-3;
RA Djebari F.L., Martin-Eauclaire M.-F.;
RT "Purification and characterization of a phospholipase A2 from Cerastes
RT cerastes (horn viper) snake venom.";
RL Toxicon 28:637-646(1990).
RN [3]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=30239061; DOI=10.1002/jbt.22219;
RA Fatah C., Samah S., Fatima L.D.;
RT "Antiplatelet and anticoagulant activities of two phospholipase A2s
RT purified from Cerastes cerastes venom: structure-function relationship.";
RL J. Biochem. Mol. Toxicol. 2018:E22219-E22219(2018).
CC -!- FUNCTION: This non-toxic acidic phospholipase A2 hydrolyzes monolayers
CC of different short chain phospholipids (PubMed:2402760). It exhibits
CC anticoagulant effects upon human plasma in vitro (PubMed:30239061).
CC PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides (PubMed:2402760). {ECO:0000269|PubMed:2402760,
CC ECO:0000269|PubMed:30239061}.
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, ECO:0000269|PubMed:2402760};
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:30239061}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2402760}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:2402760}.
CC -!- MISCELLANEOUS: Is non-lethal to mice up to a dose as high as 25 mg/kg
CC by intraperitoneal and intravenous injection.
CC {ECO:0000305|PubMed:2402760}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR PIR; A35950; A35950.
DR PIR; S13019; S13019.
DR AlphaFoldDB; P21789; -.
DR SMR; P21789; -.
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 Blood coagulation cascade inhibiting toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted;
KW Toxin.
FT CHAIN 1..120
FT /note="Acidic phospholipase A2 Cc1-PLA2"
FT /evidence="ECO:0000269|PubMed:1993470"
FT /id="PRO_0000161641"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 26..115
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 43..95
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 50..88
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 57..81
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT DISULFID 75..86
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT VARIANT 10..12
FT /note="FKM -> KHK (in strain: Tunisia)"
FT VARIANT 17..19
FT /note="PIF -> ALL (in strain: Tunisia)"
FT VARIANT 22..23
FT /note="GD -> SA (in strain: Tunisia)"
SQ SEQUENCE 120 AA; 13534 MW; E6581FA7001C62C3 CRC64;
NLYQFGKMIF KMTGKSPIFS YGDYGCYCGW GGKGTPVDAT DRCCFVHDCC YGRVNSCNPK
RSTYSYSFQN GGIVCDDQNL CKRAVCECDR VAAICFGENV NTYDKKYKDY PTSQCTETEQ
