PA2_POROP
ID PA2_POROP Reviewed; 121 AA.
AC C0HLF0;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 1.
DT 03-AUG-2022, entry version 8.
DE RecName: Full=Basic phospholipase A2 {ECO:0000303|PubMed:29886171};
DE Short=PoPLA2 {ECO:0000303|PubMed:29886171};
DE Short=PophPLA2 {ECO:0000303|PubMed:29886171};
DE Short=svPLA2 {ECO:0000305};
DE EC=3.1.1.4 {ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000269|PubMed:29886171};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000305};
OS Porthidium ophryomegas (Slender hognose viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Porthidium.
OX NCBI_TaxID=44717;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=Costa Rica {ECO:0000303|PubMed:29886171};
RC TISSUE=Venom {ECO:0000303|PubMed:29886171};
RX PubMed=29886171; DOI=10.1016/j.ijbiomac.2018.06.028;
RA Vindas J., Carrera Y., Lomonte B., Gutierrez J.M., Calvete J.J., Sanz L.,
RA Fernandez J.;
RT "A novel pentameric phospholipase A2 myotoxin (PophPLA2) from the venom of
RT the pit viper Porthidium ophryomegas.";
RL Int. J. Biol. Macromol. 118:1-8(2018).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that displays moderate
CC myotoxic activity in vivo, and cytotoxic activity in vitro. In vitro,
CC shows anticoagulant activity on human plasma and in mice causes
CC inflammatory cell infiltration and myonecrosis in the gastrocnemius
CC muscles of CD-1 mice 3 hours after injection (100 ug). PLA2 catalyzes
CC the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:29886171}.
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:29886171};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:29886171};
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:29886171}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29886171}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:29886171}.
CC -!- MASS SPECTROMETRY: Mass=14044; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:29886171};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; C0HLF0; -.
DR SMR; C0HLF0; -.
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; Myotoxin;
KW Phosphoprotein; Secreted; Toxin.
FT CHAIN 1..121
FT /note="Basic phospholipase A2"
FT /evidence="ECO:0000269|PubMed:29886171"
FT /id="PRO_0000446057"
FT ACT_SITE 47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10036"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 26..114
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 28..44
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 43..94
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 49..121
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 50..87
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 57..80
FT /evidence="ECO:0000250|UniProtKB:P14421"
FT DISULFID 74..85
FT /evidence="ECO:0000250|UniProtKB:P14421"
SQ SEQUENCE 121 AA; 14051 MW; 1B46CDEBA3AA261E CRC64;
NLFQFRKMIK KMTKKEPVVY YAFYGCYCGK GGRGKPKDAT DRCCFVHDCC YEKVTGCNPK
WGYYTYSMNK QIVCGGDDPC KKQVCECDKA AAICFRDNLK TYKKKYMSFP NFFCTDPSEK
C
