PA2B3_PROFL
ID PA2B3_PROFL Reviewed; 138 AA.
AC C7G1G6;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Basic phospholipase A2 BP-III;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Basic protein III;
DE Short=BPIII;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 88-100, FUNCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Amami-Oshima; TISSUE=Venom, and Venom gland;
RX PubMed=19463843; DOI=10.1016/j.toxicon.2009.05.003;
RA Murakami T., Kariu T., Takazaki S., Hattori S., Chijiwa T., Ohno M.,
RA Oda-Ueda N.;
RT "Island specific expression of a novel [Lys(49)]phospholipase A(2) (BPIII)
RT in Protobothrops flavoviridis venom in Amami-Oshima, Japan.";
RL Toxicon 54:399-407(2009).
RN [2]
RP ERRATUM OF PUBMED:19463843.
RA Murakami T., Kariu T., Takazaki S., Hattori S., Chijiwa T., Ohno M.,
RA Oda-Ueda N.;
RL Toxicon 55:171-172(2010).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has low
CC phospholipase A2 activity (By similarity). Shows anticoagulant
CC activities, strong myolytic activity, infiltration of polymorphonuclear
CC cells, and edema in stromal tissues. Induces cell death of Jurkat cells
CC in a concentration dependent manner. PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000250, ECO:0000269|PubMed:19463843}.
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 -!- MISCELLANEOUS: Is expressed in Amami-Oshima P.flavoviridis venom, but
CC is missing in Tokunoshima P.flavoviridis venom.
CC {ECO:0000305|PubMed:19463843}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC K49 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Binds calcium very weakly as one of the calcium-binding
CC ligands is lost (Asp->Lys in position 64, which corresponds to 'Lys-49'
CC in the current nomenclature). {ECO:0000305}.
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DR EMBL; AB470470; BAH97119.1; -; mRNA.
DR AlphaFoldDB; C7G1G6; -.
DR SMR; C7G1G6; -.
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:InterPro.
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; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Myotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..138
FT /note="Basic phospholipase A2 BP-III"
FT /id="PRO_5000503609"
FT ACT_SITE 63
FT /evidence="ECO:0000250"
FT ACT_SITE 106
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 42..132
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 59..112
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 65..138
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 66..105
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 73..98
FT /evidence="ECO:0000250|UniProtKB:Q90249"
FT DISULFID 91..103
FT /evidence="ECO:0000250|UniProtKB:Q90249"
SQ SEQUENCE 138 AA; 15508 MW; C21971C82E2F23A7 CRC64;
MRTLWIMAVL LVGVDGSLVQ LWKMIFQETG KEAAKNYGLY GCNCGVGRRG KPKDATDSCC
YVHKCCYKKV TGCNPKMDSY SYSWKNKAIV CGENNPPCLK QVCECDKAVA ICLRENLGTY
NKKYTIYPKP FCKKADTC
