PA2B2_PROFL
ID PA2B2_PROFL Reviewed; 138 AA.
AC P0DJJ9; B6F140; P20381;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Basic phospholipase A2 BP-II;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Basic protein II {ECO:0000303|PubMed:1528861, ECO:0000303|PubMed:2341374, ECO:0000303|PubMed:30787342, ECO:0000303|PubMed:7777556, ECO:0000303|PubMed:8327468};
DE Short=BP2 {ECO:0000303|PubMed:1528861};
DE Short=BPII {ECO:0000303|PubMed:30787342, ECO:0000303|PubMed:7777556, ECO:0000303|PubMed:8327468};
DE AltName: Full=PflLys49-PLA2 BPII {ECO:0000303|PubMed:30787342};
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].
RC STRAIN=Tokunoshima; TISSUE=Venom gland;
RX PubMed=1528861; DOI=10.1073/pnas.89.18.8557;
RA Ogawa T., Oda N., Nakashima K., Sasaki H., Hattori M., Sakaki Y.,
RA Kihara H., Ohno M.;
RT "Unusually high conservation of untranslated sequences in cDNAs for
RT Trimeresurus flavoviridis phospholipase A2 isozymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8557-8561(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tokunoshima; TISSUE=Liver;
RX PubMed=8327468; DOI=10.1073/pnas.90.13.5964;
RA Nakashima K., Ogawa T., Oda N., Hattori M., Sakaki Y., Kihara H., Ohno M.;
RT "Accelerated evolution of Trimeresurus flavoviridis venom gland
RT phospholipase A2 isozymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5964-5968(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=7777556; DOI=10.1073/pnas.92.12.5605;
RA Nakashima K., Nobuhisa I., Deshimaru M., Nakai M., Ogawa T.,
RA Shimohigashi Y., Fukumaki Y., Hattori M., Sakaki Y., Hattori S., Ohno M.;
RT "Accelerated evolution in the protein-coding regions is universal in
RT crotalinae snake venom gland phospholipase A2 isozyme genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5605-5609(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Amami-Oshima; TISSUE=Liver;
RX PubMed=20406671; DOI=10.1016/j.gene.2010.04.001;
RA Ikeda N., Chijiwa T., Matsubara K., Oda-Ueda N., Hattori S., Matsuda Y.,
RA Ohno M.;
RT "Unique structural characteristics and evolution of a cluster of venom
RT phospholipase A2 isozyme genes of Protobothrops flavoviridis snake.";
RL Gene 461:15-25(2010).
RN [5]
RP PROTEIN SEQUENCE OF 17-138, FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=2341374; DOI=10.1093/oxfordjournals.jbchem.a123057;
RA Liu S.-Y., Yoshizumi K., Oda N., Ohno M., Tokunaga F., Iwanaga S.,
RA Kihara H.;
RT "Purification and amino acid sequence of basic protein II, a lysine-49-
RT phospholipase A2 with low activity, from Trimeresurus flavoviridis venom.";
RL J. Biochem. 107:400-408(1990).
RN [6]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Amami-Oshima, and Tokunoshima; TISSUE=Venom;
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 [7]
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 17-138, DISULFIDE BOND, MASS
RP SPECTROMETRY, AND SUBUNIT.
RC STRAIN=Amami-Oshima;
RX PubMed=30787342; DOI=10.1038/s41598-019-38861-8;
RA Matsui T., Kamata S., Ishii K., Maruno T., Ghanem N., Uchiyama S., Kato K.,
RA Suzuki A., Oda-Ueda N., Ogawa T., Tanaka Y.;
RT "SDS-induced oligomerization of Lys49-phospholipase A2 from snake venom.";
RL Sci. Rep. 9:2330-2330(2019).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that 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. Shows a low phospholipase A2
CC activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:19463843,
CC ECO:0000269|PubMed:2341374}.
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:0000269|PubMed:2341374};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:2341374};
CC -!- SUBUNIT: Exists as a monomer in both solution and crystal states
CC (PubMed:30787342). In the presence of SDS or probably in the presence
CC of phospholipids, assembles to form SDS-resistant stable oligomers
CC (PubMed:30787342). {ECO:0000269|PubMed:30787342}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2341374}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:2341374}.
CC -!- MASS SPECTROMETRY: Mass=13753; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:30787342};
CC -!- MISCELLANEOUS: Is abundantly expressed in Tokunoshima and Amami-Oshima
CC P.flavoviridis venom, but is missing in Okinawa P.flavoviridis venom.
CC It is thought that loss of BP-II in Okinawa P.flavoviridis is due to
CC lack of necessity for a strong toxicity exerted by BP-II in the venom
CC as far as they feed mostly on frogs.
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|PubMed:2341374}.
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DR EMBL; D10719; BAA01562.1; -; mRNA.
DR EMBL; D13384; BAA02652.1; -; Genomic_DNA.
DR EMBL; AB440236; BAG82668.1; -; Genomic_DNA.
DR PIR; E48188; E48188.
DR PDB; 6AL3; X-ray; 2.57 A; A/B/C/D=17-138.
DR PDBsum; 6AL3; -.
DR AlphaFoldDB; P0DJJ9; -.
DR SMR; P0DJJ9; -.
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 3D-structure; Blood coagulation cascade inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Myotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:2341374"
FT CHAIN 17..138
FT /note="Basic phospholipase A2 BP-II"
FT /evidence="ECO:0000269|PubMed:2341374"
FT /id="PRO_0000419282"
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:0000269|PubMed:30787342,
FT ECO:0007744|PDB:6AL3"
FT DISULFID 44..60
FT /evidence="ECO:0000269|PubMed:30787342,
FT ECO:0007744|PDB:6AL3"
FT DISULFID 59..112
FT /evidence="ECO:0000269|PubMed:30787342,
FT ECO:0007744|PDB:6AL3"
FT DISULFID 65..138
FT /evidence="ECO:0000269|PubMed:30787342,
FT ECO:0007744|PDB:6AL3"
FT DISULFID 66..105
FT /evidence="ECO:0000269|PubMed:30787342,
FT ECO:0007744|PDB:6AL3"
FT DISULFID 73..98
FT /evidence="ECO:0000269|PubMed:30787342,
FT ECO:0007744|PDB:6AL3"
FT DISULFID 91..103
FT /evidence="ECO:0000269|PubMed:30787342,
FT ECO:0007744|PDB:6AL3"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:6AL3"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:6AL3"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:6AL3"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6AL3"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:6AL3"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6AL3"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:6AL3"
FT HELIX 97..115
FT /evidence="ECO:0007829|PDB:6AL3"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6AL3"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:6AL3"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6AL3"
SQ SEQUENCE 138 AA; 15522 MW; C21971C82A3B72E6 CRC64;
MRTLWIMAVL LVGVDGSLVQ LWKMIFQETG KEAAKNYGLY GCNCGVGRRG KPKDATDSCC
YVHKCCYKKV TGCNPKMDSY SYSWKNKAIV CGEKNPPCLK QVCECDKAVA ICLRENLGTY
NKKYTIYPKP FCKKADTC
