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Basic phospholipase A2 BP-I (svPLA2) (EC 3.1.1.4) (Basic protein I) (BPI) (Phosphatidylcholine 2-acylhydrolase)

 PA2B1_PROFL             Reviewed;         138 AA.
P0DJJ8; B6F140; P20381;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 1.
22-NOV-2017, entry version 23.
RecName: Full=Basic phospholipase A2 BP-I;
Short=svPLA2;
EC=3.1.1.4;
AltName: Full=Basic protein I;
Short=BPI;
AltName: Full=Phosphatidylcholine 2-acylhydrolase;
Flags: Precursor;
Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Protobothrops.
NCBI_TaxID=88087;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Tokunoshima; TISSUE=Venom gland;
PubMed=1528861; DOI=10.1073/pnas.89.18.8557;
Ogawa T., Oda N., Nakashima K., Sasaki H., Hattori M., Sakaki Y.,
Kihara H., Ohno M.;
"Unusually high conservation of untranslated sequences in cDNAs for
Trimeresurus flavoviridis phospholipase A2 isozymes.";
Proc. Natl. Acad. Sci. U.S.A. 89:8557-8561(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Tokunoshima; TISSUE=Liver;
PubMed=8327468; DOI=10.1073/pnas.90.13.5964;
Nakashima K., Ogawa T., Oda N., Hattori M., Sakaki Y., Kihara H.,
Ohno M.;
"Accelerated evolution of Trimeresurus flavoviridis venom gland
phospholipase A2 isozymes.";
Proc. Natl. Acad. Sci. U.S.A. 90:5964-5968(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=7777556; DOI=10.1073/pnas.92.12.5605;
Nakashima K., Nobuhisa I., Deshimaru M., Nakai M., Ogawa T.,
Shimohigashi Y., Fukumaki Y., Hattori M., Sakaki Y., Hattori S.,
Ohno M.;
"Accelerated evolution in the protein-coding regions is universal in
crotalinae snake venom gland phospholipase A2 isozyme genes.";
Proc. Natl. Acad. Sci. U.S.A. 92:5605-5609(1995).
[4]
PROTEIN SEQUENCE OF 17-138, FUNCTION, AND COFACTOR.
TISSUE=Venom;
PubMed=2330604; DOI=10.1016/0041-0101(90)90005-R;
Yoshizumi K., Liu S.-Y., Miyata T., Saita S., Ohno M., Iwanaga S.,
Kihara H.;
"Purification and amino acid sequence of basic protein I, a lysine-49-
phospholipase A2 with low activity, from the venom of Trimeresurus
flavoviridis (Habu snake).";
Toxicon 28:43-54(1990).
-!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has strong
myotoxic activity with a low phospholipase A2 activity. PLA2
catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
3-sn-phosphoglycerides. {ECO:0000269|PubMed:2330604}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:2330604};
Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:2330604};
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- MISCELLANEOUS: Is abundantly expressed in Tokunoshima and Amami-
Oshima P.flavoviridis venom, but is missing in Okinawa
P.flavoviridis venom. It is thought that loss of BP-I in Okinawa
P.flavoviridis is due to lack of necessity for a strong toxicity
exerted by BP-I in the venom as far as they feed mostly on frogs.
-!- SIMILARITY: Belongs to the phospholipase A2 family. Group II
subfamily. K49 sub-subfamily. {ECO:0000305}.
-!- CAUTION: Binds calcium very weakly as one of the calcium-binding
ligands is lost (Asp->Lys in position 64, which corresponds to
'Lys-49' in the current nomenclature). {ECO:0000305}.
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EMBL; D10718; BAA01561.1; -; mRNA.
EMBL; D13383; BAA02651.1; -; Genomic_DNA.
PIR; D48188; D48188.
ProteinModelPortal; P0DJJ8; -.
SMR; P0DJJ8; -.
HOVERGEN; HBG008137; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
CDD; cd00125; PLA2c; 1.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR033112; PLipase_A2_Asp_AS.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
PANTHER; PTHR11716; PTHR11716; 1.
Pfam; PF00068; Phospholip_A2_1; 1.
PRINTS; PR00389; PHPHLIPASEA2.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00119; PA2_ASP; 1.
PROSITE; PS00118; PA2_HIS; 1.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond; Hydrolase;
Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin;
Secreted; Signal; Toxin.
SIGNAL 1 16 {ECO:0000269|PubMed:2330604}.
CHAIN 17 138 Basic phospholipase A2 BP-I.
/FTId=PRO_0000022953.
ACT_SITE 63 63 {ECO:0000250}.
ACT_SITE 106 106 {ECO:0000250}.
METAL 45 45 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 47 47 Calcium; via carbonyl oxygen.
{ECO:0000250}.
DISULFID 42 132 {ECO:0000250}.
DISULFID 44 60 {ECO:0000250}.
DISULFID 59 112 {ECO:0000250}.
DISULFID 65 138 {ECO:0000250}.
DISULFID 66 105 {ECO:0000250}.
DISULFID 73 98 {ECO:0000250}.
DISULFID 91 103 {ECO:0000250}.
SEQUENCE 138 AA; 15537 MW; D91791C6D13B7D06 CRC64;
MRTLWIMAVL LLGVDGSLVQ LWKMIFQETG KEAAKNYGLY GCNCGVGRRG KPKDATDSCC
YVHKCCYKKV TGCDPKMDSY SYSWKNKAIV CGEKNPPCLK QVCECDKAVA ICLRENLGTY
NKKYTIYPKP FCKKADTC


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