PA2B1_PROFL
ID PA2B1_PROFL Reviewed; 138 AA.
AC P0DJJ8; B6F140; P20381;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Basic phospholipase A2 BP-I;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Basic protein I {ECO:0000303|PubMed:1528861, ECO:0000303|PubMed:7777556, ECO:0000303|PubMed:8327468};
DE Short=BP1 {ECO:0000303|PubMed:1528861};
DE Short=BPI {ECO:0000303|PubMed:7777556, ECO:0000303|PubMed:8327468};
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 PROTEIN SEQUENCE OF 17-138, FUNCTION, AND COFACTOR.
RC TISSUE=Venom;
RX PubMed=2330604; DOI=10.1016/0041-0101(90)90005-r;
RA Yoshizumi K., Liu S.-Y., Miyata T., Saita S., Ohno M., Iwanaga S.,
RA Kihara H.;
RT "Purification and amino acid sequence of basic protein I, a lysine-49-
RT phospholipase A2 with low activity, from the venom of Trimeresurus
RT flavoviridis (Habu snake).";
RL Toxicon 28:43-54(1990).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has strong myotoxic
CC activity with a low phospholipase A2 activity. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:2330604}.
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:2330604};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:2330604};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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-I in Okinawa P.flavoviridis is due to
CC lack of necessity for a strong toxicity exerted by BP-I in the venom as
CC 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}.
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DR EMBL; D10718; BAA01561.1; -; mRNA.
DR EMBL; D13383; BAA02651.1; -; Genomic_DNA.
DR PIR; D48188; D48188.
DR AlphaFoldDB; P0DJJ8; -.
DR SMR; P0DJJ8; -.
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 Direct protein sequencing; Disulfide bond; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Myotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:2330604"
FT CHAIN 17..138
FT /note="Basic phospholipase A2 BP-I"
FT /id="PRO_0000022953"
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; 15537 MW; D91791C6D13B7D06 CRC64;
MRTLWIMAVL LLGVDGSLVQ LWKMIFQETG KEAAKNYGLY GCNCGVGRRG KPKDATDSCC
YVHKCCYKKV TGCDPKMDSY SYSWKNKAIV CGEKNPPCLK QVCECDKAVA ICLRENLGTY
NKKYTIYPKP FCKKADTC
