PA2A1_PROFL
ID PA2A1_PROFL Reviewed; 138 AA.
AC P06859; Q92118;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Acidic phospholipase A2 1;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A2 isozyme I;
DE AltName: Full=pgPLA 1a/pgPLA 2a;
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 TISSUE=Venom gland;
RX PubMed=1707052; DOI=10.1093/oxfordjournals.jbchem.a123286;
RA Oda N., Ogawa T., Ohno M., Sasaki H., Sakaki Y., Kihara H.;
RT "Cloning and sequence analysis of cDNA for Trimeresurus flavoviridis
RT phospholipase A2, and consequent revision of the amino acid sequence.";
RL J. Biochem. 108:816-821(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOZYME [THR37]PLA2).
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=7765285; DOI=10.1271/bbb.58.1510;
RA Nakashima K., Nobuhisa I., Ogawa T., Hattori M., Sakaki Y., Kihara H.,
RA Ohno M.;
RT "Polymorphisms of Trimeresurus flavoviridis venom gland phospholipase A2
RT isozyme genes.";
RL Biosci. Biotechnol. Biochem. 58:1510-1511(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 17-36.
RC STRAIN=Amami-Oshima, and Okinawa; TISSUE=Venom, and Venom gland;
RX PubMed=12612832; DOI=10.1007/s00239-002-2400-7;
RA Chijiwa T., Yamaguchi Y., Ogawa T., Deshimaru M., Nobuhisa I.,
RA Nakashima K., Oda-Ueda N., Fukumaki Y., Hattori S., Ohno M.;
RT "Interisland evolution of Trimeresurus flavoviridis venom phospholipase
RT A(2) isozymes.";
RL J. Mol. Evol. 56:286-293(2003).
RN [6]
RP PROTEIN SEQUENCE OF 17-138.
RC TISSUE=Venom;
RX PubMed=3514593; DOI=10.1093/oxfordjournals.jbchem.a135471;
RA Tanaka S., Mohri N., Kihara H., Ohno M.;
RT "Amino acid sequence of Trimeresurus flavoviridis phospholipase A2.";
RL J. Biochem. 99:281-289(1986).
RN [7]
RP PROTEIN SEQUENCE OF 17-47.
RC TISSUE=Venom;
RX PubMed=3564060; DOI=10.1016/0041-0101(86)90138-8;
RA Kini R.M., Kawabata S., Iwanaga S.;
RT "Comparison of amino terminal region of three isoenzymes of phospholipases
RT A2 (TFV PL-Ia, TFV PL-Ib, TFV PL-X) from Trimeresurus flavoviridis (habu
RT snake) venom and the complete amino acid sequence of the basic
RT phospholipase, TFV PL-X.";
RL Toxicon 24:1117-1129(1986).
RN [8]
RP FUNCTION.
RX PubMed=1288500;
RA Kihara H., Uchikawa R., Hattori S., Ohno M.;
RT "Myotoxicity and physiological effects of three Trimeresurus flavoviridis
RT phospholipases A2.";
RL Biochem. Int. 28:895-903(1992).
RN [9]
RP ACTIVE SITES.
RX PubMed=2628422; DOI=10.1093/oxfordjournals.jbchem.a122963;
RA Kohzuma T., Oda N., Kihara H., Ohno M.;
RT "Investigation of an active site histidine-aspartate couple in Trimeresurus
RT flavoviridis phospholipase A2.";
RL J. Biochem. 106:1054-1058(1989).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that is highly lipolytic
CC and myolytic. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:1288500}.
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 per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; D10070; BAA00962.1; -; mRNA.
DR EMBL; D10720; BAA01563.1; -; mRNA.
DR EMBL; D10722; BAA01565.1; -; Genomic_DNA.
DR EMBL; D10724; BAA01567.1; -; Genomic_DNA.
DR EMBL; AB072174; BAB68547.1; -; mRNA.
DR EMBL; AB072175; BAB68548.1; -; mRNA.
DR PIR; A46169; A46169.
DR PIR; A48188; A48188.
DR PIR; B48188; PSTVIF.
DR AlphaFoldDB; P06859; -.
DR SMR; P06859; -.
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 Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:12612832,
FT ECO:0000269|PubMed:3514593, ECO:0000269|PubMed:3564060"
FT CHAIN 17..138
FT /note="Acidic phospholipase A2 1"
FT /evidence="ECO:0000269|PubMed:3514593"
FT /id="PRO_0000022952"
FT ACT_SITE 63
FT /evidence="ECO:0000269|PubMed:2628422"
FT ACT_SITE 104
FT /evidence="ECO:0000269|PubMed:2628422"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 42..131
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 44..60
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 59..110
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 65..138
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 66..103
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 73..97
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT DISULFID 91..101
FT /evidence="ECO:0000250|UniProtKB:O42191"
FT VARIANT 15
FT /note="D -> E"
FT VARIANT 53
FT /note="K -> T (in isozyme [Thr37]PLA2)"
FT CONFLICT 85..88
FT /note="NNGD -> QGN (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="E -> G (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95..97
FT /note="GPC -> DPCD (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 138 AA; 15535 MW; FF24B8253FEA1A1A CRC64;
MRTLWIMAVL LVGVDGGLWQ FENMIIKVVK KSGILSYSAY GCYCGWGGRG KPKDATDRCC
FVHDCCYGKV TGCNPKLGKY TYSWNNGDIV CEGDGPCKEV CECDRAAAIC FRDNLDTYDR
NKYWRYPASN CQEDSEPC
