PA2B_MICCO
ID PA2B_MICCO Reviewed; 146 AA.
AC Q8AXW7;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Basic phospholipase A2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Micrurus corallinus (Brazilian coral snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=54390;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Ho P.L., Soares M.B., Yamane T., Raw I.A.;
RT "Reverse biology applied to Micrurus corallinus, a South American coral
RT snake.";
RL J. Toxicol. Toxin Rev. 14:327-337(1995).
RN [2]
RP PROTEIN SEQUENCE OF 28-42, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=21515432; DOI=10.1016/j.jprot.2011.04.003;
RA Correa-Netto C., Junqueira-de-Azevedo Ide L., Silva D.A., Ho P.L.,
RA Leitao-de-Araujo M., Alves M.L., Sanz L., Foguel D., Zingali R.B.,
RA Calvete J.J.;
RT "Snake venomics and venom gland transcriptomic analysis of Brazilian coral
RT snakes, Micrurus altirostris and M. corallinus.";
RL J. Proteomics 74:1795-1809(2011).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000250}.
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 {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY157830; AAN60018.1; -; mRNA.
DR AlphaFoldDB; Q8AXW7; -.
DR SMR; Q8AXW7; -.
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; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT PROPEP 22..27
FT /evidence="ECO:0000269|PubMed:21515432"
FT /id="PRO_0000422879"
FT CHAIN 28..146
FT /note="Basic phospholipase A2"
FT /id="PRO_0000419210"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT ACT_SITE 121
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..97
FT /evidence="ECO:0000250"
FT DISULFID 52..145
FT /evidence="ECO:0000250"
FT DISULFID 54..70
FT /evidence="ECO:0000250"
FT DISULFID 69..127
FT /evidence="ECO:0000250"
FT DISULFID 76..120
FT /evidence="ECO:0000250"
FT DISULFID 86..113
FT /evidence="ECO:0000250"
FT DISULFID 106..118
FT /evidence="ECO:0000250"
SQ SEQUENCE 146 AA; 15959 MW; 8C4E00F852B2145D CRC64;
MNPAHLLVLA AVCVSLLGAS SVPPRPLNLI NFQRMIQCTT RRSAWDFTNY GCYCGAGGSG
TPVDELDRCC KVHDDCYGAA EKYHRCSPKL TLYTSTCSSQ TGSVTCKDNG TKCKAFVCNC
DRTAALCFGR APYNKNNENI NPNRCR
