PA2NA_NAJSP
ID PA2NA_NAJSP Reviewed; 146 AA.
AC Q92084; Q10756;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Neutral phospholipase A2 muscarinic inhibitor;
DE Short=NPLA;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=NAJPLA-2A;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A2 A;
DE Flags: Precursor;
OS Naja sputatrix (Malayan spitting cobra) (Naja naja sputatrix).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=33626;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-48.
RC TISSUE=Venom, and Venom gland;
RX PubMed=9028006; DOI=10.1016/s0041-0101(96)00071-2;
RA Armugam A., Earnest L., Chung M.C.M., Gopalakrishnakone P., Tan C.H.,
RA Tan N.-H., Jeyaseelan K.;
RT "Cloning and characterization of cDNAs encoding three isoforms of
RT phospholipase A2 in Malayan spitting cobra (Naja naja sputatrix) venom.";
RL Toxicon 35:27-37(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=10889214; DOI=10.1093/oxfordjournals.molbev.a026382;
RA Jeyaseelan K., Armugam A., Donghui M., Tan N.-H.;
RT "Structure and phylogeny of the venom group I phospholipase A(2) gene.";
RL Mol. Biol. Evol. 17:1010-1021(2000).
RN [3]
RP PROTEIN SEQUENCE OF 28-43, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=8638927; DOI=10.1006/abbi.1996.0137;
RA Miyoshi S., Tu A.T.;
RT "Phospholipase A2 from Naja naja sputatrix venom is a muscarinic
RT acetylcholine receptor inhibitor.";
RL Arch. Biochem. Biophys. 328:17-25(1996).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits the
CC muscarinic acetylcholine receptors (mAChR/CHRM) with no subtype
CC selectivity. Shows catalytic activity. PLA2 catalyzes the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC {ECO:0000269|PubMed:8638927}.
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, ECO:0000269|PubMed:8638927};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8638927}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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}.
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DR EMBL; L42004; AAA66027.1; -; mRNA.
DR EMBL; AF101236; AAF82187.1; -; Genomic_DNA.
DR PIR; S65520; S65520.
DR AlphaFoldDB; Q92084; -.
DR SMR; Q92084; -.
DR PRIDE; Q92084; -.
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;
KW G-protein coupled acetylcholine receptor impairing toxin;
KW G-protein coupled receptor impairing toxin; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..27
FT /evidence="ECO:0000269|PubMed:8638927,
FT ECO:0000269|PubMed:9028006"
FT /id="PRO_0000022930"
FT CHAIN 28..146
FT /note="Neutral phospholipase A2 muscarinic inhibitor"
FT /id="PRO_0000022931"
FT ACT_SITE 74
FT /evidence="ECO:0000250"
FT ACT_SITE 120
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 38..98
FT /evidence="ECO:0000250"
FT DISULFID 53..145
FT /evidence="ECO:0000250"
FT DISULFID 55..71
FT /evidence="ECO:0000250"
FT DISULFID 70..126
FT /evidence="ECO:0000250"
FT DISULFID 77..119
FT /evidence="ECO:0000250"
FT DISULFID 87..112
FT /evidence="ECO:0000250"
FT DISULFID 105..117
FT /evidence="ECO:0000250"
SQ SEQUENCE 146 AA; 16189 MW; B36CF0BFD7AE295A CRC64;
MNPAHLLILA AVCVSPLGAS SNRPMPLNLY QFKNMIQCTV PNRSWWHFAD YGCYCGRGGS
GTPVDDLDRC CQIHDNCYNE AEKISRCWPY FKTYSYECSQ GTLTCKGGNN ACAAAVCDCD
RLAAICFAGA PYNDNNYNID LKARCQ
