PA2A1_NAJMO
ID PA2A1_NAJMO Reviewed; 118 AA.
AC P00602;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Acidic phospholipase A2 CM-I;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Naja mossambica (Mozambique spitting cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8644;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=880314; DOI=10.1016/0005-2795(77)90275-6;
RA Joubert F.J.;
RT "Naja mossambica mossambica venom. Purification, some properties and the
RT amino acid sequences of three phospholipases A (CM-I, CM-II and CM-III).";
RL Biochim. Biophys. Acta 493:216-227(1977).
RN [2]
RP FUNCTION.
RX PubMed=3615669;
RA Lin W.W., Chang P.L., Lee C.Y., Joubert F.J.;
RT "Pharmacological study on phospholipases A2 isolated from Naja mossambica
RT mossambica venom.";
RL Proc. Natl. Sci. Counc. Repub. China, B, Life Sci. 11:155-163(1987).
RN [3]
RP FUNCTION.
RX PubMed=3117784; DOI=10.1016/s0021-9258(18)47808-8;
RA Kini R.M., Evans H.J.;
RT "Structure-function relationships of phospholipases. The anticoagulant
RT region of phospholipases A2.";
RL J. Biol. Chem. 262:14402-14407(1987).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that causes myonecrosis
CC when injected intramuscularly, shows indirect hemolytic activity,
CC abolishes twitches evoked by indirect stimulation earlier than those by
CC direct stimulation (in the mouse phrenic nerve-diaphragm preparation)
CC but does not produce complete neuromuscular block (up to 30 ug/ml) (in
CC the chick biventer cervicis nerve-muscle preparation) (PubMed:3615669).
CC PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides. {ECO:0000269|PubMed:3117784,
CC ECO:0000269|PubMed:3615669}.
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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not have anticoagulant activity.
CC {ECO:0000305|PubMed:3117784}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR PIR; A00743; PSNJ1M.
DR AlphaFoldDB; P00602; -.
DR SMR; P00602; -.
DR BindingDB; P00602; -.
DR ChEMBL; CHEMBL3968; -.
DR PRIDE; P00602; -.
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; Neurotoxin;
KW Secreted; Toxin.
FT CHAIN 1..118
FT /note="Acidic phospholipase A2 CM-I"
FT /id="PRO_0000161666"
FT ACT_SITE 47
FT /evidence="ECO:0000250"
FT ACT_SITE 92
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 11..70
FT /evidence="ECO:0000250"
FT DISULFID 26..117
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
FT DISULFID 43..98
FT /evidence="ECO:0000250"
FT DISULFID 50..91
FT /evidence="ECO:0000250"
FT DISULFID 59..84
FT /evidence="ECO:0000250"
FT DISULFID 77..89
FT /evidence="ECO:0000250"
SQ SEQUENCE 118 AA; 13219 MW; A0C2DEC5EAC7C751 CRC64;
NLYQFKNMIH CTVPSRPWWH FADYGCYCGR GGKGTAVDDL DRCCQVHDNC YGEAEKLGCW
PYLTLYKYEC SQGKLTCSGG NNKCEAAVCN CDLVAANCFA GAPYIDANYN VNLKERCQ
