PA2A_NAJAT
ID PA2A_NAJAT Reviewed; 119 AA.
AC A4FS04;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Acidic phospholipase A2 natratoxin;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Naja atra (Chinese cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY,
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND DISULFIDE BONDS.
RC TISSUE=Venom, and Venom gland;
RX PubMed=18247353; DOI=10.1002/prot.21964;
RA Hu P., Sun L., Zhu Z.-Q., Hou X.-W., Wang S., Yu S.-S., Wang H.-L.,
RA Zhang P., Wang M., Niu L.-W., Teng M.-K., Ruan D.-Y.;
RT "Crystal structure of Natratoxin, a novel snake secreted phospholipase A2
RT neurotoxin from Naja atra venom inhibiting A-type K(+) currents.";
RL Proteins 72:673-683(2008).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has an effectively
CC inhibitory effect on A-type K(+) currents (Kv/KCN) in acutely
CC dissociated rat dorsal root ganglion (DRG) neurons. This inhibitory
CC effect is independent of its enzymatic activity. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:18247353}.
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:18247353};
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 -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM34525.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AM492700; CAM34525.2; ALT_INIT; mRNA.
DR PDB; 2OSH; X-ray; 2.20 A; A=1-119.
DR PDBsum; 2OSH; -.
DR AlphaFoldDB; A4FS04; -.
DR SMR; A4FS04; -.
DR PRIDE; A4FS04; -.
DR EvolutionaryTrace; A4FS04; -.
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:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
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 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Ion channel impairing toxin; Lipid degradation;
KW Lipid metabolism; Metal-binding; Neurotoxin;
KW Potassium channel impairing toxin; Secreted; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT CHAIN 1..119
FT /note="Acidic phospholipase A2 natratoxin"
FT /id="PRO_0000352492"
FT ACT_SITE 47
FT /evidence="ECO:0000250"
FT ACT_SITE 93
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..71
FT /evidence="ECO:0000269|PubMed:18247353"
FT DISULFID 26..118
FT /evidence="ECO:0000269|PubMed:18247353"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:18247353"
FT DISULFID 43..99
FT /evidence="ECO:0000269|PubMed:18247353"
FT DISULFID 50..92
FT /evidence="ECO:0000269|PubMed:18247353"
FT DISULFID 60..85
FT /evidence="ECO:0000269|PubMed:18247353"
FT DISULFID 78..90
FT /evidence="ECO:0000269|PubMed:18247353"
FT CONFLICT 19
FT /note="W -> C (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 2..12
FT /evidence="ECO:0007829|PDB:2OSH"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:2OSH"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2OSH"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:2OSH"
FT HELIX 39..54
FT /evidence="ECO:0007829|PDB:2OSH"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2OSH"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2OSH"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2OSH"
FT HELIX 84..102
FT /evidence="ECO:0007829|PDB:2OSH"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2OSH"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2OSH"
SQ SEQUENCE 119 AA; 13188 MW; 9947ADA9D5BAE0CE CRC64;
NLYQFKNMIQ CTVPSRSWWD FADYGCYCGK GGSGTPVDDL DRCCQVHDNC YNEAEKISGC
WPYFKTYSYE CSQGTLTCKG GNNACAAAVC DCDRLAAICF AGAPYTDANY NIDLKARCQ
