PA2N2_VIPAA
ID PA2N2_VIPAA Reviewed; 137 AA.
AC P34180; Q9I967;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Neutral phospholipase A2 ammodytin I2 {ECO:0000303|PubMed:1551386, ECO:0000303|PubMed:16156665};
DE Short=AmI2 {ECO:0000250|UniProtKB:Q910A1};
DE Short=AmdI1;
DE Short=AtnI2 {ECO:0000303|PubMed:16156665};
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Vipera ammodytes ammodytes (Western sand viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX NCBI_TaxID=8705;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-137, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=1551386; DOI=10.1111/j.1432-1033.1992.tb16728.x;
RA Krizaj I., Liang N.-S., Pungercar J., Strukelj B., Ritonja A., Gubensek F.;
RT "Amino acid and cDNA sequences of a neutral phospholipase A2 from the long-
RT nosed viper (Vipera ammodytes ammodytes) venom.";
RL Eur. J. Biochem. 204:1057-1062(1992).
RN [2]
RP SEQUENCE REVISION TO 132.
RA Pungercar J.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kordis D., Gubensek F.;
RT "Molecular evolution of phospholipase A2 multigene family in Vipera
RT ammodytes.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC TISSUE=Venom;
RX PubMed=16156665; DOI=10.1021/bi051024r;
RA Petan T., Krizaj I., Gelb M.H., Pungercar J.;
RT "Ammodytoxins, potent presynaptic neurotoxins, are also highly efficient
RT phospholipase A2 enzymes.";
RL Biochemistry 44:12535-12545(2005).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has enzymatic
CC activity but is non-toxic. Displays low binding affinity and enzymatic
CC activity on phosphatidylserine-containing vesicles and HEK-293 plasma
CC membranes, in contrast to ammodytoxins that have high activity on these
CC phospholipids. PLA2 catalyzes the calcium-dependent hydrolysis of the
CC 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:16156665}.
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:16156665};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16156665};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:16156665};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1551386}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:1551386}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; X56878; CAA40200.2; -; mRNA.
DR EMBL; X84018; CAA58840.1; -; Genomic_DNA.
DR PIR; S22388; S22388.
DR AlphaFoldDB; P34180; -.
DR SMR; P34180; -.
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: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; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:1551386"
FT CHAIN 17..137
FT /note="Neutral phospholipase A2 ammodytin I2"
FT /id="PRO_0000022973"
FT ACT_SITE 63
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 42..131
FT /evidence="ECO:0000250"
FT DISULFID 44..60
FT /evidence="ECO:0000250"
FT DISULFID 59..111
FT /evidence="ECO:0000250"
FT DISULFID 65..137
FT /evidence="ECO:0000250"
FT DISULFID 66..104
FT /evidence="ECO:0000250"
FT DISULFID 73..97
FT /evidence="ECO:0000250"
FT DISULFID 91..102
FT /evidence="ECO:0000250"
SQ SEQUENCE 137 AA; 15309 MW; BDEC100B7F524431 CRC64;
MRTLWIVAVC LIGVEGNLYQ FGNMIFKMTK KSALLSYSNY GCYCGWGGKG KPQDATDRCC
FVHDCCYGRV NGCDPKLSIY SYSFENGDIV CGGDDPCLRA VCECDRVAAI CFGENLNTYD
KKYKNYPSSH CTETEQC
