ID   PA2_NOTSC               Reviewed;          20 AA.
AC   Q7LZG5;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Phospholipase A2 II-5b;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Notechis II-5b non-toxic venom protein;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Notechis.
OX   NCBI_TaxID=70142;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=1814009; DOI=10.1016/0041-0101(91)90120-g;
RA   Yang C.C., Chang L.S., Wu F.S.;
RT   "Venom constituents of Notechis scutatus scutatus (Australian tiger snake)
RT   from differing geographic regions.";
RL   Toxicon 29:1337-1344(1991).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that exhibits weak
CC       enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of
CC       the 2-acyl groups in 3-sn-phosphoglycerides.
CC       {ECO:0000269|PubMed:1814009}.
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:0000269|PubMed:1814009}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:1814009}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       {ECO:0000305}.
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DR   PIR; A39328; A39328.
DR   AlphaFoldDB; Q7LZG5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Secreted.
FT   CHAIN           <1..>20
FT                   /note="Phospholipase A2 II-5b"
FT                   /id="PRO_0000408026"
FT   NON_TER         1
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2188 MW;  3419336D2B7DD7E1 CRC64;
     NLIQLSNMIK CAIPGSQPLF