ID   PA21B_STRCA             Reviewed;          22 AA.
AC   P86043;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Phospholipase A2 {ECO:0000303|PubMed:17656163};
DE            EC=3.1.1.4;
DE   AltName: Full=Group IB phospholipase A2 {ECO:0000250|UniProtKB:Q9Z0Y2};
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase 1B;
DE   Flags: Fragment;
GN   Name=PLA2G1B {ECO:0000250|UniProtKB:Q9Z0Y2};
OS   Struthio camelus (Common ostrich).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=8801;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Pancreas {ECO:0000269|PubMed:17656163};
RX   PubMed=17656163; DOI=10.1016/j.jchromb.2007.07.012;
RA   Ben Bacha A., Gargouri Y., Bezzine S., Mosbah H., Mejdoub H.;
RT   "Ostrich pancreatic phospholipase A(2): purification and biochemical
RT   characterization.";
RL   J. Chromatogr. B 857:108-114(2007).
CC   -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:17656163}.
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:17656163};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q9Z0Y2, ECO:0000269|PubMed:17656163};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9Z0Y2,
CC       ECO:0000269|PubMed:17656163};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.2. Stable when incubated for 10 minutes between pH 2
CC         and 11. Retains 70% of its activity when incubated for 10 minutes at
CC         pH 1.5. {ECO:0000269|PubMed:17656163};
CC       Temperature dependence:
CC         Stable after incubation at 70 degrees Celsius for 10 minutes. Retains
CC         80% of its activity after incubation at 80 degrees Celsius for 20
CC         minutes. {ECO:0000269|PubMed:17656163};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000255}.
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DR   AlphaFoldDB; P86043; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
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; Metal-binding; Secreted.
FT   CHAIN           1..>22
FT                   /note="Phospholipase A2"
FT                   /id="PRO_0000352758"
FT   NON_TER         22
FT                   /evidence="ECO:0000303|PubMed:17656163"
SQ   SEQUENCE   22 AA;  2625 MW;  5E9F478F89C0E0BB CRC64;
     AVWQFREMIK CTIPPSDDLL DF