ID   PA22_SCODE              Reviewed;          28 AA.
AC   P0DPT8;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Phospholipase A2;
DE            Short=PLA2;
DE            EC=3.1.1.4 {ECO:0000255|PROSITE-ProRule:PRU10035};
DE   Flags: Fragment;
OS   Scolopendra dehaani (Thai centipede) (Scolopendra subspinipes dehaani).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Scolopendromorpha; Scolopendridae; Scolopendra.
OX   NCBI_TaxID=2609776;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, FUNCTION,
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Venom;
RX   PubMed=23148443; DOI=10.1021/pr300881d;
RA   Liu Z.C., Zhang R., Zhao F., Chen Z.M., Liu H.W., Wang Y.J., Jiang P.,
RA   Zhang Y., Wu Y., Ding J.P., Lee W.H., Zhang Y.;
RT   "Venomic and transcriptomic analysis of centipede Scolopendra subspinipes
RT   dehaani.";
RL   J. Proteome Res. 11:6197-6212(2012).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:23148443}.
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:0000269|PubMed:23148443};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P14555};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=840 uM/min/mg enzyme for egg yolk {ECO:0000269|PubMed:23148443};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23148443}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:23148443}.
CC   -!- MASS SPECTROMETRY: Mass=13081.2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23148443};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DPT8; -.
DR   SMR; P0DPT8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Secreted.
FT   CHAIN           1..>28
FT                   /note="Phospholipase A2"
FT                   /id="PRO_0000446682"
FT   BINDING         28
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        27..?
FT                   /evidence="ECO:0000305"
FT   NON_TER         28
SQ   SEQUENCE   28 AA;  3100 MW;  C0CA19B381F0D305 CRC64;
     SLANFLSMTL TAAKRKPKEY DGYGNYCG