ID   PA2CS_RHIDP             Reviewed;          39 AA.
AC   C0HLL0;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Phospholipase A2 CS24a {ECO:0000303|PubMed:30519258};
DE            Short=PLA2 {ECO:0000305};
DE            Short=RsPLA2 {ECO:0000303|PubMed:30519258};
DE   Contains:
DE     RecName: Full=Phospholipase A2 CS25-CS26 {ECO:0000303|PubMed:30519258};
DE   Flags: Fragment;
OS   Rhinella diptycha (Cururu toad) (Rhinella schneideri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Rhinella.
OX   NCBI_TaxID=2736592;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=30519258; DOI=10.1186/s40409-018-0173-8;
RA   Shibao P.Y.T., Cologna C.T., Morandi-Filho R., Wiezel G.A., Fujimura P.T.,
RA   Ueira-Vieira C., Arantes E.C.;
RT   "Deep sequencing analysis of toad Rhinella schneideri skin glands and
RT   partial biochemical characterization of its cutaneous secretion.";
RL   J. Venom. Anim. Toxins Incl. Trop. Dis. 24:36-36(2018).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {ECO:0000250|UniProtKB:P62022}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30519258}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:30519258}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HLL0; -.
DR   SMR; C0HLL0; -.
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:InterPro.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR001211; PLipase_A2.
DR   InterPro; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   Pfam; PF00068; Phospholip_A2_1; 1.
DR   PRINTS; PR00389; PHPHLIPASEA2.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Metal-binding; Secreted.
FT   CHAIN           1..>39
FT                   /note="Phospholipase A2 CS24a"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000447719"
FT   CHAIN           3..>39
FT                   /note="Phospholipase A2 CS25-CS26"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000447720"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   BINDING         31
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P62022"
FT   NON_TER         39
FT                   /evidence="ECO:0000303|PubMed:30519258"
SQ   SEQUENCE   39 AA;  4605 MW;  3FDC5ED6581887B4 CRC64;
     GLLEFNKMIK FETRKNAIPF YAFYGCYCGW GGRRRPKDA