ID   PA2_TRILM               Reviewed;          50 AA.
AC   P84736;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Phospholipase A2 trimorphin;
DE            Short=svPLA2;
DE            EC=3.1.1.4 {ECO:0000269|PubMed:15225559};
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Fragment;
OS   Trimorphodon lambda (Sonoran lyre snake) (Trimorphodon biscutatus lambda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Trimorphodon.
OX   NCBI_TaxID=356346;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000269|PubMed:15225559};
RX   PubMed=15225559; DOI=10.1016/j.toxicon.2004.03.027;
RA   Huang P., Mackessy S.P.;
RT   "Biochemical characterization of phospholipase A2 (trimorphin) from the
RT   venom of the sonoran lyre snake Trimorphodon biscutatus lambda (family
RT   Colubridae).";
RL   Toxicon 44:27-36(2004).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:15225559}.
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:15225559};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:15225559};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:15225559};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:15225559}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5. No activity below pH 5.5 or above pH 10.5.
CC         {ECO:0000269|PubMed:15225559};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15225559}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:15225559}.
CC   -!- MASS SPECTROMETRY: Mass=13996.7; Mass_error=10; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15225559};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P84736; -.
DR   SMR; P84736; -.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
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   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   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.
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..>50
FT                   /note="Phospholipase A2 trimorphin"
FT                   /id="PRO_0000161698"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000250|UniProtKB:P00592,
FT                   ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
FT                   ProRule:PRU10036"
FT   BINDING         28
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00592"
FT   DISULFID        11..?
FT                   /evidence="ECO:0000250|UniProtKB:P00592"
FT   DISULFID        27..?
FT                   /evidence="ECO:0000250|UniProtKB:P00592"
FT   DISULFID        29..45
FT                   /evidence="ECO:0000250|UniProtKB:P00592"
FT   DISULFID        44..?
FT                   /evidence="ECO:0000250|UniProtKB:P00592"
FT   NON_TER         50
FT                   /evidence="ECO:0000303|PubMed:15225559"
SQ   SEQUENCE   50 AA;  5471 MW;  80B1214DE8985F7B CRC64;
     NLYQFSNMIQ CTIPGSDPLS DYGNYGCYCG YGGSGTPVDE LLRCCQVHDD