ID   PA2_CHEFU               Reviewed;         103 AA.
AC   Q3YAU5;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Phospholipase A2 large subunit;
DE            Short=HfPLA2;
DE            EC=3.1.1.4;
DE   Flags: Fragment;
OS   Chersonesometrus fulvipes (Indian black scorpion) (Heterometrus fulvipes).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Heterometrinae;
OC   Chersonesometrus.
OX   NCBI_TaxID=141248;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND 3D-STRUCTURE MODELING.
RC   TISSUE=Venom gland;
RX   PubMed=17454010; DOI=10.1080/10425170701243294;
RA   Hariprasad G., Singh B., Das U., Ethayathulla A.S., Kaur P., Singh T.P.,
RA   Srinivasan A.;
RT   "Cloning, sequence analysis and homology modeling of a novel phospholipase
RT   A2 from Heterometrus fulvipes (Indian black scorpion).";
RL   DNA Seq. 18:242-246(2007).
CC   -!- FUNCTION: Phospholipase toxin, which catalyzes the calcium-dependent
CC       hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits
CC       both skeletal (RYR1) and cardiac (RYR2) ryanodine receptors (calcium
CC       release channels). Probably blocks ryanodine receptors by generating a
CC       lipid product (By similarity). {ECO:0000250}.
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};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer composed of a large subunit and a small subunit;
CC       disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other phospholipases, it lacks the typical Asp
CC       active site (Asp->Glu in position 62). {ECO:0000305}.
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DR   EMBL; DQ146998; AAZ78243.1; -; mRNA.
DR   AlphaFoldDB; Q3YAU5; -.
DR   SMR; Q3YAU5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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; IPR016090; PLipase_A2_dom.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   InterPro; IPR033113; PLipase_A2_His_AS.
DR   Pfam; PF05826; Phospholip_A2_2; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
DR   PROSITE; PS00118; PA2_HIS; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel impairing toxin; Disulfide bond; Glycoprotein;
KW   Hydrolase; Ion channel impairing toxin; Lipid degradation;
KW   Lipid metabolism; Metal-binding; Neurotoxin;
KW   Ryanodine-sensitive calcium-release channel impairing toxin; Secreted;
KW   Toxin; Zymogen.
FT   CHAIN           1..>103
FT                   /note="Phospholipase A2 large subunit"
FT                   /id="PRO_0000429186"
FT   ACT_SITE        33
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   BINDING         7
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00630"
FT   BINDING         9
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00630"
FT   BINDING         11
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00630"
FT   BINDING         34
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00630"
FT   CARBOHYD        16
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        8..30
FT                   /evidence="ECO:0000250|UniProtKB:Q6T178"
FT   DISULFID        29..68
FT                   /evidence="ECO:0000250|UniProtKB:Q6T178"
FT   DISULFID        36..61
FT                   /evidence="ECO:0000250|UniProtKB:Q6T178"
FT   DISULFID        59..96
FT                   /evidence="ECO:0000250|UniProtKB:Q6T178"
FT   DISULFID        101..?
FT                   /note="Interchain (between large and small subunits)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6T178"
FT   NON_TER         103
SQ   SEQUENCE   103 AA;  11487 MW;  471F6317F84A9BB3 CRC64;
     TMWGTKWCGS GNKAINYTDL GYFSNLDSCC RTHDHCDNIA AGETKYGLTN EGKYTMMNCK
     CEATFQQCLR DVHGPLEGKA AFTIRKLYFG LYGNGCFNVQ CPS