PA2_HOFGE
ID PA2_HOFGE Reviewed; 239 AA.
AC P0C8L9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Phospholipase A2;
DE Short=HgPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Group III heterodimeric phospholipase A2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Contains:
DE RecName: Full=Phospholipase A2 large subunit;
DE Contains:
DE RecName: Full=Phospholipase A2 small subunit;
DE Flags: Precursor;
OS Hoffmannihadrurus gertschi (Scorpion) (Hadrurus gertschi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Iuroidea; Hadrurus.
OX NCBI_TaxID=380989;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Venom gland;
RX PubMed=17506894; DOI=10.1186/1471-2164-8-119;
RA Schwartz E.F., Diego-Garcia E., Rodriguez de la Vega R.C., Possani L.D.;
RT "Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus
RT gertschi (Arachnida: Scorpiones).";
RL BMC Genomics 8:119-119(2007).
CC -!- FUNCTION: Toxic phospholipase A2, which may catalyze the calcium-
CC dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC Inhibits both skeletal (RYR1) and cardiac (RYR2) ryanodine receptors
CC (calcium release channels). Probably blocks ryanodine receptors by
CC generating a 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 small subunit and a large subunit;
CC disulfid-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}.
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DR EMBL; EL698905; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0C8L9; -.
DR SMR; P0C8L9; -.
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; Hydrolase;
KW Ion channel impairing toxin; Lipid degradation; Lipid metabolism;
KW Metal-binding; Neurotoxin;
KW Ryanodine-sensitive calcium-release channel impairing toxin; Secreted;
KW Signal; Toxin; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..105
FT /evidence="ECO:0000250"
FT /id="PRO_0000358874"
FT CHAIN 107..210
FT /note="Phospholipase A2 large subunit"
FT /id="PRO_0000358875"
FT PROPEP 211..213
FT /evidence="ECO:0000250"
FT /id="PRO_0000358876"
FT CHAIN 214..239
FT /note="Phospholipase A2 small subunit"
FT /id="PRO_0000358877"
FT ACT_SITE 139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 114..136
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 135..174
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 142..167
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 165..202
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 207..217
FT /note="Interchain (between large and small chains)"
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
SQ SEQUENCE 239 AA; 26640 MW; 7ADBB466986CD207 CRC64;
MSLIIVLVIS VLSADAVLSM DNELYLNLEP SQRSSWPVAR AVRMQFSKRS EGGRESRKMQ
GCQILESLND IAREALRTPR HTTKRISKDE MEFFEGRCLS VGESERTVLG TKWCGAGNEA
ANYSDLGYFN NVDRCCREHD HCDNIPAGET KYGLKNEGTY TMMNCKCEKA FDKCLSDISG
YFTRKAVSAV KFTYFTLYGN GCYNVKCENG RSPSNECPNG VAEYTGETGL GAKVINFGK
