PA2_PANIM
ID PA2_PANIM Reviewed; 145 AA.
AC P0DKU2;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Phospholipase A2 phospholipin;
DE EC=3.1.1.4;
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 Pandinus imperator (Emperor scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Pandininae; Pandinus.
OX NCBI_TaxID=55084;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-86; 88-123 AND 129-145,
RP CATALYTIC ACTIVITY, SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10556514; DOI=10.1016/s0014-5793(99)01392-7;
RA Conde R., Zamudio F.Z., Becerril B., Possani L.D.;
RT "Phospholipin, a novel heterodimeric phospholipase A2 from Pandinus
RT imperator scp6pion venom.";
RL FEBS Lett. 460:447-450(1999).
CC -!- FUNCTION: Scorpion venom phospholipase A2 (PLA2) that contains
CC enzymatic activity, but does not inhibit ryanodine receptors in
CC contrary to imperatoxin-1, another heterodimer of P.imperator venom.
CC PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in
CC 3-sn-phosphoglycerides.
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 ECO:0000269|PubMed:10556514};
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:0000269|PubMed:10556514}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=14841.2; Method=MALDI; Note=The measured ranges
CC are 16-123, 129-145.; Evidence={ECO:0000269|PubMed:10556514};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: The sequence signal is uncertain for 2 reasons. Firstly, it
CC contains 2 consecutive basic residues (Arg) that may indicate that this
CC segment corresponds to the message for translating an unknown third
CC peptide or long propeptide. Secondly, it is not predicted by the
CC predictive tools. {ECO:0000305}.
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DR AlphaFoldDB; P0DKU2; -.
DR SMR; P0DKU2; -.
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: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 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Secreted; Signal; Toxin; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:10556514"
FT CHAIN 16..123
FT /note="Phospholipase A2 large subunit"
FT /id="PRO_0000420883"
FT PROPEP 124..128
FT /evidence="ECO:0000269|PubMed:10556514"
FT /id="PRO_0000420884"
FT PEPTIDE 129..145
FT /note="Phospholipase A2 small subunit"
FT /id="PRO_0000420885"
FT ACT_SITE 49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 25..46
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 45..84
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 52..77
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 75..116
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 121..132
FT /note="Interchain (between large and small chains)"
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
SQ SEQUENCE 145 AA; 16441 MW; 7B58F0869CE6788A CRC64;
MVDLARRCSG STEGRFLMWE CTKWCGPGNN AKCESDLGPL EADKCCRTHD HCDYIASGET
KYGITNYAFF TKLNCKCEEA FDRCLTEAYN KEEKESAKSS TKRLQNFYFG TYSPECYVVT
CNSKRSGRDA GCENGVATWK KSYKD
