PA2_ANUPH
ID PA2_ANUPH Reviewed; 157 AA.
AC Q6PXP0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Phospholipase A2 phaiodactylipin;
DE Short=PLA2;
DE Contains:
DE RecName: Full=Phaiodactylipin large subunit;
DE EC=3.1.1.4;
DE Contains:
DE RecName: Full=Phaiodactylipin small subunit;
DE Flags: Precursor;
OS Anuroctonus phaiodactylus (Mafia scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Chactoidea; Chactidae; Uroctoninae; Anuroctonus.
OX NCBI_TaxID=246982;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS98377.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-133 AND 140-157,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP TISSUE SPECIFICITY, GLYCOSYLATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland {ECO:0000269|PubMed:15066171};
RX PubMed=15066171; DOI=10.1111/j.1432-1033.2004.04047.x;
RA Valdez-Cruz N.A., Batista C.V.F., Possani L.D.;
RT "Phaiodactylipin, a glycosylated heterodimeric phospholipase A from the
RT venom of the scorpion Anuroctonus phaiodactylus.";
RL Eur. J. Biochem. 271:1453-1464(2004).
CC -!- FUNCTION: Scorpion venom phospholipase A2 (PLA2) that is lethal to
CC crickets and crustaceae. Causes inflammation in mice and lysis of human
CC erythrocytes. Has a mild anticoagulant effect on human platelets. PLA2
CC catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-
CC sn-phosphoglycerides. {ECO:0000269|PubMed:15066171}.
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:15066171};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15066171};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:15066171};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=211 umol/min/mg enzyme with SAPE as substrate
CC {ECO:0000269|PubMed:15066171};
CC Vmax=142 umol/min/mg enzyme with SAPC as substrate
CC {ECO:0000269|PubMed:15066171};
CC Vmax=84 umol/min/mg enzyme with SAPS as substrate
CC {ECO:0000269|PubMed:15066171};
CC Vmax=51 umol/min/mg enzyme with DSPE as substrate
CC {ECO:0000269|PubMed:15066171};
CC Vmax=149 umol/min/mg enzyme with DSPC as substrate
CC {ECO:0000269|PubMed:15066171};
CC Vmax=63 umol/min/mg enzyme with DSPS as substrate
CC {ECO:0000269|PubMed:15066171};
CC Vmax=48 umol/min/mg enzyme with DPPE as substrate
CC {ECO:0000269|PubMed:15066171};
CC Vmax=67 umol/min/mg enzyme with DPPC as substrate
CC {ECO:0000269|PubMed:15066171};
CC Vmax=32 umol/min/mg enzyme with DPPS as substrate
CC {ECO:0000269|PubMed:15066171};
CC pH dependence:
CC Optimum pH is 8.0. Less active at pH 5.0 and pH 10.0.
CC {ECO:0000269|PubMed:15066171};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. Less active at 25 degrees
CC Celsius. {ECO:0000269|PubMed:15066171};
CC -!- SUBUNIT: Heterodimer composed of a small subunit and a large subunit;
CC disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15066171}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:15066171}.
CC -!- MASS SPECTROMETRY: [Phaiodactylipin small subunit]: Mass=3242.5;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:15066171};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks one of the four calcium-binding sites found in other
CC family members. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AY571967; AAS98377.1; -; mRNA.
DR AlphaFoldDB; Q6PXP0; -.
DR SMR; Q6PXP0; -.
DR iPTMnet; Q6PXP0; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:1990142; P:envenomation resulting in hemolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:UniProtKB.
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; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hemolysis; Hemostasis impairing toxin; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin; Zymogen.
FT SIGNAL 1..?
FT /evidence="ECO:0000305"
FT PROPEP ?..25
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:15066171"
FT /id="PRO_0000022984"
FT CHAIN 26..133
FT /note="Phaiodactylipin large subunit"
FT /evidence="ECO:0000269|PubMed:15066171"
FT /id="PRO_0000022985"
FT PROPEP 134..139
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:15066171"
FT /id="PRO_0000022986"
FT CHAIN 140..157
FT /note="Phaiodactylipin small subunit"
FT /evidence="ECO:0000269|PubMed:15066171"
FT /id="PRO_0000022987"
FT ACT_SITE 59
FT /evidence="ECO:0000250|UniProtKB:P00630,
FT ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 88
FT /evidence="ECO:0000250|UniProtKB:P00630,
FT ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000303|PubMed:15066171"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000303|PubMed:15066171"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15066171"
FT DISULFID 35..56
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 55..94
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 62..87
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 85..127
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
FT DISULFID 132..143
FT /note="Interchain (between large and small subunits)"
FT /evidence="ECO:0000250|UniProtKB:Q6T178"
SQ SEQUENCE 157 AA; 18172 MW; 23F13CAC3D9CC4CD CRC64;
MVKRVSKEEM DALERSCSQP FEEERFLIVS GTKWCGNNNI AANYSDLGFL EADKCCRDHD
HCDHIASGET KYGLENKGLF TILNCDCDEA FDHCLKEISN NVTTDIRQKG GAENVWRFYF
QWYNANCYRL YCKDEKSARD EACTNQYAVV KKNFTVQ
