PA2_XYLAI
ID PA2_XYLAI Reviewed; 179 AA.
AC I7GQA7;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Phospholipase A(2) {ECO:0000303|PubMed:28546807};
DE EC=3.1.1.4 {ECO:0000255|PROSITE-ProRule:PRU10035};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P00630};
DE Flags: Precursor;
GN Name=PLA2 {ECO:0000312|EMBL:BAM25049.1};
OS Xylocopa appendiculata circumvolans (Japanese carpenter bee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Xylocopa; Alloxylocopa.
OX NCBI_TaxID=135722 {ECO:0000312|EMBL:BAM25049.1};
RN [1] {ECO:0000312|EMBL:BAM25049.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 40-65, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000303|PubMed:28546807}, and
RC Venom gland {ECO:0000303|PubMed:28546807};
RX PubMed=28546807; DOI=10.1186/s40409-017-0119-6;
RA Kawakami H., Goto S.G., Murata K., Matsuda H., Shigeri Y., Imura T.,
RA Inagaki H., Shinada T.;
RT "Isolation of biologically active peptides from the venom of Japanese
RT carpenter bee, Xylocopa appendiculata.";
RL J. Venom. Anim. Toxins Incl. Trop. Dis. 23:29-29(2017).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000305}.
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;
CC Evidence={ECO:0000250|UniProtKB:P00630};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250|UniProtKB:P00630};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC ECO:0000269|PubMed:28546807}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:28546807}.
CC -!- MASS SPECTROMETRY: Mass=16508; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:28546807};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC subfamily. {ECO:0000305}.
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DR EMBL; AB731659; BAM25049.1; -; mRNA.
DR AlphaFoldDB; I7GQA7; -.
DR SMR; I7GQA7; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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: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 SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..39
FT /evidence="ECO:0000305|PubMed:28546807"
FT /id="PRO_0000441214"
FT CHAIN 40..179
FT /note="Phospholipase A(2)"
FT /evidence="ECO:0000305|PubMed:28546807"
FT /id="PRO_0000441215"
FT ACT_SITE 73
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT ACT_SITE 103
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 48..70
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 69..109
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 76..102
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 100..133
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT DISULFID 142..150
FT /evidence="ECO:0000250|UniProtKB:P00630"
SQ SEQUENCE 179 AA; 20385 MW; A10A3C024A299FB2 CRC64;
MHALRSSVLA LWLCLHVSVR AWMTYRSANG LDEYEPEDRI IFVGTKWCGN GNVAEGPEDL
GSLKETDACC REHDMCPDLI EAGQSKHGLT NTASYTRLNC ACDEKFYNCL KNSSETGSGA
VRFTYFTLLG TMCYRNEHPL ICVKKGWFSC SKYELDQSQP KRYQWFDVSS NFAFPRMLT
