PA2_PITAZ
ID PA2_PITAZ Reviewed; 146 AA.
AC C0HLL2;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2019, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Phospholipase A2 {ECO:0000303|PubMed:31173792};
DE EC=3.1.1.4 {ECO:0000269|PubMed:31173792};
DE AltName: Full=Pa-PLA2 {ECO:0000303|PubMed:31173792};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000305};
DE Flags: Precursor;
OS Pithecopus azureus (Orange-legged monkey tree frog) (Phyllomedusa azurea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Pithecopus.
OX NCBI_TaxID=2034991;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-105 AND 113-133,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP GLYCOSYLATION AT ASN-85 AND ASN-126.
RC TISSUE=Skin secretion {ECO:0000303|PubMed:31173792};
RX PubMed=31173792; DOI=10.1016/j.toxicon.2019.06.002;
RA Souza B.B.P., Cardozo Fh J.L., Murad A.M., Prates M.V., Coura M.M.A.,
RA Brand G.D., Barbosa E.A., Bloch C. Jr.;
RT "Identification and characterization of phospholipases A2 from the skin
RT secretion of Pithecopus azureus anuran.";
RL Toxicon 167:10-19(2019).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:31173792}.
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:0000269|PubMed:31173792};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:31173792};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31173792}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands (at protein level).
CC {ECO:0000269|PubMed:31173792}.
CC -!- PTM: N-glycosylated. Glycosylated with mannose chains including
CC Man2(GlcNAc), Man2(GlcNAc)2, Man2(GlcNAc)3, Man2(GlcNAc)4 and
CC Man2(GlcNAc)5. {ECO:0000269|PubMed:31173792}.
CC -!- MASS SPECTROMETRY: Mass=15775.930; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:31173792};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR AlphaFoldDB; C0HLL2; -.
DR SMR; C0HLL2; -.
DR iPTMnet; C0HLL2; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IDA:UniProtKB.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 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..18
FT /evidence="ECO:0000269|PubMed:31173792"
FT CHAIN 19..146
FT /note="Phospholipase A2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000448064"
FT ACT_SITE 65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:31173792"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:31173792"
FT DISULFID 44..137
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 46..62
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 61..117
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 67..144
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 68..110
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 77..103
FT /evidence="ECO:0000250|UniProtKB:O42187"
FT DISULFID 95..108
FT /evidence="ECO:0000250|UniProtKB:O42187"
SQ SEQUENCE 146 AA; 16346 MW; 8D5B43ADA5559DA7 CRC64;
MAFLVFAFLT LMAVETYGSL FQFRLMINYL TGKLPILSHS FYGCYCGAGG SGWPKDAIDW
CCQVHDCCYG RMSASGCDPY FQPYNFSYIN KNLQCVETDT SGCPRRICEC DRLASICFQQ
HDATYNSSNI DPKRKGCGTK SPPCPN
