PA2V_MEIAT
ID PA2V_MEIAT Reviewed; 152 AA.
AC P0DP54;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Phospholipase A2 {ECO:0000303|PubMed:28366739};
DE Short=PLA2 {ECO:0000303|PubMed:28366739};
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 10 {ECO:0000250|UniProtKB:O15496};
DE Flags: Precursor;
OS Meiacanthus atrodorsalis (Forktail blenny) (Petroscirtes atrodorsalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Blenniimorphae; Blenniiformes; Blennioidei; Blenniidae;
OC Blenniinae; Meiacanthus.
OX NCBI_TaxID=1405650;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Venom gland;
RX PubMed=28366739; DOI=10.1016/j.cub.2017.02.067;
RA Casewell N.R., Visser J.C., Baumann K., Dobson J., Han H., Kuruppu S.,
RA Morgan M., Romilio A., Weisbecker V., Ali S.A., Debono J., Koludarov I.,
RA Que I., Bird G.C., Cooke G.M., Nouwens A., Hodgson W.C., Wagstaff S.C.,
RA Cheney K.L., Vetter I., van der Weerd L., Richardson M.K., Fry B.G.;
RT "The evolution of fangs, venom, and mimicry systems in blenny fishes.";
RL Curr. Biol. 27:1184-1191(2017).
CC -!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000250|UniProtKB:O15496}.
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, ECO:0000255|PROSITE-
CC ProRule:PRU10036};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28366739}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. Heavily expressed in
CC the venom gland transcriptome. {ECO:0000269|PubMed:28366739}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR AlphaFoldDB; P0DP54; -.
DR SMR; P0DP54; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW Metal-binding; Secreted; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..152
FT /note="Phospholipase A2"
FT /id="PRO_0000440254"
FT ACT_SITE 73
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT ACT_SITE 118
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT DISULFID 39..96
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT DISULFID 53..142
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT DISULFID 55..70
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT DISULFID 69..124
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT DISULFID 75..149
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT DISULFID 76..117
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT DISULFID 85..110
FT /evidence="ECO:0000250|UniProtKB:O15496"
FT DISULFID 103..115
FT /evidence="ECO:0000250|UniProtKB:O15496"
SQ SEQUENCE 152 AA; 17012 MW; E8A70F4462731E52 CRC64;
MAACHRILLL LSVAVASGAA QKPPLTKRGL LEFGGIITCS TGRSPLSYVM YGCYCGLGGK
GWPRDKADCC HEHDCCYGEA ETLGCQTKTD QYRWKCEDKK VECDDLNDKC EKFLCKCDRD
AAKCLEKAPY NQKYLFWPSF MCGSEEPKCS IY
