PA2_URTCR
ID PA2_URTCR Reviewed; 155 AA.
AC A7LCJ2;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Phospholipase A2 A2-actitoxin-Ucs2a {ECO:0000303|PubMed:22683676};
DE Short=A2-AITX-Ucs2a {ECO:0000303|PubMed:22683676};
DE EC=3.1.1.4 {ECO:0000269|PubMed:20553498};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=UcPLA2 {ECO:0000303|PubMed:20553498};
DE Flags: Precursor;
OS Urticina crassicornis (Mottled anemone) (Tealia crassicornis).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Urticina.
OX NCBI_TaxID=45621;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-69, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, AND 3D-STRUCTURE MODELING.
RC TISSUE=Tentacle;
RX PubMed=20553498; DOI=10.1111/j.1742-4658.2010.07674.x;
RA Razpotnik A., Krizaj I., Sribar J., Kordis D., Macek P., Frangez R.,
RA Kem W.R., Turk T.;
RT "A new phospholipase A2 isolated from the sea anemone Urticina crassicornis
RT - its primary structure and phylogenetic classification.";
RL FEBS J. 277:2641-2653(2010).
RN [2]
RP NOMENCLATURE.
RX PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA Oliveira J.S., Fuentes-Silva D., King G.F.;
RT "Development of a rational nomenclature for naming peptide and protein
RT toxins from sea anemones.";
RL Toxicon 60:539-550(2012).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:20553498}.
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, ECO:0000269|PubMed:20553498};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:20553498};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:20553498};
CC -!- SUBCELLULAR LOCATION: Secreted. Nematocyst.
CC -!- MISCELLANEOUS: Lacks hemolytic activity on bovine red blood cells as
CC well as neurotoxic activities. {ECO:0000269|PubMed:20553498}.
CC -!- MISCELLANEOUS: mRNA is obtained from a single animal, whereas the
CC protein is isolated from exudates of several specimens.
CC {ECO:0000269|PubMed:20553498}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- CAUTION: Possesses an Asp at position 69 instead of a conseved Cys.
CC {ECO:0000305}.
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DR EMBL; EU003992; ABS19666.1; -; mRNA.
DR AlphaFoldDB; A7LCJ2; -.
DR SMR; A7LCJ2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; 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 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; Nematocyst; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..42
FT /id="PRO_0000413798"
FT CHAIN 45..155
FT /note="Phospholipase A2 A2-actitoxin-Ucs2a"
FT /id="PRO_0000413799"
FT ACT_SITE 90
FT /evidence="ECO:0000250"
FT ACT_SITE 137
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 55..118
FT /evidence="ECO:0000250"
FT DISULFID 71..87
FT /evidence="ECO:0000250"
FT DISULFID 86..143
FT /evidence="ECO:0000250"
FT DISULFID 93..136
FT /evidence="ECO:0000250"
FT DISULFID 100..129
FT /evidence="ECO:0000250"
FT DISULFID 122..134
FT /evidence="ECO:0000250"
FT CONFLICT 45..46
FT /note="DI -> NL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="G -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="R -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="F -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 17319 MW; D4C567640BA93626 CRC64;
MKNNIILVIL LGISVFVDCL PLNDQEEDKS LNAQESEVSA VQKRDILQFS GMIRCATGRS
AWKYFNYGNW CGWGGSGTAV DGVDSCCRSH DWCYKRHDSC YPKIIPYIAS TSGSHPSCSI
TCHSANNRCQ RDVCNCDKVA AECFARNTYH PNNKH
