PA2A2_TROCA
ID PA2A2_TROCA Reviewed; 151 AA.
AC Q45Z29;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Acidic phospholipase A2 2;
DE Short=svPLA2;
DE EC=3.1.1.4;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2;
DE Short=PLA-2;
DE Flags: Precursor;
OS Tropidechis carinatus (Australian rough-scaled snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Notechinae; Tropidechis.
OX NCBI_TaxID=100989;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16261251; DOI=10.1007/s00018-005-5384-9;
RA St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.;
RT "Identification and analysis of venom gland-specific genes from the coastal
RT taipan (Oxyuranus scutellatus) and related species.";
RL Cell. Mol. Life Sci. 62:2679-2693(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 52-139, AND DISULFIDE BONDS.
RX PubMed=15720395; DOI=10.1111/j.1742-4658.2005.04547.x;
RA Lok S.M., Gao R., Rouault M., Lambeau G., Gopalakrishnakone P.,
RA Swaminathan K.;
RT "Structure and function comparison of Micropechis ikaheka snake venom
RT phospholipase A2 isoenzymes.";
RL FEBS J. 272:1211-1220(2005).
CC -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC groups in 3-sn-phosphoglycerides.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ085837; AAZ22655.1; -; mRNA.
DR PDB; 1P7O; X-ray; 2.30 A; A/B/C/D/E/F=52-141.
DR PDBsum; 1P7O; -.
DR AlphaFoldDB; Q45Z29; -.
DR SMR; Q45Z29; -.
DR PRIDE; Q45Z29; -.
DR EvolutionaryTrace; Q45Z29; -.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Disulfide bond; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Secreted; Signal; Toxin.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..151
FT /note="Acidic phospholipase A2 2"
FT /id="PRO_0000043277"
FT ACT_SITE 75
FT /evidence="ECO:0000250"
FT ACT_SITE 126
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 38..104
FT /evidence="ECO:0000269|PubMed:15720395"
FT DISULFID 54..151
FT /evidence="ECO:0000269|PubMed:15720395"
FT DISULFID 56..72
FT /evidence="ECO:0000269|PubMed:15720395"
FT DISULFID 71..132
FT /evidence="ECO:0000269|PubMed:15720395"
FT DISULFID 78..125
FT /evidence="ECO:0000269|PubMed:15720395"
FT DISULFID 88..118
FT /evidence="ECO:0000269|PubMed:15720395"
FT DISULFID 111..123
FT /evidence="ECO:0000269|PubMed:15720395"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1P7O"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1P7O"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1P7O"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1P7O"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1P7O"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:1P7O"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1P7O"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1P7O"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1P7O"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:1P7O"
SQ SEQUENCE 151 AA; 16891 MW; 678C0EF2DEB9934A CRC64;
MYPAHLLVLL AVCVSLLGAA SIPARPLNLY QFGNMIQCAN HGRRPTRHYM DYGCYCGKGG
SGTPVDELDR CCQTHDDCYG EAEKLPACNY MMSGPYYNTY SYECNDGELT CKDNNDECKA
FICNCDRTAA ICFARAPYND ANWNIDTKTR C
