ID A0A1X7VAQ6_AMPQE Unreviewed; 798 AA.
AC A0A1X7VAQ6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN Name=105312057 {ECO:0000313|EnsemblMetazoa:Aqu2.1.37106_001};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.37106_001, ECO:0000313|Proteomes:UP000007879};
RN [1] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20686567; DOI=10.1038/nature09201;
RA Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The Amphimedon queenslandica genome and the evolution of animal
RT complexity.";
RL Nature 466:720-726(2010).
RN [2] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT evolution of animal complexity.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.37106_001}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2017) to UniProtKB.
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:0000256|ARBA:ARBA00023422};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000256|ARBA:ARBA00023422};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01161}.
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DR RefSeq; XP_011402697.1; XM_011404395.2.
DR AlphaFoldDB; A0A1X7VAQ6; -.
DR EnsemblMetazoa; Aqu2.1.37106_001; Aqu2.1.37106_001; Aqu2.1.37106.
DR GeneID; 105312057; -.
DR eggNOG; KOG0513; Eukaryota.
DR InParanoid; A0A1X7VAQ6; -.
DR OrthoDB; 518048at2759; -.
DR Proteomes; UP000007879; Unassembled WGS sequence.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR047148; PLPL9.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR24139:SF34; 85/88 KDA CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR24139; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51635; PNPLA; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01161};
KW Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU01161};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW ProRule:PRU01161}; Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 192..219
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 388..420
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 477..656
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT MOTIF 519..523
FT /note="GXSXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT MOTIF 643..645
FT /note="DGA/G"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT ACT_SITE 521
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT ACT_SITE 643
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 798 AA; 88682 MW; 36CE909897DCE054 CRC64;
MSYMVRHSKL NDSTSLDHLC SENSFCHEFY DAIEQAHYPN EALVVRRNSA DSVETSSTSS
TSSNCFVQST LILLPVKDQK SSLWKRTKAA FGYTPPKYQI LFLQEQEDKP TISYTLYGGD
DASEAMIAFD QLNATIAPLM RDGSVLLNEA ILREIVLPKP LQPADISFRL VEVMEADPRA
HPEWHKLLQV LLHNACSRQN KNEIKLLLNK GGNLDQEDND GNTPIHTAAF SSSKEGMDWL
LSIAAPSIPV GHIIERRNSE GLSPIDIAKG SHNNGAIRAL MMKQAVPQAT KLDLFDEVTE
LHEAVDDDNS NQIWQYCSKV GLTSVHVRGR RKAVSMKRAP LLKKQQTVDV PMSSGSTPLI
VAIEKQYIKS TLLLLLGGAD PDQHHPGTGN TPLHFAITEG NLVIVKMLLV FGADPTLCNE
DGITPLQLSK DLDKDGSKVK ITQVLEEMAM LQEKTWNYFI SNHEVPETRK EKETYLLAMD
GGGIRSFNIC QAFLAIEDRM KQLDPHCPSF FSYFDYVAGT SAGAIVALIS TYTDAQTSVS
RALTYKIVTD VFSKPKSERG KLMDKYLQEM LGEDTRMSHP IDQRLIITTT LANVSPSKLH
LMTNYGDERD GQAGPSERKV WEAAKATSAA PYFFPTFQGK FLDGGLMANN PTLDAMVEIQ
DQAEKEGKDV KMGLVLSLGT GYAPSKSVDN IEVFMPGLSF KTISSMKETL SGIQSLLDLF
ITQVTQSDGQ EVQRAKTWCK SLKTPYFRLS PPLTEEIDPL SFDDEAIVNM LYEDKKYLLN
QPQVIDSIAK CLLSKNMD
//