ID   A0A3B3TM73_9TELE        Unreviewed;       795 AA.
AC   A0A3B3TM73;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000002330.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000002330.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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};
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DR   RefSeq; XP_014873234.1; XM_015017748.1.
DR   RefSeq; XP_014873243.1; XM_015017757.1.
DR   RefSeq; XP_014873251.1; XM_015017765.1.
DR   AlphaFoldDB; A0A3B3TM73; -.
DR   STRING; 48699.ENSPLAP00000002330; -.
DR   Ensembl; ENSPLAT00000013229.1; ENSPLAP00000002330.1; ENSPLAG00000000727.1.
DR   GeneID; 106936627; -.
DR   KEGG; plai:106936627; -.
DR   CTD; 8398; -.
DR   GeneTree; ENSGT00940000158756; -.
DR   OrthoDB; 518048at2759; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07212; Pat_PNPLA9; 1.
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; 3.
DR   Pfam; PF01734; Patatin; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS51635; PNPLA; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          150..183
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          218..250
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          315..347
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          348..380
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          472..656
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
SQ   SEQUENCE   795 AA;  88100 MW;  4407A2F15970B548 CRC64;
     MQFLGRLLDT VSSVSTLFTN PYRVRDVQLS DYGGGGKVRL KEDGRMVLYK NTQCQSWDCV
     LLSPETPTVA LRLFQVGSEE DAMNWFPQFA LKLRPFYESL TLKADTVQTI VDCIRNHPDW
     SSAHIAVETG MRECLKHNYV QSQINARDAS GQTPLHLACE RGDLACVKEL LDESQARTDI
     RDQKGETPMH YASKQESPVI IQALCSRLCS GVNELNSNGE TPLHVACRLG RVESVKALLE
     GGAKCDTRGS TGNPIHTAMK YSEKGCVEQI LKADPFQLQA EDCVYGGTPL HWAKTAEMCR
     LLLDRGCEIN YLSKTGESAL HVLTKKGRFE AAMVLLTHGA NANLKGQDGN TALHLAMKMD
     HMELIKGLIV FGADVEIHND LGETPGLIAA RTSKGPNRRI LLDMLCSVGV QRCLPRSPSS
     PPPLPPPPVS NKTKPRAIGF EDIMYVGAAI GAIGKSEIDG QVMEKKKIDR LLCLDGGGIK
     GLVLIQMLIA LEKEAGRPTR ELFDWVAGTS TGGILALAII HGKSMEYLRC LYFRMKEQVF
     RGSRPYESAP LEDFLKKEFG ENTKMTDIRF PRVMVTSVLA DRHPGELHIF RNYDPPSVRR
     EPSYTTTATF KPLTIPQEQL IWRAARSSGA APTYFRPMGR FLDGGLLANN PTLDAMAEIH
     QFNKSLKAEG REANIKKLGI VVSLGTGKPP QEVVTSVDVF RPSNPLELAK TFVGAKELGK
     MLVDCCTDSD GCAVDRARAW CEMIDTIYHR LSPQLSQEVM LDEVSDKVLV NMLWETQMYL
     FEKREVLQSL AKTLL
//