ID F7ABM8_CALJA Unreviewed; 741 AA. AC F7ABM8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 27-NOV-2024, entry version 66. DE RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278}; DE EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278}; GN Name=PLA2G6 {ECO:0000313|Ensembl:ENSCJAP00000022063.3}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae; OC Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000022063.3, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000022063.3} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000022063.3} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2024) 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; F7ABM8; -. DR Ensembl; ENSCJAT00000023325.5; ENSCJAP00000022063.3; ENSCJAG00000011999.5. DR GeneTree; ENSGT00940000158756; -. DR HOGENOM; CLU_010817_0_0_1; -. DR Proteomes; UP000008225; Chromosome 1. DR Bgee; ENSCJAG00000011999; Expressed in liver and 6 other cell types or tissues. DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter. DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:InterPro. DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IEA:TreeGrafter. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; IEA:TreeGrafter. DR CDD; cd07212; Pat_PNPLA9; 1. DR FunFam; 1.25.40.20:FF:000338; 85/88 kDa calcium-independent phospholipase A2; 1. DR FunFam; 3.40.1090.10:FF:000006; 85/88 kDa calcium-independent phospholipase A2; 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; 2. 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}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW 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:UP000008225}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}. FT REPEAT 151..184 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 219..251 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 316..348 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT REPEAT 349..381 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT DOMAIN 416..600 FT /note="PNPLA" FT /evidence="ECO:0000259|PROSITE:PS51635" FT MOTIF 420..425 FT /note="GXGXXG" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161" FT MOTIF 452..456 FT /note="GXSXG" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161" FT MOTIF 587..589 FT /note="DGA/G" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161" FT ACT_SITE 454 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161" FT ACT_SITE 587 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161" SQ SEQUENCE 741 AA; 82574 MW; 6215825B31498972 CRC64; MQFLGRLVNT LSSVTNLFSN PFRVKEVAVA DYASSRRVRE EGQLTLFQNA PSRTWDCVLV NPRNSQSGFR LFQLEVEADA LVNFQQYSSQ LLPFYESSPQ VLQTEVLQHL TDLIRNHPSW SVAHLAVELG IRECFHHSRI ISCANSTENE EGCTPLHLAC RKGNEEILVE LVRYCHAQME VTDNKGETAF HYAVQGENSQ VLQLLGKNAV AGLNQVNNQG LTPLHLACQL GKQDMVRALL LCNARCNIMG PSGYPIHSAM KFSQKECAEM IISMDSSQIH SKDPRYGASP LHWAKNAEMA RMLLKRGCDV NGTSSAGNTA LHVAVMRDRF DCAMVLLTHG ANADARGEHG NTPLHLAMSK DNVEMIKALI VFGAEVDTQN DFGETPTLLA SKISKRMCSA PSSLPRYSHC SHDHLLCLDG GGVKGLVIIQ LLIAIEKASG VATKDLFDWV AGTSTGGILA LAILHSKSMA YMRSVYFRMK DEVFRGSRPY ESGPLEEFLK REFGEHTKMT DVKKPKVMLT GTLSDRQPAE LHLFRNYEAP ETVREPRFNQ NVNLRPPTQP SDQLVWRAAR SSGAAPTYFR PNGRFLDGGL LANNPTLDAM TEIHEYNQDL IRKGQANKVK KLSIVVSLGT GRSPQVPVTC VDVFRPSNPW ELAKTVFGAK ELGKMVVDCC TDPDGRAVDR ARAWCEMVGI QYFRLNPQLG TDIMLDEVSD TVLVNALWET EVYIYEHREE FQKLIRLLLS P //