ID   A8K460_HUMAN            Unreviewed;       752 AA.
AC   A8K460;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAF83514.1};
RN   [1] {ECO:0000313|EMBL:BAF83514.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:BAF83514.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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   EMBL; AK290825; BAF83514.1; -; mRNA.
DR   AlphaFoldDB; A8K460; -.
DR   PeptideAtlas; A8K460; -.
DR   DNASU; 8398; -.
DR   BioGRID-ORCS; 8398; 8 hits in 1163 CRISPR screens.
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; 3.
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.
DR   Genevisible; A8K460; HS.
PE   2: Evidence at transcript level;
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          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          427..611
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
SQ   SEQUENCE   752 AA;  84092 MW;  129099FF946D0D18 CRC64;
     MQFFGRLVNT FSGVTNLFSN PFRVKEVAVA DYTSSDRVRE EGQLILFQNT PNRTWDCVLV
     NPRNSQSGFR LFQLELEADA LVNFHQYSSQ LLPFYESSPQ VLHTEVLQHL TDLIRNHPSW
     SVPHLAVELG IRECFHHSRI ISCANCAENE EGCTPLHLAC RKGDGEILVE LVQYCHTQMD
     VTDYKGETVF HYAVQGDNSQ VLQLLGRNAV AGLNQVNNQG LTPLHLACQL GKQEMVRVLL
     LCNARCNIMG PNGYPIHSAM KFSQKGCAEM IISMDSSQIH SKDPRYGASP LHWAKNAEMA
     RMLLKRGCNV NSTSSAGSTA LHVAVMRNRF DCAIVLLTHG ANADARGEHG NTPLHLAMSK
     DNVEMIKALI VFGAEVDTPN DFGETPTFLA SKIGRQLQDL MHISRARKPA FILGSMRDEK
     RTHDHLLCLD GGGVKGLIII QLLIAIEKAS GVATKDLFDW VAGTSTGGIL ALAILHSKSM
     AYMRGMYFRM KDEVFRGSRP YESGPLEEFL KREFGEHTKM TDVRKPKVML TGTLSDRQPA
     ELHLFRNYDA PETVREPRFN QNVNLRPPAQ PSDQLVWRAA RSSGAAPTYF RPNGRFLDGG
     LLANNPTLDA MTEIHEYNQD LIRKGQANKV KKLSIVVSLG TGRSPQVPVT CVDVFRPSNP
     WELAKTVFGA KELGKMVVDC CTDPDGRAVD RARAWCEMVG IQYFRLNPQL GTDIMLDEVS
     DTVLVNALWE TEVYIYEHRE EFQKLIQLLL SP
//