ID   I3M5U6_ICTTR            Unreviewed;       752 AA.
AC   I3M5U6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 68.
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:ENSSTOP00000004753.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000004753.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000004753.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; AGTP01024209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGTP01024210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_013212735.1; XM_013357281.1.
DR   AlphaFoldDB; I3M5U6; -.
DR   Ensembl; ENSSTOT00000005303.3; ENSSTOP00000004753.3; ENSSTOG00000005291.3.
DR   GeneID; 101968308; -.
DR   CTD; 8398; -.
DR   eggNOG; KOG0513; Eukaryota.
DR   GeneTree; ENSGT00940000158756; -.
DR   HOGENOM; CLU_010817_0_0_1; -.
DR   OrthoDB; 518048at2759; -.
DR   TreeFam; TF319230; -.
DR   Proteomes; UP000005215; 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   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; 2.
DR   Pfam; PF01734; Patatin; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 7.
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   Reference proteome {ECO:0000313|Proteomes:UP000005215};
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"
FT   REGION          551..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  83613 MW;  BCBF2C06CE0EBC64 CRC64;
     MQFFGRLVNT LTSVTNLFSN PFRVKEVAVA DYASSNRVRE EGQLVLFQNT PSRTWDCILV
     NPRNSHSGFR LFQLESEADA LVHFQQFSSQ LPPFYESSLQ VLHLEALQHL TDLIRNHPSW
     SVAHLAVELG IRECFHHSRI ISCANSTENE EGCTPLHLAC RKGDSEILVE LVQYCHAQMD
     VTDNKGETAF HYAVQGDNSQ VLQLLGKNAS AGLNQVNNQG LTPLHLACQM GKQEMVRVLL
     LCNARCNIMG PGGYPIHTAM KFSQKGCAEM IISMDSNQIH SKDPRYGASP LHWAKNAEMA
     RMLLKRGCDV DSTSASGNTA LHVAVTRNRF DCVMVLLTYG ANAGARGENG NTPLHLAMSK
     DNVEMIKALI VFGAEVDVPN DFGETPALIA SKISRQLQDL MHISRARKPA FILSSLRDEK
     RTHDHLLCLD GGGVKGLVII QLLIAIEKAS GVATKDLFDW VAGTSTGGIL ALAILHSKSM
     AYMRGVYFRM KDEVFRGSRP YESGPLEEFL KREFGEHTKM TDVKKPKVML TGTLSDRQPA
     ELHLFRNYEA PEASREPRFS PSANLKPPTH PSDQLVWRAA RSSGAAPTYF RPNGRFLDGG
     LLANNPTLDA MTEIHEYNQD LIRKGQANKV KKLSIVVSLG TGRSPQVPVT CVDVFRPSNP
     WELAKTVFGA KELGKMVVDC CTDPDGRAVD RARAWCEMVG IQYFRLNPQL GTDIMLDEVS
     DAVLINALWE TEVYIYEHRE QFQKLVQLLL SP
//