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Database: UniProt
Entry: A0A287DDQ4_ICTTR
LinkDB: A0A287DDQ4_ICTTR
Original site: A0A287DDQ4_ICTTR 
ID   A0A287DDQ4_ICTTR        Unreviewed;       807 AA.
AC   A0A287DDQ4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
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:ENSSTOP00000031636.1};
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:ENSSTOP00000031636.1, 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:ENSSTOP00000031636.1}
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_005322315.1; XM_005322258.2.
DR   RefSeq; XP_013212731.1; XM_013357277.1.
DR   RefSeq; XP_013212732.1; XM_013357278.1.
DR   RefSeq; XP_013212733.1; XM_013357279.1.
DR   RefSeq; XP_013212734.1; XM_013357280.1.
DR   AlphaFoldDB; A0A287DDQ4; -.
DR   STRING; 43179.ENSSTOP00000031636; -.
DR   Ensembl; ENSSTOT00000034492.1; ENSSTOP00000031636.1; ENSSTOG00000005291.3.
DR   GeneID; 101968308; -.
DR   CTD; 8398; -.
DR   GeneTree; ENSGT00940000158756; -.
DR   InParanoid; A0A287DDQ4; -.
DR   OrthoDB; 518048at2759; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:Ensembl.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:Ensembl.
DR   GO; GO:0017171; F:serine hydrolase activity; IEA:Ensembl.
DR   GO; GO:0019731; P:antibacterial humoral response; IEA:Ensembl.
DR   GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IEA:Ensembl.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:Ensembl.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; IEA:Ensembl.
DR   GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
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; 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          482..666
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          606..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   807 AA;  89540 MW;  A2E8FE4CD6957CB8 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 SKISRHATRK ALLTLLRTVG ANYRISLLQE
     VPTEQGSTAS SHPLVSPERA QPPPISLNNL ELQDLMHISR ARKPAFILSS LRDEKRTHDH
     LLCLDGGGVK GLVIIQLLIA IEKASGVATK DLFDWVAGTS TGGILALAIL HSKSMAYMRG
     VYFRMKDEVF RGSRPYESGP LEEFLKREFG EHTKMTDVKK PKVMLTGTLS DRQPAELHLF
     RNYEAPEASR EPRFSPSANL KPPTHPSDQL VWRAARSSGA APTYFRPNGR FLDGGLLANN
     PTLDAMTEIH EYNQDLIRKG QANKVKKLSI VVSLGTGRSP QVPVTCVDVF RPSNPWELAK
     TVFGAKELGK MVVDCCTDPD GRAVDRARAW CEMVGIQYFR LNPQLGTDIM LDEVSDAVLI
     NALWETEVYI YEHREQFQKL VQLLLSP
//
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