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
//