ID A0A1S2ZHD3_ERIEU Unreviewed; 753 AA.
AC A0A1S2ZHD3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN Name=PLA2G6 {ECO:0000313|RefSeq:XP_007519386.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007519386.1};
RN [1] {ECO:0000313|RefSeq:XP_007519386.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_007519386.1; XM_007519324.2.
DR AlphaFoldDB; A0A1S2ZHD3; -.
DR GeneID; 103110157; -.
DR CTD; 8398; -.
DR OrthoDB; 518048at2759; -.
DR Proteomes; UP000079721; Unplaced.
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; 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:UP000079721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 151..184
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 220..252
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 317..349
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 350..382
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 428..612
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 753 AA; 83918 MW; 65E3469736B2A57F CRC64;
MQFFGRLVNT LSSVSTLFSS PFRVKEVTLS DYTTNVRVRE EGQLILFQNM PSRTWDCVLV
NPRNSQSGFR LFQLETEAEA LVNFQQFSSQ LPPFYESSAH VLHIEILQSL TDLIRSHPSW
SVAHLAVELG IRECFHHSRI ISCANSTESE EGCTPLHLAC RKGDGEILVE LVHYCHAQMD
VTDNNGETAF HYAVQGDNAQ VLQLLGKNVS SAGLNQVNNQ GQTPLHLACQ MGKQEMVRVL
LLCNARCNIM GPGGYPIHTA MKYSQKGCAE MIISMDSNQI HSKDPRYGAS PLHWAKTGEM
ARLLLKRGCD VNSTSAAGNT ALHVAVMRNR FECVMMLLTH GANADARGEN GNTPLHLAMS
KDNVEMVKAL IVFGAEVDTP NDYGETPVLI ASKISKQLQD IVHISRARKP AFILSSMRDE
NRTHDHLLCL DGGGVKGLII IQLLIAIEKA SGVATKDLFD WVAGTSTGGI LALAILHSKS
MAYMRGVYFR MKDEVFRGSR PYESGPLEEF LKREFGEHTK MTDVKKPKVM LTGTLSDRQP
AELHLFRNYE APEMIREPRF SQNINLKPPT QPSDQLVWRA ARSSGAAPTY FRPNGRFLDG
GLLANNPTLD AMTEIHEYNQ DLIRKGQGNK VKKLSIVVSL GTGRSPQVPV TCVDVFRPSN
PWELAKTVFG AKELGKMVVD CCTDPDGRAV DRARAWCEMV DIQYFRLNPQ LGVDIMLDEV
SNSVLVNALW ETEVYIHEHR DEFQKLIQLL LSP
//