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Database: UniProt
Entry: A0A2U9BMG2_SCOMX
LinkDB: A0A2U9BMG2_SCOMX
Original site: A0A2U9BMG2_SCOMX 
ID   A0A2U9BMG2_SCOMX        Unreviewed;       793 AA.
AC   A0A2U9BMG2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN   ORFNames=SMAX5B_011584 {ECO:0000313|EMBL:AWP05233.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP05233.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP05233.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-2017) 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; CP026250; AWP05233.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9BMG2; -.
DR   STRING; 52904.ENSSMAP00000034679; -.
DR   Proteomes; UP000246464; Chromosome 8.
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; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13606; Ank_3; 1.
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.
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:UP000246464};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          150..183
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          218..250
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          315..347
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          348..380
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          469..653
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
SQ   SEQUENCE   793 AA;  87374 MW;  8BB496475EF35DAD CRC64;
     MQFLGRLLDT VSSVSTLFTN PYRVRDVPLS DYGGGGKVLL KEEGRILLYR NTNYQSWDGL
     LMCPETPTMV LRLFQVASEE DAMNWFAQYA LKLRPFYETL PLKAETTQPI VDCIRQHPDW
     SSAHVAVETG LRECLKHNYV QSQINSRDAL GQTPLHRACE RGDLVCVKEL LDESQARTDI
     KDHSGETPMH CAAKQDSPAV IQVLCLRLCS GVNELNGNGE TPLHVACRLG RVEGVKALLD
     GGAKCDVAGG TGYPIHSAMK YSEKGCVEEI LKADRGQLQA EDSMYGGTPL HWAKTAEMCR
     VLLEHGCAVN YLSKTGESAL HILTKRGRFE AAMVLLTHGA NANLKGQDGN TALHLAMKMD
     HIDLIKALIV FGADVEIHND LGETPGLIAA RTSKGPNRKI LLDMLCSVGV QRCHPPSPGS
     PPPVSYQVKT QGIGFEDIMY VGATIGAMGK GTSEVDGRKM VKTKMDRLLC LDGGGIKGLV
     LIQMLIALEK EAGRPTRDLF DWVAGTSTGG ILALAIIHGK SMEYLRCLYF RMKEQVFRGS
     RPYESAPLED FLKKEFGENT KMTDVQYPRV MVTSVLADRH PGELHIFRNY NPPSVHRVPP
     YATTATYKPI TVPQEQLVWR AARSSGAAPT YFRPMGRFLD GGLLANNPTL DAMSEINQYN
     KALKAEGHGE KIKKLGMVVS LGTGKPPQVV VSSVDVFRPS NPLELAKSFV GARELGKMLV
     DCCTDSDGCA VDRASAWCEM IDTIYHRLSP QLSQEVMLDE VSDAVLVDML WETQMYLYEK
     REMLRSLANV LLG
//
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