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Database: UniProt
Entry: A0A1I8P3D0_STOCA
LinkDB: A0A1I8P3D0_STOCA
Original site: A0A1I8P3D0_STOCA 
ID   A0A1I8P3D0_STOCA        Unreviewed;       684 AA.
AC   A0A1I8P3D0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN   Name=106085447 {ECO:0000313|EnsemblMetazoa:SCAU004450-PA};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU004450-PA, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU004450-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU004450-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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_013105156.1; XM_013249702.1.
DR   AlphaFoldDB; A0A1I8P3D0; -.
DR   STRING; 35570.A0A1I8P3D0; -.
DR   EnsemblMetazoa; SCAU004450-RA; SCAU004450-PA; SCAU004450.
DR   KEGG; scac:106085447; -.
DR   VEuPathDB; VectorBase:SCAU004450; -.
DR   OrthoDB; 518048at2759; -.
DR   Proteomes; UP000095300; 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; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 3.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          21..53
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          115..147
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          148..180
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          361..545
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          308..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   684 AA;  74426 MW;  4A315C166FC5F8FE CRC64;
     MAGSTNLIDK STVNLNHINS DGYTPLHLAC LADKPECVKA LLIAGADVNI EAKNISKLYK
     TSTPTSVAEF LKQNANKLYT QDMKFGGSPL HWCSSRETLN ALIMQGCNVN ATNFDGRTAL
     HVMVARNRFE CVVTLLAHDA EIDIVDKDGN TPLHIAIEQK LVNIVQCLVV FGCDINIKNK
     NGETPRHMVG AETGASKQDE ILYILHSVGA KRCSDVKGKC PAGCSSSGTY NGIPPEAPES
     VEKREHIENM LASTSRQVAV GMFASAANGF LNEVKEPPVV VNTEKVEKGQ SIMDALLSMF
     KVNADSMKAS PSSSVENINP NEGDEATSGK CSPEATSSNM SLNSATSTQK GDKPYGKGRL
     LCLDGGGIRG LVLVQVLLEI EKISQTPIVH MFDWIAGTST GGILALGLGC GKSMRQCMGL
     YLRMKEQCFV GSRPYPSEFF ETILKDNLGE FTVMTDIKHP KVMVTGVMAD RKPVDLHLFR
     SYQSASDILG IITPITNRRS PPPDPKDQLV WRAARATGAA PSYFRAFGRF LDGGLIANNP
     TLDAMTEIHE YNMALRSVGR ENEAVPVSVV VSIGTGLIPV TELKDIDVFR PESIWDTAKL
     AYGLSTIGNL LVDQATASDG RVVDRARAWC STIGVPYYRF NPQLSEDIAM DEKNDQKLIN
     MLWCAKAYVH ANRNKIIEMI NCLK
//
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