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Database: UniProt
Entry: A0A093CQR2_TAUER
LinkDB: A0A093CQR2_TAUER
Original site: A0A093CQR2_TAUER 
ID   A0A093CQR2_TAUER        Unreviewed;       813 AA.
AC   A0A093CQR2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN   ORFNames=N340_05020 {ECO:0000313|EMBL:KFV18220.1};
OS   Tauraco erythrolophus (Red-crested turaco).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX   NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV18220.1, ECO:0000313|Proteomes:UP000053661};
RN   [1] {ECO:0000313|EMBL:KFV18220.1, ECO:0000313|Proteomes:UP000053661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV18220.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KL469278; KFV18220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093CQR2; -.
DR   Proteomes; UP000053661; 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; 2.
DR   Pfam; PF12796; Ank_2; 2.
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:UP000053661};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          159..191
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          226..258
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          323..355
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          356..388
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          489..673
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
SQ   SEQUENCE   813 AA;  90726 MW;  8320ED6C3ED16E7F CRC64;
     MQFFGRLVNT INSVTQIFTN PYRVKEVPAA EYAAHTCLRE EGRVALYKNS LARSWDCLLV
     NPQSPQVAFR LFQLDNEADA LVRFEQYAGQ LRPFYESSHQ PLSLEELQQL SDCFRNHPSW
     SSAHVAVEIG RRENFRHNHV LRQGAGRGVH CVNNTDSEDG CTPLHLACRK GDMECLLELL
     ECHARVDITD RNGETVFHYA VRGNNPHIIE LLGRTPTAGL DHLSHEGLTA LHLACQLGKE
     DMVRSLLKCR ASCSVVGTLG YPIHTALKFS QKGCAQAILE VDASQVRSKD PRHEATPLHW
     AKKAEMTRLL LEYGSEVNLT SRTADMALHI AVKRGRFDCA MVLLTHGAHT NARGQDGNTP
     LHLAMKHDHL DMIKAIIVFG GDVEIPNDFG ETPGLLAARS SKGANRKVLL DLLQTIGTER
     CHPPNPDSPS LAPSAASFFL EGQPSSRSSF NSLGYKDLLY VSTTLGQLLK APDVVDSPSE
     GRRNHDRLLC LDGGGIRGLV LIQLLLAIEK AAGRPIREIF DWIAGTSTGG ILALAIVHGK
     SMDYMRCLYF RMKDMVFRGS RPYESEPLDE FLKKEFGENT KMTDVQKPKV MVTGTLCDRQ
     PAELHLFRNY PVPETKTSTE YKTSASFKPL TQPEDQLVWR AARCSGAAPT YFRPIGRFLD
     GGLLANNPTL DAMAEIHEYN KTLIKKGQRQ KVRKLGLVVS LGTGKPPQVP VSSVDVFRPS
     NPWELAKTVF GARELGKMVV DCCTDADGPA VDRARAWCEM TDVPYFRLSP QLHTEVMLDE
     VNDTVLVNAL WDTQLYIYQQ REQFEQLVQH LCR
//
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