ID   A0A091HLJ8_CALAN        Unreviewed;       805 AA.
AC   A0A091HLJ8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=phospholipase A2 {ECO:0000256|ARBA:ARBA00013278};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278};
GN   ORFNames=N300_11539 {ECO:0000313|EMBL:KFO95962.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO95962.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFO95962.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO95962.1};
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; KL217503; KFO95962.1; -; Genomic_DNA.
DR   RefSeq; XP_008494299.1; XM_008496077.1.
DR   AlphaFoldDB; A0A091HLJ8; -.
DR   STRING; 9244.A0A091HLJ8; -.
DR   GeneID; 103530504; -.
DR   CTD; 8398; -.
DR   OrthoDB; 518048at2759; -.
DR   Proteomes; UP000054308; 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; 1.
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; 3.
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:UP000054308};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          151..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          481..665
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          410..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   805 AA;  89830 MW;  B0F3F29D41E9EF39 CRC64;
     MQFFGRLVDT FNSVTQIFTN PYRVKEVSAA EYSAQTCLRE EGRVALYKNR HGHSWDCVLV
     NLQSPQVAFR LFQLDNEAEA LAWFEEFAKH LRPFYESSPQ PLSLEDLQQL SDCFRSHPSW
     SSAHFAVEFG RRENFRHNQI LSCVNNTDSE DGCTPLHLAC RKGDMECLLE LLECHARVDI
     TDRKGETVFH YAVRGNNPQI IELLGSAPTA VLDHLSHEGL TALHLACQLG KEDMVRSLLK
     CHASCSIQGT LGYPIHTALK FSQKGCAQAI LEVDASQVCS RDPRYEATPL HWAKKAEMTR
     LLLEYGSEVN LSSRTADMAL HIAVQRERFD CAMVLLTHGA HTNAKGQDGN TPLHLAMKHD
     NLDMIKAIIV FGGDVEIPND FGETPGLLAA RSSKGANRKV LLDLLQTVGT ERCHPPNPDS
     PSLASSAASS FLEGQPSSRS SFNSLGYQDL LYVSSTLGQL LKAPDVVDSP SEGRRNHDRL
     LCLDGGGIRG LVLIQLLLAI EKAAGRPIRE IFDWVAGTST GGILALAIVH GKSMDYMRCL
     YFRMKDMVFR GSRPYESEPL DEFLKKEFGE NTKMTDVQKP KVMVTGTLCD RQPAELHLFR
     NYPVPETKSS TEYKTTASFK PLTQPEDQLV WRAARCSGAA PTYFRPIGRF LDGGLLANNP
     TLDAMAEIHE YNKTLIKKGQ SQNVRKLGLV VSLGTGKPPQ VPVSSVDVFR PSNPWELAKT
     VFGARELGKM VVDCCTDADG PAVDRARAWC EMTDVPYFRL SPQLHTEVML DEVNDTVLVN
     ALWDTQLYIY QQQEQFKQLV QHLCR
//