ID   A0A093G7L5_DRYPU        Unreviewed;       795 AA.
AC   A0A093G7L5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Phospholipase A2 {ECO:0000256|ARBA:ARBA00013278, ECO:0000256|RuleBase:RU362102};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278, ECO:0000256|RuleBase:RU362102};
DE   Flags: Fragment;
GN   ORFNames=N307_11665 {ECO:0000313|EMBL:KFV66205.1};
OS   Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX   NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV66205.1, ECO:0000313|Proteomes:UP000053875};
RN   [1] {ECO:0000313|EMBL:KFV66205.1, ECO:0000313|Proteomes:UP000053875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV66205.1};
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|RuleBase:RU362102};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon
CC       calcium binding. {ECO:0000256|RuleBase:RU362102}.
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DR   EMBL; KL215719; KFV66205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093G7L5; -.
DR   STRING; 118200.A0A093G7L5; -.
DR   Proteomes; UP000053875; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   CDD; cd04036; C2_cPLA2; 1.
DR   CDD; cd07201; cPLA2_Grp-IVB-IVD-IVE-IVF; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR041847; C2_cPLA2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR040723; cPLA2_C2.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF54; PLA2C DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF18695; cPLA2_C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU362102};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362102};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053875}.
FT   DOMAIN          1..107
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          258..795
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV66205.1"
FT   NON_TER         795
FT                   /evidence="ECO:0000313|EMBL:KFV66205.1"
SQ   SEQUENCE   795 AA;  91142 MW;  E62874D4D27AB08D CRC64;
     SSLCYLLTVR VIRARNIHQA DVLSQTDCYV SLWLPTASAD RFQTKTIKNC KDPVWNETFY
     FRIQSQVKNV LELALYDKDV VTQDDHLFTV YFDIAKLSLG EQVFMHFKCD SQRQEELEMG
     FSLDNISGPP ETIITNGVLV SRKICCLEVQ VVEKKKKQKK SLSKKGFSFK VRGSYEGTQD
     IMLGSDLIFN NSSAKFHYAR YKQPMLDVTL PGKKEPSSFH SHMHDTGSPN VELHSLPSGK
     NMILAEVSAC SLVGEVEKPD PDHLDVRLGF DLCRQEQDFL CKRQKHVAPA LKKVLQLEQD
     LLDNETPVVA IMTTGGGMRS LTALYGSLRG LKKLNVLDCA TYLTGLSGTT WTMSNLYRDA
     DWSQKDLDKQ ISEARKHMTK CKINSLSLDY LKYYKKQLCQ RKREGRKTSF IDLWGLVLES
     LLHDGKDNHR LSDQQQAIDR GQNPLPIYTA VNVKNNYSTL DFKEWVEFTP YEVGLQKYGV
     FVRAEDFGSE FFMGRLMKKI PESRICFLEG IWSSLFSLNV LYLWNLSHSS EDFWHRWTRD
     KIDNIEEEPV LPLKPHELRT RLATPPGPLS SALRGALTDR LCIAQEHNFL KGLQLNNDYL
     ENKHFCRWKD TVLDTFPNQL TQSDEFLSLV DTGFFINTSI MPLLKPERKV DVILHLNYSA
     GSQTQALEQT CKYCSEQGIL FPKVDLSEED RKNLKECYLF DGAETPGAPV LLFFPLINDT
     FQKYKAPGLK RSESEMEDGK VDLYGCCSPY STYSVQYSEK AYDRLVQLGE YNILNNEALI
     MQALRTAVAR KRQKK
//