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Database: UniProt
Entry: A0A093GHC0_DRYPU
LinkDB: A0A093GHC0_DRYPU
Original site: A0A093GHC0_DRYPU 
ID   A0A093GHC0_DRYPU        Unreviewed;       827 AA.
AC   A0A093GHC0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-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_11658 {ECO:0000313|EMBL:KFV66199.1};
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:KFV66199.1, ECO:0000313|Proteomes:UP000053875};
RN   [1] {ECO:0000313|EMBL:KFV66199.1, ECO:0000313|Proteomes:UP000053875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV66199.1};
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; KFV66199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093GHC0; -.
DR   STRING; 118200.A0A093GHC0; -.
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:SF22; CYTOSOLIC PHOSPHOLIPASE A2 ZETA; 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|RuleBase:RU362102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053875}.
FT   DOMAIN          12..133
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          293..827
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV66199.1"
FT   NON_TER         827
FT                   /evidence="ECO:0000313|EMBL:KFV66199.1"
SQ   SEQUENCE   827 AA;  94562 MW;  0B94B4F2A90B2D7B CRC64;
     RALPLLAAVL FQRKERKETG LYRWRWEKHP YYNLTVKVLR ARNIKGTDLL SKADCYVEIK
     LPTASPIVSR TRVIDNSDNP EWNQTFQYRI HSAVKNILEL TLYDKDILAS DELTSIVFDV
     GGMKPGQPLL RTFKLNPEAN EELDVEFYLE KCSDAPTEVL TNGVLVVHPC LSLQGTVNKE
     EKTKEKQQGS CEVKVSVPGS YERQLSIPWR PDNEDYETSF VFHMDKEMCP ELQVELEQTI
     SVLQDGVNPD VEKHTTVLGL GTVPVDSLPT GQQVDRIISL GEGQSLNMSL KTEESTWDLD
     VRLGFDLCKE EREFLDKRKK IVSEVLRKTL QLKESPPKDE VPVVAVLGSG GGMRALTSFY
     GSLAGLQELG LLDATMYLCG ISGSTWCLST LYQDPDWSQK DLQAAISRAQ VTVSSSKAGA
     FSPERLKYYF QELSAMEISG RKVSFTDLWG LIVEYFLQQK EDPSKLSDQQ AAVKWAQNPY
     PIYAAVNVKP SISSVDFAEW CEFTPYEVGF RKYGAFVRTE DFDSEFFMGR LVQKHPEPRI
     CFLQGMWGSA FAASLDDICL KVIGIGLGFL DSFKDVIKVV DDCRRFHFRD PTRLKTRLVI
     PGGPLLQIFQ DFFRSRVTCG ETFNFMQGLY LHKDYVNVKK FVAWRGTHLD AFPNQLTPME
     ESLYLVDGGF SINSPFPLVL QPERDVDVIL SFNYSWEAPF EVLELTQKYC EEQEIPFPKI
     KISEEDERKP KECYMFVDND NPKAPIVLHF PLVNDTFQEY KAPGVKRESE EEKAFGDFDI
     ESKDSPYRTL NFTFEPYDFS RLVEVNRYNV LNSKDTLFRT LNLALQR
//
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