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
//