ID A0A091GLP6_9AVES Unreviewed; 770 AA.
AC A0A091GLP6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=N303_08199 {ECO:0000313|EMBL:KFO82913.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO82913.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO82913.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO82913.1};
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; KL448321; KFO82913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GLP6; -.
DR STRING; 55661.A0A091GLP6; -.
DR Proteomes; UP000053760; 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:SF35; PHOSPHOLIPASE A2; 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:UP000053760}.
FT DOMAIN 1..88
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 236..770
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO82913.1"
FT NON_TER 770
FT /evidence="ECO:0000313|EMBL:KFO82913.1"
SQ SEQUENCE 770 AA; 87863 MW; 38C86A308C8E2AF2 CRC64;
SSTVTQSDCY VSLSLPTASV QHFRTKTVQN NKNPTWNETF HFTIQSQVKN ILELKVCDED
NTTEDDHLLT VFFDVSKIQL GENIRLCFQL NPQGKEELEV EFTMESRALL IVDAFLSFPG
CVLQSREVSC LDVQVNGGRL RKDSTERKFA LTVDGSYEGT QIHTLSSCLC PTSSARFHYI
KYNQSVLTVA LPRRRTLSRV CGCCQSGVHA GSVLSGRFQL QAFVCQIVLF QTQGLFFRPR
NLDARLGFDL CSDEQDFLRN RKRVVAAALK EVLHLEEDLQ EHEVPIVAVT TAGCGIRALT
AMYGSILGLQ KLRVLDCISY ISGSSGTTWT MTKLYEDADW SRKDLGEIII EARKQAAKCK
MDAFCLRSLR NYYRELSQRT QAGHKTSFID LWGLMIESML NDGKCHHRLS DQRRAVNQGQ
NPLPIYLALN VKDKVTTKDF REWVEFTPYE VGFLKYGAFI RAEDFGSEFF MGRLMKKLPE
SRICFMQGMW SSIFSKNLLD AWHAADNSED FWHRWTQDKV TEIEEQPDLP EKPHEMATCM
FTPTSGLSTS LRDILTDRPA VSKYHNFLRG FQMHNEYIQQ EHFTKWKDTL LDASPNDLRS
NSDHLELVDA AFFFETSCPP LMRPERKVDV IIFLNYTGGS QTLPLEQACR YFSEQGIAFP
STGLKDDEKN LKECYMFDGA GMPGAPLLLY FPLVNDTFQR YVAPGMSRSA AEMEEGKVDI
SSFCSPYSTR EVSLKAEDFN KLMKLTNYNI MNNENMILQA LRMAVAQKKQ
//