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Database: UniProt
Entry: A0A091GLP6_9AVES
LinkDB: A0A091GLP6_9AVES
Original site: A0A091GLP6_9AVES 
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
//
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