ID   A0A093ESP0_TYTAL        Unreviewed;       784 AA.
AC   A0A093ESP0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=N341_12840 {ECO:0000313|EMBL:KFV43461.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV43461.1, ECO:0000313|Proteomes:UP000054190};
RN   [1] {ECO:0000313|EMBL:KFV43461.1, ECO:0000313|Proteomes:UP000054190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV43461.1};
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; KK370757; KFV43461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093ESP0; -.
DR   Proteomes; UP000054190; 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:SF24; CYTOSOLIC PHOSPHOLIPASE A2 EPSILON; 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:UP000054190}.
FT   DOMAIN          1..101
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          248..784
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV43461.1"
FT   NON_TER         784
FT                   /evidence="ECO:0000313|EMBL:KFV43461.1"
SQ   SEQUENCE   784 AA;  89970 MW;  58744DA2E37C6FC8 CRC64;
     LTVKIISMRN LHKADLLSQT DCYVKLWLPT ASCREARTRT VRNCRNPVWN ETFHFMIQSA
     VKNVLELTVC DEDTFTPDDQ LLTVSFDVAK IQPGEKVHLI FELNPENQEE LEVEFLLENI
     PGVSENIITN GVLVSREVSC LEVHVNDTKM KSPYTRRDFT FTMKGSYEET QNVSISPHCR
     RGSSETTMFH YIKHSQPRLH MTRPKERFFC GVSRREMGVS SPLAVPLHSL DLGKKVTVMR
     VMCLVLFLCS SYKNLDLRLG FDLCAKEQDF ICKRKKVVAA ALKNVLHLDE DLQEDEVPVV
     AVMTTAGGVR SMTAMLGSLL ALQELGVLDC VSYISGLSAT TWTMAKLYED ANWSQKDLRG
     PVDDIRKHVI KSKLHCFSLD HMEYYEKELC ERKQEGHKLS FTDLWGLFID CMLHHQESTH
     KLSDQQLAVN QGQNPLPIYL SLNVKDNFST LDFREWVEFT PYEVGFLKYG AFVCSEDFGS
     EFFMGHLMKK IPESRICFLE GTWSNIFSQN FMDAVYLSGH SDGFWHRWTR NTEHDIEEHP
     ALPKKPHEQT TCLSIPKGFL SNALREMMTG RPVVSTYHNF LKGLQLHNKY LENESFCMWK
     DTVLDSSPNQ LNEMGDYLKL IDTAFFINTS CPPILRPERK VDVILHLNYS GGSQTLPLDL
     FSEYCLEHGI PFPGTELSQE DREHLKECYV FEDSVEAPIL AYFPLVCDTF QKYKAPNVAR
     SPTELDQGRV DVSNCSAPYG TGLLTYTEEN FNKLLNLCSY NILNNKHLIL QALRTAVERK
     KQFK
//