ID   A0A091MNX0_9PASS        Unreviewed;       789 AA.
AC   A0A091MNX0;
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=N310_02365 {ECO:0000313|EMBL:KFP78358.1};
OS   Acanthisitta chloris (rifleman).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC   Acanthisitta.
OX   NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP78358.1, ECO:0000313|Proteomes:UP000053537};
RN   [1] {ECO:0000313|EMBL:KFP78358.1, ECO:0000313|Proteomes:UP000053537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP78358.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KK833545; KFP78358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091MNX0; -.
DR   Proteomes; UP000053537; 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:SF54; PLA2C DOMAIN-CONTAINING PROTEIN-RELATED; 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:UP000053537}.
FT   DOMAIN          1..107
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          251..789
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP78358.1"
FT   NON_TER         789
FT                   /evidence="ECO:0000313|EMBL:KFP78358.1"
SQ   SEQUENCE   789 AA;  90956 MW;  D79178AE758625EE CRC64;
     SSLCYLLTIR VIRARNIHQA DVLSQTDCYV SLWLPTASTV KFQTKAIKNC KDPVWNETFY
     FRIQSRVKNV LELALYDKDI VTQDDHLFTV YFDIAKLSLG EEVFMHFKCD SQRQEELEVG
     FALDNISGPP ETIITNGVLV SRKICCLEVQ VVEKKKKEKK SLSKKEFFFK VQGSYEGTQD
     ITLGSDLVFS SSSPAKFHYA RYKQPTLDVM LPGKKRPPSL CSPNMELHSI PSGEKMVLAE
     VSACCFVGET EKPEYYLDVR LGFDLCMQEQ DFLRKRQNYV APALKKVLQL EHDLLDHETP
     VVAIMTTGGG MRSLTALYGS LQGLRKLNVL DCATYLTGLS GTTWTMSNLY RDADWSQKDL
     DKQISEARKH MTKCKINSLS LEYLKYYKKQ LCQRKREGRK TSFIDLWGLV LESLLHDGKD
     NHRLSDQQRA VDCGQNPLPI YTAVNVKNNY STLDFKEWVE FTPYEVGLQK YGVFVRAEDF
     GSEFFMGRLM KKVPESRICF LEGMWSSLFS LNVLYIWNLS HSSEDFWHRW TRDQIDNIEE
     EPLLPLKLHE LQTRLFTPAG PLSSALRSVL TDRLCIAQEH NFLKGFQIHN DYLENTHFRR
     WKDTVLDTFP NQLTQSDEFL SLVDTGFFIN TSIMPLLKPE RKVDVILHLN YSAGSQIQAL
     DQTCKYCSEQ GILFPRVDLS EEDRKKLKEC YLFDGGETPG APVLLFFPLI NDTFQKYKAP
     GQKRSESEME DGKVDLYGCC SPYSTYSIQY TEKAYDRLVQ LAEYNILNNK DLILQALRTA
     VARKRQLKK
//