ID   A0A0Q3UU43_AMAAE        Unreviewed;       805 AA.
AC   A0A0Q3UU43;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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};
GN   ORFNames=AAES_37992 {ECO:0000313|EMBL:KQK85850.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK85850.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK85850.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK85850.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQK85850.1}.
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DR   EMBL; LMAW01000714; KQK85850.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3UU43; -.
DR   Proteomes; UP000051836; 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   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:SF32; CYTOSOLIC PHOSPHOLIPASE A2 BETA; 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:UP000051836}.
FT   DOMAIN          1..116
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          258..805
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   805 AA;  93156 MW;  6C8F8F628A9A232A CRC64;
     MGSPPAKMKF CPIHMLSVRI IQAKNITSRD LLTASDCYVR LWLPSASNRK LQTKTIKNSD
     NPVWNETFYF RIQREVENIL ELAVCDEDPL TKDDMQFTVL FNVARIRPGE IIRETFALKS
     ETGAMHFSAS GPGPSEHLIT NDVLVSRDVC CLEVQVDINE SRKYLQEGKN LVLTVPESHE
     GTQKTTEDTD TFYFHCVKAW EPVLKIRLQK VCDKEDEDSN LSDTLTVPLK FLPVGYKVKI
     TLPVRNNVPL YLYLQLNDCT EKLDVRLGYD LCLEEQEFLL KRKRVVANAL KRVLRLERDL
     HGHEVPVIAV MATGGGLRAM SAMFGHLIAL QKLNLLDCVT YVTGASGSTW TLADLYEHAD
     WSQKSLEGPL KAVKEQVTKC KLNLMSIEHL KYYHKELAER AKAGHVSSFT TLWSLVQEMF
     LHERPRKYKL TDQRKALEHG QNPLPFYSVL NVKEEKFSTF RFREWAEFSP YEVAIPKYGA
     SIPSEYFDSE FFMGRRVKKL PESRICYLEG LWTNIFTRNL LDGLYWSSNS NEFWERWAKD
     MVDIEKHSPE EDITVIEPPS CLSGKLYEMF QDIMTKRPLL GKSHNFLRGL EFHKDYIHQR
     KFIEWKDSVL DAFPNNLTPL QKYLCLIDVG YFINTSGAGL FKPERNVDVI ISLDYGLGNV
     FKQLEMTYKY CKIQKIPFPK VEISKEEEMN PKECYVFSDA EDPRAPIVIH FPLVNDTFKE
     FKEPGVKRSL SEMEEGKVNL DNSCSPYYLI RLIYSSENFD KLVNLSTYNI LNNKDLLLQT
     IQSAVERRRS SXTWNLPSYS RAGYR
//