ID A0A091RGD0_9GRUI Unreviewed; 748 AA.
AC A0A091RGD0;
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=N332_11177 {ECO:0000313|EMBL:KFQ38903.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ38903.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ38903.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ38903.1};
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; KK817766; KFQ38903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RGD0; -.
DR Proteomes; UP000053369; 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: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:UP000053369}.
FT DOMAIN 1..88
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 234..748
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ38903.1"
FT NON_TER 748
FT /evidence="ECO:0000313|EMBL:KFQ38903.1"
SQ SEQUENCE 748 AA; 85964 MW; 1E0832D37BC9D4DA CRC64;
SSLVSQADCY VSLWLPTAMC EKCRTKTVRN SNNPVWNETF YFRIQSQVKN VLELTVYDED
FATPDDHLLC ALFDTAKLPI ERTVLLYFKP SPKAKEELEV EFKLEAASGP HEAIATNGVL
VCRELCCLEV EVAEKKQQKS NKELSFTVKG SFEGTQDMML GPDGVVSPSG PTKFHYIKYS
QPTLDVMLPK KRRYHPVYTG SPVVMLNSLP MGRTTTVAEE LCFSSSFLHK SNCSCHQDLD
MRFGFDLCSE EMVFLGKRKR YVASALKNVF HLQQDLQDHE VPIVAIITTG GGLKSMTGLY
GSLMGLKKLN LLDCITYISG LSGTTWTMAN LYRDAYWSQK DLDSHIGEAQ KQATKCKMGC
FSMDRMKYYN KQLCQRKEEG YRTSFIDLWG LMIEYLLNDG KDSRKLSDQQ EALCDGQNPL
PIYVSVSVRD NYSTNDFKEW VEFTPYEVGL LKYGAFVRTE NFGSEFFMGR LLKKLPESRI
CYLQGMWSSI FSVNLLQIWG LSHSSEDFWK RWTQDRIEEV DEDPVLPTRP HELRTRMYTP
PGPLSSALRG ALTDRFSVAQ HYNFLKGYQL HSNYLENEHF CRWKDTVLDS RPNQLMGNPD
HLGMIDAGFF INTSSAPLLR PQRKVDVIIY LSYTTGSHTS VLDKAYKYYS EQKIPFPKIS
LTDEDRKNLK ECYLFQDSDL PGCPIVIFLP LVNDTFREYK APGVKRCCSE MEGGQLDLTS
RFSPYRMFSV RYTDENYHRL LKLSEYHI
//