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Database: UniProt
Entry: A0A091RGD0_9GRUI
LinkDB: A0A091RGD0_9GRUI
Original site: A0A091RGD0_9GRUI 
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
//
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