ID A0A2K5NCS6_CERAT Unreviewed; 817 AA.
AC A0A2K5NCS6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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 Name=PLA2G4D {ECO:0000313|Ensembl:ENSCATP00000035292.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000035292.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000035292.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000256|ARBA:ARBA00023922};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000256|ARBA:ARBA00023922};
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|ARBA:ARBA00023422};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000256|ARBA:ARBA00023422};
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 AlphaFoldDB; A0A2K5NCS6; -.
DR STRING; 9531.ENSCATP00000035292; -.
DR Ensembl; ENSCATT00000059574.1; ENSCATP00000035292.1; ENSCATG00000040519.1.
DR GeneTree; ENSGT01030000234606; -.
DR OMA; NSSHPVW; -.
DR Proteomes; UP000233060; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IEA:Ensembl.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IEA:Ensembl.
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:SF31; CYTOSOLIC PHOSPHOLIPASE A2 DELTA; 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:UP000233060}.
FT DOMAIN 5..124
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 272..817
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 817 AA; 91731 MW; 7405ED49455CC73C CRC64;
MESLSPGGPP GHPYQQEASA CWQLTVRVLE ARNLRRADLL SEADPYVILQ LSTVPGMKFK
TKTLTDTSHP VWNEPFHFLI QSQVKNVLEL SIYDEDSITE DDICFKVLYD ISEVLPGKLL
RKTFSQSPQG QEELDVEFLM EETSDRPENL ITNKVLVARE LSCLDVHLDS AGSTAVVADQ
DKLELELELK GSYEDTQTSS LGTASAFRFH YMAALETELS GRLRSSTSNV WNGDNSARRL
TVPLRPLIGK EVTMDVPAQD VPGVRLQLKA EGCSKELAVH LGFNLCAEEQ AFLSRRKQVV
AKALKQALQL DRDLQEDEVP IVGIMATGGG ARAMTSLYGH LLALQKLGLL DCVTYFSGVS
GSTWTMAHLY GDPEWSQKDL EGPIRHAREH LAKSKLEVFS PERLASYRRE LELQAEQDHP
TSFVDLWALV LESMLHGQVM DQKLSGQRAA LERGQNPLPL YLSLNVKENN LETLDFKEWV
EFSPYEVGFL KYGAFVPPEL FGSKFFMGRL MRRIPEPRIC FLEAIWSNVF SLNLLDAWYD
LTSSGESWKQ HIKDKTRSSE KEPLTSLETS SWLEASWLQP GTALAQAFKG FLTDRPLHQR
SPNFLQGLQL HQDYCSHKGF STWADCQLDS TPSQLTPQEP QLCLVDAGYF INTSCPSMFR
PGRRLDLILS FDYSLSAPFE ALQQTEVYCR ARGLPFPRVE PSPQDHQQPR ECHLFSDPAC
PEAPILLHFP LVNASFKDHS APGVQRSPAE LQAGQVNLTG ATSPYALPNM TYKEEDFERL
LRLSDYNVQT SQGAILQALR TALKHRALEA RPPGAQT
//
