ID A0A3P8PC95_ASTCA Unreviewed; 724 AA.
AC A0A3P8PC95;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phospholipase A2 {ECO:0000256|RuleBase:RU362102};
DE EC=3.1.1.4 {ECO:0000256|RuleBase:RU362102};
GN Name=PLA2G4A {ECO:0000313|Ensembl:ENSACLP00000014636.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000014636.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000014636.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000014636.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00004496}.
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 AlphaFoldDB; A0A3P8PC95; -.
DR Ensembl; ENSACLT00000014986.1; ENSACLP00000014636.1; ENSACLG00000009930.1.
DR GeneTree; ENSGT01030000234606; -.
DR Proteomes; UP000265100; Chromosome 17.
DR Bgee; ENSACLG00000009930; Expressed in anal fin and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; 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; cd07200; cPLA2_Grp-IVA; 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; IPR002642; LysoPLipase_cat_dom.
DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR10728:SF13; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR Pfam; PF00168; 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}.
FT DOMAIN 1..116
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 112..716
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 402..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 82137 MW; 7FAE9BDC466D5F85 CRC64;
MSKLQVEQQF SHKFTVTVVR AQNVTKGALG DLLDTPDPYV EIFIPTAPES RRRTKHIDND
INPKWNETFH FILDPNQHNV LELTLMDANY VMDETLGTAS FEISKLNVGQ TKTEVTNLDL
RFSHTLCDKE KQFREARREK VMLGIKKLLR TEDPCHPEEV PVIAIAGSGG GFRAMVGFSG
VMKALFESGV LDCTTYIAGL SGSTWYMSTL YSNPDFPNKG PKDINSELMK RVSSNPLRLL
MPQHITHYIQ ALWTKKASGQ PVTFADIFGM LIGETLIPSR MGIKLSDIQE KINQAQCPLP
LFTCLHVKPD VSELMFADWV EFSPYEIGMA KYGTFMTPDL FGSKFFMGTV VKKYEENPLH
FLMGVWGSAF SILFNRVLGV KDRAGGSTME EELEQIKPQH IVGEDTLDDD EPRKGGTENQ
EAEEEFHRTA QASWVQRMFT SVLGDSALFN TREGRAGKVH NFMLGLNLNT NMPFSPLLEI
THAMTPEEEV DAVTDPDEFD RIYEPLDVKS KKIHVVDSGL TYNLPYPLIL RSQRGVDLII
SFDFSARPSD SSPPFKELLL AEKWARMNKL PFPKIDPKVF DREGLKECYV FKPKSGEKNC
PTVIHFVLVN INFRKFKAPG VARETEKEKE LADFDIFDDT ETPYSTFNFQ YSNEAFIQLH
DLMEFNTLNN LEVIKEAIKD CIASRKDNPS SVSRPFNLSE IPKKKILKRD HQGKPVNHLG
NNSQ
//
