ID A0A2B4RE75_STYPI Unreviewed; 684 AA.
AC A0A2B4RE75;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 Name=pla2g4a {ECO:0000313|EMBL:PFX14688.1};
GN ORFNames=AWC38_SpisGene21135 {ECO:0000313|EMBL:PFX14688.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX14688.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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 -!- 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:PFX14688.1}.
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DR EMBL; LSMT01000746; PFX14688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4RE75; -.
DR STRING; 50429.A0A2B4RE75; -.
DR EnsemblMetazoa; XM_022951720.1; XP_022807455.1; LOC111344484.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
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; 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:SF40; LYSOPHOSPHOLIPASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF01735; PLA2_B; 2.
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|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|RuleBase:RU362102};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706}.
FT DOMAIN 1..84
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 100..684
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 395..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PFX14688.1"
SQ SEQUENCE 684 AA; 78600 MW; 34D57CE4E40C219E CRC64;
DTPDPYVKLY IQNAPNGRTK TQFISNDPNP VWNEEFKFLI DKELENVLHI TLMDADTFSD
DVVGKTQIFP LDGLEIDRIC RKTFVFRKKS EVDITLELRK CEDPRDLRYS VELCQEEIDF
RENRKPFLFQ AMKKLLGPRG PARMDELPTV GIVGSGGGFR AMVGLSGVFC ALKDMGVLDC
AMYAAGLSGS TWYLSALYSH PKFPYIHPKI VMQQLRHNVQ YSWIRLLTPS WLYKHIKIIH
EKKVRGQPIS FTDFFGYLVG ETILRDRKTI PKLSDQRVAV RYGNVPLPLY TCVQVKNDVS
AKSYNEWVEF SPYEVGMAKY GTFMKAEHFG SKFFCGQLHT QYPEPPLEYL QGIWGSAFTV
LLQRLLSEGQ VPSAIEKVRP SSSVMREDLH QILYSENQDD DEESDSEEEE QSVDGHHIKE
APVFDDNDME EPKEEDHNDP GLLGRIAQRF MNKFPVLQTR SGRAGRVHNF LRGLGLAFAP
VPLESEDVTD AADQLSVKSK RIFLADSGLV FNSPYPLLIR PQRGCDVLLS FDFSSREREI
EMPFEELLLA EEWARKNRLK FPPINAKEQY EEHGLKEFYV FSDPNDPECP VVIHFVLMNG
SFKDYSRPGV PRKTSSEKEF GTFAVFEDPD DHYSTFNFHY SHNSFDRLSQ LMEFNTLLAE
ETIKDVIADG VRRKRQLNAM KSST
//
