PLD3A_DANRE
ID PLD3A_DANRE Reviewed; 784 AA.
AC A5D6R3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3-A {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q8N3E9};
DE AltName: Full=Phosphoinositide phospholipase C-delta-3-A;
DE AltName: Full=Phospholipase C-delta-3-A;
DE Short=PLC-delta-3-A;
GN Name=plcd3a; ORFNames=zgc:158396;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP GENE DUPLICATION.
RX PubMed=18722520; DOI=10.1016/j.ygeno.2008.07.012;
RA Kim M.S., Seo J.S., Ahn S.J., Kim N.Y., Je J.E., Sung J.H., Lee H.H.,
RA Chung J.K.;
RT "Duplication of phospholipase C-delta gene family in fish genomes.";
RL Genomics 92:366-371(2008).
CC -!- FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2)
CC to generate 2 second messenger molecules diacylglycerol (DAG) and
CC inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of
CC protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular
CC stores (By similarity). {ECO:0000250|UniProtKB:Q8N3E9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000250|UniProtKB:Q8N3E9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:Q8N3E9};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 5 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound
CC to the C2 domain. {ECO:0000250|UniProtKB:Q8N3E9};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8N3E9};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N3E9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8N3E9}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q8N3E9}. Note=Localizes at the cleavage furrow
CC during cytokinesis. {ECO:0000250|UniProtKB:Q8N3E9}.
CC -!- DOMAIN: The C2 domain is a Ca(2+)-dependent membrane-targeting module.
CC {ECO:0000250|UniProtKB:Q8N3E9}.
CC -!- DOMAIN: The PH domain mediates interaction with the surface membrane by
CC binding to PIP2. {ECO:0000250|UniProtKB:Q8N3E9}.
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 EMBL; BC139849; AAI39850.1; -; mRNA.
DR RefSeq; NP_001092893.1; NM_001099423.1.
DR AlphaFoldDB; A5D6R3; -.
DR SMR; A5D6R3; -.
DR STRING; 7955.ENSDARP00000093449; -.
DR PaxDb; A5D6R3; -.
DR Ensembl; ENSDART00000102674; ENSDARP00000093449; ENSDARG00000052957.
DR GeneID; 569040; -.
DR KEGG; dre:569040; -.
DR CTD; 569040; -.
DR ZFIN; ZDB-GENE-070620-1; plcd3a.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000156993; -.
DR HOGENOM; CLU_002738_0_2_1; -.
DR InParanoid; A5D6R3; -.
DR OMA; HTWIHSY; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; A5D6R3; -.
DR TreeFam; TF313216; -.
DR Reactome; R-DRE-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR PRO; PR:A5D6R3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000052957; Expressed in muscle tissue and 19 other tissues.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR CDD; cd16218; EFh_PI-PLCdelta3; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR039504; PLC-delta3_EF-hand.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF14788; EF-hand_10; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transducer.
FT CHAIN 1..784
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase delta-3-A"
FT /id="PRO_0000306823"
FT DOMAIN 38..149
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 159..194
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 195..230
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 227..262
FT /note="EF-hand 3"
FT /evidence="ECO:0000305"
FT DOMAIN 313..458
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 506..621
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 621..750
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..78
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT REGION 473..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 534
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 561
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 664
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 666
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 690
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
FT BINDING 721
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000250"
SQ SEQUENCE 784 AA; 89381 MW; 4078823F379343C6 CRC64;
MLGRKKNPET VQTESKSVES KTHDPLRRLG VLDDEDVLLM LQGSKMMKVR SQRWRKDRRL
KLLEDCVTVW CESSKTSRKS NRQQTFSVTE VECVREGCQS ECLRRMTDLV PEKNCFTVVF
RGGRKSLDLC CHTQEEAERW VRGIRTLKDR VSNMSQKEKL DHWIRGYLRR ADQNQDGKMS
YDEVKHLLQL INIDLNEQYA RTLFKKCDRS CDGRLDHVEI EEFCREMMRR PELDAVFRHY
SGNGCVLTTL ELRDFLGDQG EDASLVHAKS LIQTFELNDW AQKNLFMTQN GFTMYMLSKE
NDVFNPDHTH VYQDMSKPLA HYYISSSHNT YLTKDQVTSA SSTEPYIRAL NQGCRCVELD
CWDGDKGEPI IYHGHTLTSK VLFKEVIETI AQYAFKASPY PLILSLENHC SVEQQAIMAQ
QLQSILGKKL LAKPLSDLPL KQLPSPEELK GRILLKGKKL NGLLGKTESW TSFTNSSDEE
SVAGGNKKES KKDLARSAST KLSPELSDLV VYCQSVPFSG FETANQRPPS VITSFSENEA
LKLIKDSGKL FVRNNSRQLS RIYPSAQRLQ SSNFDPQDMW NAGCQMVALN FQTPGEQMDL
NQGRFLPNGR CGYVLKPEFL CDPKSDFDPE NTGGGPGHIP TQLTIRVISA QQLPKINTDK
PNSIVDPQVW VEIHGVSIDK ARAKTQRIDN NGFNPRWDCT VSFQLQLPEL ALVRFMVEDH
DHKSKNDFIG QFTLPFTSLR TGYRHVHLLK ADGSTLSPAT LFIHVKVVRR GVHIKTVSER
IGKA
