PLC_DICDI
ID PLC_DICDI Reviewed; 801 AA.
AC Q02158; Q54CR5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase C;
DE Short=PLC;
GN Name=plc; Synonyms=pipA; ORFNames=DDB_G0292736;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NC-4;
RX PubMed=1326523; DOI=10.1016/s0021-9258(19)36974-1;
RA Drayer A.L., van Haastert P.J.;
RT "Molecular cloning and expression of a phosphoinositide-specific
RT phospholipase C of Dictyostelium discoideum.";
RL J. Biol. Chem. 267:18387-18392(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15075287; DOI=10.1128/ec.3.2.564-566.2004;
RA Escalante R., Iranfar N., Sastre L., Loomis W.F.;
RT "Identification of genes dependent on the MADS box transcription factor
RT SrfA in Dictyostelium discoideum development.";
RL Eukaryot. Cell 3:564-566(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes.
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 -!- DEVELOPMENTAL STAGE: Expressed at all stages; increase in expression in
CC the culminating fruiting body and during starvation.
CC -!- CAUTION: It is uncertain whether Met-1 is the initiator. {ECO:0000305}.
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; M95783; AAA33235.1; -; mRNA.
DR EMBL; AY392433; AAQ98875.1; -; Genomic_DNA.
DR EMBL; AAFI02000196; EAL61042.1; -; Genomic_DNA.
DR PIR; A44165; A44165.
DR RefSeq; XP_629476.1; XM_629474.1.
DR AlphaFoldDB; Q02158; -.
DR SMR; Q02158; -.
DR STRING; 44689.DDB0201656; -.
DR PaxDb; Q02158; -.
DR EnsemblProtists; EAL61042; EAL61042; DDB_G0292736.
DR GeneID; 8628866; -.
DR KEGG; ddi:DDB_G0292736; -.
DR dictyBase; DDB_G0292736; plc.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_002738_0_2_1; -.
DR InParanoid; Q02158; -.
DR OMA; HTWIHSY; -.
DR PhylomeDB; Q02158; -.
DR Reactome; R-DDI-112043; PLC beta mediated events.
DR Reactome; R-DDI-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-DDI-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-DDI-416476; G alpha (q) signalling events.
DR Reactome; R-DDI-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR PRO; PR:Q02158; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0016020; C:membrane; IDA:dictyBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:dictyBase.
DR GO; GO:0045184; P:establishment of protein localization; IMP:dictyBase.
DR GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IMP:dictyBase.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR GO; GO:0050922; P:negative regulation of chemotaxis; IMP:dictyBase.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0050764; P:regulation of phagocytosis; IMP:dictyBase.
DR GO; GO:0048837; P:sorocarp sorus development; IMP:dictyBase.
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; IPR001192; PI-PLC_fam.
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; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 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; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Calcium; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..801
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase"
FT /id="PRO_0000088509"
FT DOMAIN 206..241
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 322..464
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 542..652
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 656..781
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 471..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 501
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 566
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 593
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 531
FT /note="Phosphothreonine; by PKA and PKG"
FT /evidence="ECO:0000255"
SQ SEQUENCE 801 AA; 91280 MW; DB4FA8C829812DD9 CRC64;
MDTLTNSQDY SNVDLSLESL AEELYNIQSF NKDVILDSFD IDDYDHTQLD TTIDFNKFKI
GLTILKISSK GKPQKKKLIF DLARNQIVCG KKKKVNFSEI DEIRVGHKTN IFNQFKSSKN
LKEDIESIQQ SFSILFSGNL RKTMDFVCSD IPERRQIVSA LYHVVQESKS VNNEYNFVKR
EWDRVGKDSI DFSTLKKILA RLNFTTSDAV LHNLMKFSDS NSDYHLDFSE FSNLLKLLRS
HPEMKPVFYK YNGGNGEWVP IQGMIDFFRI EQSEVWTVEQ CRDLIKKYHH ERLDCISFEN
FEEFICGEAN LAQYPHTSTV YQDTSKPLSY YFINSSHNTY LSGHQLKGLS TSEMYTNTLR
QGCKCVELDV WDGNDGDPII FHGNTLTSQI KFSHVCETIK ARGFETSPYP VILSLEVHCS
VPQQIMMANH MKEIFGEMLP TPLPEGTKEL PTLDSLKYKI LLKGHTSHTH VSAVGNSSAS
SSQSNIQTDD NDDDGAVDLT EYDEVDDRSA SSSSSSFSLS FGSSGKKKKI TKIKIAPEFE
ELIYLVSHGF KSGNTTKEIP SYKIHSLVEE KVKQLVQSEP REVVEASQNH LLRVYPRGTR
FDSSNFDPMP GWSIGCQLAA LNQQTSSEPM WINDGMFSDN GGCGYVLKPP CLLPGECETY
DPTSPERIKS SKYSRLIVNV ISARQLPKYT KSTKGEVIDP YVTLSIVGTH FDQKVEKTKV
IDNNGFNPHW GEEFEFPLYN SQLSMLLIRV DDKDKVGHNR IGHHCIRVEN IRPGYRILKL
KNNFNRTIPL ANLLCKFTFV E
