PLC1_YEAST
ID PLC1_YEAST Reviewed; 869 AA.
AC P32383; D6W3A2;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1;
DE EC=3.1.4.11 {ECO:0000269|PubMed:8395015};
DE AltName: Full=Phosphoinositide phospholipase C;
DE AltName: Full=Phospholipase C-1;
DE Short=PLC-1;
GN Name=PLC1; OrderedLocusNames=YPL268W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8383328; DOI=10.1073/pnas.90.5.1804;
RA Yoko-O T., Matsui Y., Yagisawa H., Nojima H., Uno I., Toh-e A.;
RT "The putative phosphoinositide-specific phospholipase C gene, PLC1, of the
RT yeast Saccharomyces cerevisiae is important for cell growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1804-1808(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RX PubMed=8395015; DOI=10.1128/mcb.13.9.5861-5876.1993;
RA Flick J.S., Thorner J.W.;
RT "Genetic and biochemical characterization of a phosphatidylinositol-
RT specific phospholipase C in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:5861-5876(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8391635; DOI=10.1128/mcb.13.7.4351-4364.1993;
RA Payne W.E., Fitzgerald-Hayes M.;
RT "A mutation in PLC1, a candidate phosphoinositide-specific phospholipase C
RT gene from Saccharomyces cerevisiae, causes aberrant mitotic chromosome
RT segregation.";
RL Mol. Cell. Biol. 13:4351-4364(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP FUNCTION, AND INTERACTION WITH SGD1.
RX PubMed=12073033; DOI=10.1007/s00438-002-0647-8;
RA Lin H., Nguyen P.H., Vancura A.;
RT "Phospholipase C interacts with Sgd1p and is required for expression of
RT GPD1 and osmoresistance in Saccharomyces cerevisiae.";
RL Mol. Genet. Genomics 267:313-320(2002).
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 Required for cell growth, osmoresistance and expression of GPD1.
CC {ECO:0000269|PubMed:12073033, ECO:0000269|PubMed:8395015}.
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:0000269|PubMed:8395015};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000269|PubMed:8395015};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:8395015};
CC -!- SUBUNIT: Interacts with SGD1. {ECO:0000269|PubMed:12073033}.
CC -!- INTERACTION:
CC P32383; Q06132: SGD1; NbExp=3; IntAct=EBI-13485, EBI-34377;
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DR EMBL; D12738; BAA02230.1; -; Genomic_DNA.
DR EMBL; L13036; AAA99927.1; -; Genomic_DNA.
DR EMBL; S63468; AAB27349.2; -; Genomic_DNA.
DR EMBL; Z73624; CAA98004.1; -; Genomic_DNA.
DR EMBL; Z73623; CAA98003.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11168.1; -; Genomic_DNA.
DR PIR; A47257; A47257.
DR RefSeq; NP_015055.1; NM_001184082.1.
DR AlphaFoldDB; P32383; -.
DR SMR; P32383; -.
DR BioGRID; 35945; 102.
DR IntAct; P32383; 6.
DR MINT; P32383; -.
DR STRING; 4932.YPL268W; -.
DR SwissLipids; SLP:000000122; -.
DR iPTMnet; P32383; -.
DR MaxQB; P32383; -.
DR PaxDb; P32383; -.
DR PRIDE; P32383; -.
DR EnsemblFungi; YPL268W_mRNA; YPL268W; YPL268W.
DR GeneID; 855860; -.
DR KEGG; sce:YPL268W; -.
DR SGD; S000006189; PLC1.
DR VEuPathDB; FungiDB:YPL268W; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000169016; -.
DR HOGENOM; CLU_002738_1_2_1; -.
DR InParanoid; P32383; -.
DR OMA; VRWTVWN; -.
DR BioCyc; YEAST:YPL268W-MON; -.
DR BRENDA; 3.1.4.11; 984.
DR Reactome; R-SCE-112043; PLC beta mediated events.
DR Reactome; R-SCE-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-SCE-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-SCE-416476; G alpha (q) signalling events.
DR Reactome; R-SCE-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR PRO; PR:P32383; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32383; protein.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IPI:SGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:SGD.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IMP:SGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:SGD.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:SGD.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IGI:SGD.
DR CDD; cd13360; PH_PLC_fungal; 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; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR037755; Plc1_PH.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR Pfam; PF09279; EF-hand_like; 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 1: Evidence at protein level;
KW Calcium; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Reference proteome; Transducer.
FT CHAIN 1..869
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase 1"
FT /id="PRO_0000088514"
FT DOMAIN 269..304
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 382..520
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 590..709
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 713..862
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 546..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 614
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 643
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 159
FT /note="T -> M (in Ref. 2; AAA99927)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="A -> T (in Ref. 2; AAA99927)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="A -> V (in Ref. 2; AAA99927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 869 AA; 100548 MW; 13EE751259405E90 CRC64;
MTESAIDDQR FNLTKELQRH SCRDQGKITQ KDDALDFISY SSFQSSFNTD QKSANNGSTV
RRSIRSIFRR AAELPRVHMG PLTYSHGINE LVNKKLRKDC DLSTLCRVLQ RGIRMIRMTR
RRRKFYEFKL INNNGQIIWK DGSKYLELDS VKDIRIGDTA STYQEEVDPK RLRSDSKLWI
AIIYKVSNKL KALHVVALNE LDFNTFLSCI CGLVKLRREL MESILLPDNS QFARIHWQIT
VSEKEEDEKK DTLSFADVKK LCDKFHIYVS TGQLLEFFQL ADINHNGLLN YFEFEKFIKI
LKNRKEVNMI WSKFTKPPHS HLSFENFFQF LITEQHEQVD RQTAWSYFIK YREPTQLTMG
QDGFTKFLKE QPYLVEVKEE LYSKPLNHYF IASSHNTYLL GKQIAETPSV EGYIQVLQQG
CRCVEIDIWD GENGPVVCHG FLTSAIPLKT VIRVIKKYAF ITSPYPLIIS LEINCNKDNQ
KLASLIMREV LAEQLYFVGT RTDKLPSPRE LKHKILLKSK KTSEATRGLS VNEPFPSSFS
SSYESANEQE LRMKDDSTNS SSATNSSSMQ RIKRIGLKKH ADIINDVSNI SGIHGIKFRN
FSLPESKTIA HCFSLNERKV EYMIKDKHLK LSLDKHNRRY LMRVYPHVLR YKSSNFNPIP
FWKAGVQMVA TNWQTNDIGQ QLNLAMFQIL DHQPDGSFKS GYVLKPKKLL PVVTKAKMIP
LIYEHFENGS DPVTVKIRIL STQLLPRLND TSPSRNNTNS FVKVEFHTDD EPTMPISIDK
GTRISATEAS TKSSQGNGFN PIWDAEVSIT LKDTDLTFIK FMVISEETQI ASVCLKLNYL
RMGYRHIPLF NMEGEQYIFC TLFIHTQIL
