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   27-MAR-2024, entry version 207.
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;
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; 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; 104.
DR   IntAct; P32383; 6.
DR   MINT; P32383; -.
DR   STRING; 4932.YPL268W; -.
DR   SwissLipids; SLP:000000122; -.
DR   iPTMnet; P32383; -.
DR   MaxQB; P32383; -.
DR   PaxDb; 4932-YPL268W; -.
DR   PeptideAtlas; P32383; -.
DR   EnsemblFungi; YPL268W_mRNA; YPL268W; YPL268W.
DR   GeneID; 855860; -.
DR   KEGG; sce:YPL268W; -.
DR   AGR; SGD:S000006189; -.
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; HWQREMS; -.
DR   OrthoDB; 2900494at2759; -.
DR   BioCyc; YEAST:YPL268W-MONOMER; -.
DR   BRENDA; 3.1.4.11; 984.
DR   Reactome; R-SCE-112043; PLC beta mediated events.
DR   Reactome; R-SCE-114604; GPVI-mediated activation cascade.
DR   Reactome; R-SCE-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-SCE-202433; Generation of second messenger molecules.
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   Reactome; R-SCE-5607764; CLEC7A (Dectin-1) signaling.
DR   BioGRID-ORCS; 855860; 0 hits in 10 CRISPR screens.
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:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   GO; GO:0001402; P:signal transduction involved in filamentous growth; IGI:SGD.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16207; EFh_ScPlc1p_like; 1.
DR   CDD; cd13360; PH_PLC_fungal; 1.
DR   CDD; cd08598; PI-PLC1c_yeast; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 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
//