ID   PLC1_SCHPO              Reviewed;         899 AA.
AC   P40977;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 209.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1;
DE            EC=3.1.4.11;
DE   AltName: Full=Phospholipase C-1;
DE            Short=PLC-1;
GN   Name=plc1; ORFNames=SPAC22F8.11;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7732727; DOI=10.1002/yea.320110209;
RA   Andoh T., Yoko-O T., Matsui Y., Toh-e A.;
RT   "Molecular cloning of the plc1+ gene of Schizosaccharomyces pombe, which
RT   encodes a putative phosphoinositide-specific phospholipase C.";
RL   Yeast 11:179-185(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8590474; DOI=10.1007/bf00315789;
RA   Fankhauser H., Schweingruber A.-M., Edenharter E., Schweingruber M.E.;
RT   "Growth of a mutant defective in a putative phosphoinositide-specific
RT   phospholipase C of Schizosaccharomyces pombe is restored by low
RT   concentrations of phosphate and inositol.";
RL   Curr. Genet. 28:199-203(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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;
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DR   EMBL; D38309; BAA07426.1; -; Genomic_DNA.
DR   EMBL; X83615; CAA58591.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB52721.1; -; Genomic_DNA.
DR   PIR; S55075; S55075.
DR   PIR; S57259; S51092.
DR   RefSeq; NP_594734.1; NM_001020162.3.
DR   AlphaFoldDB; P40977; -.
DR   SMR; P40977; -.
DR   BioGRID; 277944; 13.
DR   FunCoup; P40977; 143.
DR   IntAct; P40977; 1.
DR   STRING; 284812.P40977; -.
DR   iPTMnet; P40977; -.
DR   PaxDb; 284812-P40977; -.
DR   GeneID; 2541439; -.
DR   KEGG; spo:2541439; -.
DR   PomBase; SPAC22F8.11; plc1.
DR   VEuPathDB; FungiDB:SPAC22F8.11; -.
DR   eggNOG; KOG0169; Eukaryota.
DR   HOGENOM; CLU_002738_1_0_1; -.
DR   InParanoid; P40977; -.
DR   OMA; HWQREMS; -.
DR   PhylomeDB; P40977; -.
DR   Reactome; R-SPO-114604; GPVI-mediated activation cascade.
DR   Reactome; R-SPO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-SPO-202433; Generation of second messenger molecules.
DR   Reactome; R-SPO-5607764; CLEC7A (Dectin-1) signaling.
DR   PRO; PR:P40977; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol-4,5-bisphosphate phospholipase C activity; IGI:PomBase.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; ISO:PomBase.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
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   FunFam; 2.60.40.150:FF:000404; Phosphoinositide phospholipase C; 1.
DR   FunFam; 3.20.20.190:FF:000039; Phosphoinositide phospholipase C; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
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; 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 BETA-4; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF13499; EF-hand_7; 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; SM00054; EFh; 2.
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   Phosphoprotein; Reference proteome; Transducer.
FT   CHAIN           1..899
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase 1"
FT                   /id="PRO_0000088513"
FT   DOMAIN          330..365
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          441..584
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   DOMAIN          638..753
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT   DOMAIN          750..879
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   ACT_SITE        456
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        500
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   BINDING         343
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         345
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         347
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         349
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         354
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         582
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         584
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         666
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         693
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        480
FT                   /note="R -> A (in Ref. 2; CAA58591)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   899 AA;  102673 MW;  C7CC935DAB820245 CRC64;
     MNCEMVTSPE SVNLGDSNRA VSPFCLPDCS ENAVAQTRSK TLDNAALDLP YVGNRKKSEQ
     DFFKMLSSRD RDAHSTLRKR SNSLSSFLST KSTSASENKF HGGLNWLSLK LNLLLRLQGR
     MNSARTNTSM NPYSCDSNEN LSTLSSVNQN FNSRQLLATI VPESIQNGCS LLRITKKKVR
     QRKVSLDPIS GYLMLDKNTG KAYKKLCVDD IKEIRQGRDA RNYREQYKIS SENEKRWFTI
     IYCADNKLKA MHMISPTLDA HNQWIMALEG LKTYRLNEFI IGLNLVCHQG EKMIDYSENL
     NPWEKLEKEQ SAQLDLGDVH RMCQMLHLNA SMEFLEETFQ KADADHSGKL SFEEFQHFVS
     LLKTRSEIVD IFKEYTSGSD KMSLEQFRHF LSTSQKARLD SDSIRTLYVS FCSNDDSKMG
     LIEFTSFLLS PHNSPVVPVI QDMSRPLNEY LISSSHNTYL LGKQFGGESS IEGYIRSLQR
     GCKCIEIDCW DGPNGPVVCH GHTFTSMIKF NDVIDAIRKY AFVVSPYPLF ISLEIHCCPD
     QQRQMVSYMK QAFGDTLVMK PVTANESVLP SPEDLLNKIL LKVKCSATPL HQFSTDILKV
     GITDSSTDTT ESSELENSEL TGLRKGKRRM KNIIVQELQQ LAPYARSLKF RNFSLPESKT
     YSHIFSFSER TIKKHGKAMV PRLSKHNLRY LCRVYPGPLR VGSTNFNPQV YWRLGVQMVA
     LNWQTYDTGL QINDALFIAD PPTGYLLKPP CQRIIGTTVG EEGLPRKIKL TIDVISGQQL
     RRARELSNSE TLSPYVEIQV HSMEESPFRW CSKVVHENGF RPFWGETMVY ESIISDDFYS
     MIRFLVHHRG SNGNDSIFAN FTCPIDRLQQ GYRHIRLLDM QGENLLFSSL FLKIKKEDI
//