PLC1_SCHPO
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 03-AUG-2022, entry version 192.
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_001020162.2.
DR AlphaFoldDB; P40977; -.
DR SMR; P40977; -.
DR BioGRID; 277944; 12.
DR STRING; 4896.SPAC22F8.11.1; -.
DR iPTMnet; P40977; -.
DR MaxQB; P40977; -.
DR PaxDb; P40977; -.
DR PRIDE; P40977; -.
DR EnsemblFungi; SPAC22F8.11.1; SPAC22F8.11.1:pep; SPAC22F8.11.
DR GeneID; 2541439; -.
DR KEGG; spo:SPAC22F8.11; -.
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; VRWTVWN; -.
DR PhylomeDB; P40977; -.
DR Reactome; R-SPO-112043; PLC beta mediated events.
DR Reactome; R-SPO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-SPO-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-SPO-416476; G alpha (q) signalling events.
DR Reactome; R-SPO-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
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; ISM:PomBase.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISO:PomBase.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0009395; P:phospholipid catabolic process; ISO:PomBase.
DR GO; GO:0019220; P:regulation of phosphate metabolic process; ISO:PomBase.
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; 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; PF13202; EF-hand_5; 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; 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 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
