PLC1_CANAX
ID PLC1_CANAX Reviewed; 1099 AA.
AC O13433;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1;
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase C;
DE AltName: Full=Phospholipase C-1;
DE Short=PLC-1;
GN Name=PLC1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=132A;
RX PubMed=9467900; DOI=10.1099/00221287-144-1-55;
RA Bennett D.E., McCreary C.E., Coleman D.C.;
RT "Genetic characterization of a phospholipase C gene from Candida albicans:
RT presence of homologous sequences in Candida species other than Candida
RT albicans.";
RL Microbiology 144:55-72(1998).
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; Y13975; CAA74308.1; -; Genomic_DNA.
DR PIR; T18257; T18257.
DR AlphaFoldDB; O13433; -.
DR SMR; O13433; -.
DR VEuPathDB; FungiDB:C7_03710C_A; -.
DR VEuPathDB; FungiDB:CAWG_05702; -.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd13360; PH_PLC_fungal; 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; 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; 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; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase; Lipid degradation; Lipid metabolism; Transducer.
FT CHAIN 1..1099
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase 1"
FT /id="PRO_0000088512"
FT DOMAIN 566..726
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 794..912
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 917..1071
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 579
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 642
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 724
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 726
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 823
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 852
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1099 AA; 124592 MW; D54D687D53A2829B CRC64;
MLESLNRRNS IDSNQADNDN DNDNHSNDEL SPSELYYSPS GSPPKSQLLL RKSSSPSSYS
PIKSDLPNIY SHLRSNDSES PPQPSPKQQS SLSSSSSSSS SSNTKSSTTK NIFKKLLRIN
KSSDNIDESR SIVSNNGGSP MSDSTTVTST LSTDTAPKRG KSIQRSQILH HTDSDSLYLE
NQIELRPEIS KSIGNIKIPS IFTNDGMPLL KISHKSKKRI LFWIDPSCFK FSWRMANSTT
TTTSATTSAT TSGLPQGITN TTALSNSAII STPAIATSAI HRLSITNRTT HEFVLDDIKS
IYIQNEGSGY REELNISQKL EKNWITIIYF NHKKNSLKSL HLITDNDHDF KKLISAIYNL
KQLRSQLAKE FLIDLNELDE NYVKMLLNKE LLAGDNGNVD GNEVDIRKSH KHVREFLSFN
DILKYSKRLN INVNTNHLQQ IFDQVLLLSS ATTEKPVSTP LFEKGLNFEQ FKQFVSILKD
RKDLQEIWDS LAQGKEVLQF DEIKNFIINI QKENFSDDDD NSTINLIFQK YCSNDNGWNK
ESLNEYLLSS YSTPYREITQ TQTNYYDYPL NEYFISSSHN TYLTGRQVAG DSSVEGYIRT
LQRGCRCVEI DIWNGDSNTT TTTVIGTKDD DDKNEYEPIV NHGRTFTKPI SFANVIRAIK
KFAFIVSPWP LILSLEIHCS PECQIKVVNI LKDILGENMI IAPIDIDSVI LPSPAELKHK
FIIKVKKTTS FQNLIETENG SFTTSTTTTT TTTTTTTTAT SLSEDNENNK SNSSSTSSFI
IRRRKNKSPK IINELSNLGI YTQGIKFRNF SLPESKTFNH CFSLGEKSIN RMIKDDDKKI
SLDKHNRRYL MRVYPSGTRL KSSNFNPLPY WSHGVQMVAT NWQTYDLGQQ LNEALFENKI
FQGYVLKPSV LRKPTLKSSS SNVDTRTSLT TTNSKTIRFN FEIISGHQLP KFPKDDYKDQ
AINPYISFEI IGAQDVQWDN NDSSPIAPTT SSSPFIRTTK IIRENGFNPN FNTKFSGSII
TTTNDLIFIK FVVYASTSLN YPDYGENFPI AILVTKLNYL KQGYRYIYLN DLLGEQLVYS
SIFIKIEYDE DLLNEFINK
