ID E3M251_CAERE Unreviewed; 825 AA.
AC E3M251;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=Cre-plc-1 {ECO:0000313|EMBL:EFO89618.1};
GN ORFNames=CRE_07427 {ECO:0000313|EMBL:EFO89618.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU361133};
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DR EMBL; DS268422; EFO89618.1; -; Genomic_DNA.
DR RefSeq; XP_003109476.1; XM_003109428.1.
DR AlphaFoldDB; E3M251; -.
DR STRING; 31234.E3M251; -.
DR EnsemblMetazoa; CRE07427.1; CRE07427.1; WBGene00079584.
DR eggNOG; KOG0169; Eukaryota.
DR HOGENOM; CLU_404533_0_0_1; -.
DR InParanoid; E3M251; -.
DR OMA; TINICIC; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
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; cd00275; C2_PLC_like; 1.
DR CDD; cd01780; RA2_PLC-epsilon; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR028398; PLC-epsilon1_RA2.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10336:SF6; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE EPSILON-1; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00788; RA; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00314; RA; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50200; RA; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 210..316
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 336..462
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 492..587
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 666..775
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 92378 MW; CEFDD7C68A19FB0F CRC64;
MIDRGAIQRG ETQLTLHRKQ SKNSYESSTV DEVEDDDLDE FLDDEENEED DQEEVPVRSE
KEDSPKTSKR AEKSARNIKQ QDSLCSDHSV EQAKPSTSKS TSKANEGKTE DEVLYAQLAQ
NAIRNQQPRK NNTGVQIAPE LSDIVIYMQA TKFKGFPPVD GIQSPRITEE QPASASLSFS
SRARTPSNLL NTPAPPRRQR SSTQLSQELA VEFLPSGRPN ATATCYQVTS LNENAAKKLM
KRHPAKCISY TRDHLIRTYP SAKHYDSSNF NPINCWAHGM QMVALNFQTP DVIMAVNQAM
FEQSGNCGYQ LKPRCLWDES HLLYNKFLPL SKDIAGHSAL LLNLTVSVST RNIKNLCFQI
ISGQHVYPNT HYASLYVEIE VIGIHNDCVR EKSKVVQRNS VNPIWNHTTQ LRIACVDLAF
LRIAVCDSGQ NGRVVAHRVV PVKCIRPGFR HLPLRTPTNL PIDNAMVFLR YLLKAREIIT
PHLSPTPILK KQIFVLRITG AFADETAITV HSESGSTVKT VMQQALLNAG KNADQVEEYL
LFEESLPAPS GEDPIEPRVL PLNVPIMDAV ACWNGSMRRF VLRKKGSDPS SRAWIASIIK
SGTSGSSTSV SPSPLTKDGH VKSASSNQLH GRSLDTDAFG EHLEVTEGKW LNPRARSMGD
TFLVCVHNVS EDQPYAILRA GINSTAADII RQVFVKARRP NVDDAEYVLI EETGDENKKD
QGQSKLQAFS LARKRSNDLT PKYPTSRVLG PNENVWKAQS RWKTTGRFVL ENRKDTVHAT
LEKVRSFISK LEEFLDMAKL LREGIPKKEE PYYMIYYAGL PGEDI
//
