ID A0A1U7Q5X1_MESAU Unreviewed; 2286 AA.
AC A0A1U7Q5X1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN Name=Plce1 {ECO:0000313|RefSeq:XP_005063688.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005063688.1};
RN [1] {ECO:0000313|RefSeq:XP_005063688.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
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DR RefSeq; XP_005063688.1; XM_005063631.3.
DR STRING; 10036.ENSMAUP00000003069; -.
DR GeneID; 101832834; -.
DR KEGG; maua:101832834; -.
DR CTD; 51196; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16203; EFh_PI-PLCepsilon; 1.
DR CDD; cd08596; PI-PLCc_epsilon; 1.
DR CDD; cd17229; RA1_PLC-epsilon; 1.
DR CDD; cd01780; RA2_PLC-epsilon; 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; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 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; IPR046973; PLC-epsilon1_cat.
DR InterPro; IPR028398; PLC-epsilon1_RA2.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR046974; PLC_epsilon1_EF.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
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; PF09279; EF-hand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00147; RasGEF; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR SUPFAM; SSF48366; Ras GEF; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
PE 4: Predicted;
KW Guanine-nucleotide releasing factor {ECO:0000256|PROSITE-ProRule:PRU00168};
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:UP000189706};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 531..784
FT /note="Ras-GEF"
FT /evidence="ECO:0000259|PROSITE:PS50009"
FT DOMAIN 1739..1829
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1835..1960
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 2119..2222
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT REGION 45..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2243..2265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2286 AA; 255389 MW; 5B0AF53EE438B4F6 CRC64;
MTSEEMAASI LIPVTQRKVA SAQSAVAEDK SENVLDAHIP KTCAGRHSGQ IPHTISQWNK
PEAGPSRSDL SQLFPIASGE VMSDENHNEK CWEKNLPDSV KNHAINCNSL LQSHQSDRPQ
SQLCVACDSV SGEDLCLQTG ISSPLERKVF PGIQLEMDDS PMNVSPLGNE PGLTGTRGPH
PDSNMAVFHF RYEADRTISD AFHTLSEKLI LDDCANCVTL PGGQQKKTCM AYTCKLVELT
KTCGRKNGQL QCEPCSSLGD EHLCFESSCQ QADDVLCSSR MFFREGFAHN PPAKTFLSPL
EDFSDNCEDG DEFFKSKKER STLLVRRFCK NDREVKKSVY TGTRAIMRTL PSGHIGPAAW
KHVEQRRARL IGPCGDVMEP LSAIDVRPRG TQHLTEAQWC LIYSAVRRGE ETEDTIGSLL
HCSRQLPTSE TACGRIRDGP CLKQCVRDTE CEYRATLQRT SIAQYITGSL LEATTSLGAR
SSLLSNFGGS TGRIMLKERQ LGTSMANSNT VPSSSAGISK ELIDLQPLIQ FPEEVASILT
EQEQNIYRKV LPMDYLCFLT RDLSSPECQS SLPHLKASIS ASILTSQNGE HNALEDLVMR
FNEVSSWVTW LILTAGSMEE KREVFSYLVH VAKCCWNMGN YNAVMEFLAG LRSRKVLKMW
QFMDQSDIET MRSLKDAMAQ HESSLEYKKV VTRALHIPGC KVVPFCGVFL KELCEVLDGA
SGLLKLCPRY SSQEAALEFV ADYSGQDNFL QRVGQNGLKN TEKESTVNSI FQIIRSCSRS
LEMEEEDSSS EGAGSRKNSL KDKTRWQLII GDFLDSENDI FEKSKECDLH GSEESQKAFD
HGTELIPWYV LSIQADVHQF LLQGATAIHY DQDTHLSARC FLQLQPDNST LTWMKPPTSS
PAGARPKFGV LSNMSEPGKF PSVGSPGLSG LAEGILDLFS VKAVYMGHPG IDIHTVCVQN
KLSSLLLSET GVTLLYGLQT TDNRLLHFVA PKHTAKMIFS GLLELTTAVR KIRKFPDQRQ
QWLRKQYVSL YQEDGRYEGP TLAHAVELFG GRRWSARNVS PGMSTKNAEK SSIQRNNTLG
ISTTKKKKKM LMRGESGEAT DDETATRKAK MCRECRSRSG SDPQDANEQE ESEANVITNP
PNPLHSRRAH SLTTAGSSNL TTGMSSPISA WSSSSWHGRI KGGMKGFQSF MVSDSNMSFI
EFVELFKSFS VRSRKDLKDI FDIYSVPCNR SASESAPLYT NLTIEENASD FQPDLDLLTR
NVSDLGLFIK SKQQLSDNQR QISDAIAAAS IVTNGTGIES TSLGIFGVGI LQLNDFLVNC
QGEHCTYDEI LSIIQKFEPS VSMCHQGLMS FEGFARFLMD KDNFASKNDE SQENKRELQL
PLSYYYIESS HNTYLTGHQL KGESSVELYS QVLLQGCRSI ELDCWDGDDG MPIIYHGHTL
TTKIPFKEVV EAIDRSAFIT SDLPIIISIE NHCSLPQQRK MAEIFKSVFG EKLVAKFLFE
TDFSDDPMLP SPDQLRKKVL LKNKKLKAHQ TPVDILKQKA HQLASMQAQA FTGGSANPPP
ASNEEEEDEE DEYDYDYESL SDDNILEDKP ENKSCADKLQ FEYNEEIPKR IKKADNSSCN
KGKVYDMELG EEFYLPQNKK ESRQIAPELS DLIIYCQAVK FPGLSTLNSS GSSRGKERKS
RKSIFGNNPG RMSPGETASF NRTSGKSSNE GIRQTWEESC SPLSPSTSLS AIIRTPKCYH
ISSLNENAAK RLCRRYSQKL IQHTACQLLR TYPAATRIDS SNPNPLMFWL HGIQLVALNY
QTDDLPLHLN AAMFEANGGC GYVLKPPVLW DKSCPMYQKF SPLERDLDSM DPAIYSLTII
SGQNVCPSNS TGSPCIEVDV LGMPLDSCHF RTKPIHRNPL NPMWNEQFLF RVHFEDLVFL
RFAVVENNSS AITAQRIIPL KALKRGYRHL QLRNLHNEIL EISSLFINSR RMEENPSGST
MPASLMFNTE ERKCSQTHRV TVHGVPGPEP FAVFTINGGT KAKQLLQQVL VIDPDTKLSA
TDYFLMEEKY FISKEKNECK KQPFQRAVGP EEDIVQILNS WFPEEGYVGR IVLKPQQETL
EEKSIVQDDK EVILSSEEES FFVQVHDVSP EQPRTVIKAP RVSTAQDVIQ QTLCKAKYSY
SILNNPNPGD YVLLEEVMKE APSKKSSTPK SSQRILLDQE CVFQAQSKWK GAGKFILKLK
EQVQASREDK RKGISFASEL KKLTKSTKQP RGLASPPQLV APESVQIKEE KPVGALSSSD
TVAYQQ
//
