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1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (EC 3.1.4.11) (PLC-154) (Phosphoinositide phospholipase C-beta-1) (Phospholipase C-I) (PLC-I) (Phospholipase C-beta-1) (PLC-beta-1)

 PLCB1_RAT               Reviewed;        1216 AA.
P10687;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
18-JUL-2018, entry version 168.
RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;
EC=3.1.4.11;
AltName: Full=PLC-154;
AltName: Full=Phosphoinositide phospholipase C-beta-1;
AltName: Full=Phospholipase C-I;
Short=PLC-I;
AltName: Full=Phospholipase C-beta-1;
Short=PLC-beta-1;
Name=Plcb1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3390863; DOI=10.1016/0092-8674(88)90548-X;
Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.;
"Cloning and sequence of multiple forms of phospholipase C.";
Cell 54:161-169(1988).
[2]
CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=8454637;
Jhon D.-Y., Lee H.-H., Park D., Lee C.-W., Lee K.-H., Yoo O.J.,
Rhee S.G.;
"Cloning, sequencing, purification, and Gq-dependent activation of
phospholipase C-beta 3.";
J. Biol. Chem. 268:6654-6661(1993).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-1197; SER-1199
AND SER-1200, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: The production of the second messenger molecules
diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is
mediated by activated phosphatidylinositol-specific phospholipase
C enzymes.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
diacylglycerol. {ECO:0000269|PubMed:8454637}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
-!- SUBUNIT: Interacts with DGKQ. {ECO:0000250}.
-!- INTERACTION:
Q8TEW0:PARD3 (xeno); NbExp=3; IntAct=EBI-7551252, EBI-81968;
Q9NPB6:PARD6A (xeno); NbExp=2; IntAct=EBI-7551252, EBI-81876;
-!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}. Cytoplasm
{ECO:0000269|PubMed:8454637}. Note=Colocalizes with the adrenergic
receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac
myocytes. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highest expression in brain. Also expressed in
parotid gland, liver, uterus, lung, heart, adrenal gland and
ovary. Not detected in spleen, pancreas, intestine, thymus or
kidney. {ECO:0000269|PubMed:8454637}.
-!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-1 is
mediated by two G-protein alpha subunits, alpha-Q and alpha-11.
-----------------------------------------------------------------------
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EMBL; M20636; AAA41885.1; -; mRNA.
PIR; A28821; A28821.
RefSeq; NP_001071109.1; NM_001077641.1.
RefSeq; XP_017446955.1; XM_017591466.1.
UniGene; Rn.45523; -.
ProteinModelPortal; P10687; -.
SMR; P10687; -.
BioGrid; 246789; 162.
CORUM; P10687; -.
IntAct; P10687; 2.
MINT; P10687; -.
STRING; 10116.ENSRNOP00000006389; -.
BindingDB; P10687; -.
SwissLipids; SLP:000000946; -.
iPTMnet; P10687; -.
PhosphoSitePlus; P10687; -.
SwissPalm; P10687; -.
PaxDb; P10687; -.
PRIDE; P10687; -.
GeneID; 24654; -.
KEGG; rno:24654; -.
UCSC; RGD:3344; rat.
CTD; 23236; -.
RGD; 3344; Plcb1.
eggNOG; KOG0169; Eukaryota.
eggNOG; ENOG410XPSW; LUCA.
HOGENOM; HOG000232046; -.
HOVERGEN; HBG053609; -.
InParanoid; P10687; -.
KO; K05858; -.
PhylomeDB; P10687; -.
TreeFam; TF313216; -.
BRENDA; 3.1.4.11; 5301.
SABIO-RK; P10687; -.
PRO; PR:P10687; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; ISS:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0060466; P:activation of meiosis involved in egg activation; ISS:BHF-UCL.
GO; GO:1902618; P:cellular response to fluoride; IDA:RGD.
GO; GO:1905631; P:cellular response to glyceraldehyde; IDA:RGD.
GO; GO:1904637; P:cellular response to ionomycin; IDA:RGD.
GO; GO:1904117; P:cellular response to vasopressin; IDA:RGD.
GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL.
GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:RGD.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0007612; P:learning; IEP:RGD.
GO; GO:0007613; P:memory; IEP:RGD.
GO; GO:2000438; P:negative regulation of monocyte extravasation; ISS:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:BHF-UCL.
GO; GO:0031161; P:phosphatidylinositol catabolic process; IDA:RGD.
GO; GO:0046488; P:phosphatidylinositol metabolic process; IEP:RGD.
GO; GO:2000560; P:positive regulation of CD24 biosynthetic process; ISS:BHF-UCL.
GO; GO:0048639; P:positive regulation of developmental growth; ISS:BHF-UCL.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:BHF-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; ISS:BHF-UCL.
GO; GO:0034284; P:response to monosaccharide; IDA:BHF-UCL.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IDA:BHF-UCL.
CDD; cd13361; PH_PLC_beta; 1.
Gene3D; 2.60.40.150; -; 1.
Gene3D; 3.20.20.190; -; 2.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR001192; PI-PLC_fam.
InterPro; IPR016280; PLC-beta.
InterPro; IPR028400; PLC-beta1.
InterPro; IPR014815; PLC-beta_C.
InterPro; IPR009535; PLC-beta_CS.
InterPro; IPR037862; PLC-beta_PH.
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
InterPro; IPR015359; PLC_EF-hand-like.
InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
PANTHER; PTHR10336; PTHR10336; 1.
PANTHER; PTHR10336:SF12; PTHR10336:SF12; 1.
Pfam; PF06631; DUF1154; 1.
Pfam; PF09279; EF-hand_like; 1.
Pfam; PF00388; PI-PLC-X; 1.
Pfam; PF00387; PI-PLC-Y; 1.
Pfam; PF08703; PLC-beta_C; 1.
PIRSF; PIRSF000956; PLC-beta; 1.
PRINTS; PR00390; PHPHLIPASEC.
SMART; SM00239; C2; 1.
SMART; SM00148; PLCXc; 1.
SMART; SM00149; PLCYc; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF51695; SSF51695; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Cytoplasm; Hydrolase; Lipid degradation;
Lipid metabolism; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Transducer.
CHAIN 1 1216 1-phosphatidylinositol 4,5-bisphosphate
phosphodiesterase beta-1.
/FTId=PRO_0000088488.
DOMAIN 316 467 PI-PLC X-box. {ECO:0000255|PROSITE-
ProRule:PRU00270}.
DOMAIN 540 656 PI-PLC Y-box. {ECO:0000255|PROSITE-
ProRule:PRU00271}.
DOMAIN 663 761 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
ACT_SITE 331 331 {ECO:0000255|PROSITE-ProRule:PRU00270}.
ACT_SITE 378 378 {ECO:0000255|PROSITE-ProRule:PRU00270}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1B3}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1B3}.
MOD_RES 509 509 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Z1B3}.
MOD_RES 511 511 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1B3}.
MOD_RES 582 582 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 887 887 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P10894}.
MOD_RES 978 978 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1B3}.
MOD_RES 987 987 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z1B3}.
MOD_RES 1197 1197 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1199 1199 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1200 1200 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
SEQUENCE 1216 AA; 138344 MW; 92F23691781F788E CRC64;
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE
TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV
AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA
DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL
TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS
GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV
ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ
QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK
KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM
SNLVNYIQPV KFESFETSKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK
HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG
NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER
NQPLMLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK
EADPGETSSE APSETRTTPA ENGVNHTATL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL
RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR
QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI
TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP
KLQMELEQEY QDKFKRLPLE ILEFVQEAMK GKVSEDSNHG SAPPSLASDP AKVNLKSPSS
EEVQGENAGR EFDTPL


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