LOCUS       NP_001071109            1216 aa            linear   ROD 09-APR-2024
DEFINITION  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
            [Rattus norvegicus].
ACCESSION   NP_001071109 XP_017446955 XP_342525
VERSION     NP_001071109.1
DBSOURCE    REFSEQ: accession NM_001077641.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1216)
  AUTHORS   Park,J., Kim,S.H., Kim,Y.J., Kim,H., Oh,Y., Choi,K.Y., Kim,B.C.,
            Lee,K.H. and Song,W.K.
  TITLE     Elevation of phospholipase C-beta1 expression by amyloid-beta
            facilitates calcium overload in neuronal cells
  JOURNAL   Brain Res 1788, 147924 (2022)
   PUBMED   35469845
  REMARK    GeneRIF: Elevation of phospholipase C-beta1 expression by
            amyloid-beta facilitates calcium overload in neuronal cells.
REFERENCE   2  (residues 1 to 1216)
  AUTHORS   Lee,J. and Kwag,J.
  TITLE     Activation of PLCbeta1 enhances endocannabinoid mobilization to
            restore hippocampal spike-timing-dependent potentiation and
            contextual fear memory impaired by Alzheimer's amyloidosis
  JOURNAL   Alzheimers Res Ther 13 (1), 165 (2021)
   PUBMED   34625112
  REMARK    GeneRIF: Activation of PLCbeta1 enhances endocannabinoid
            mobilization to restore hippocampal spike-timing-dependent
            potentiation and contextual fear memory impaired by Alzheimer's
            amyloidosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1216)
  AUTHORS   Garwain,O., Yerramilli,V.S., Romero,K. and Scarlata,S.
  TITLE     The Galphaq/phospholipase Cbeta signaling system represses tau
            aggregation
  JOURNAL   Cell Signal 71, 109620 (2020)
   PUBMED   32247043
  REMARK    GeneRIF: The Galphaq/phospholipase Cbeta signaling system represses
            tau aggregation.
REFERENCE   4  (residues 1 to 1216)
  AUTHORS   Garwain,O., Valla,K. and Scarlata,S.
  TITLE     Phospholipase Cbeta1 regulates proliferation of neuronal cells
  JOURNAL   FASEB J 32 (5), 2891-2898 (2018)
   PUBMED   29401590
  REMARK    GeneRIF: results present a model in which the transient high
            expression of PLCbeta1 that occurs at the onset of differentiation
            arrests cells in the G1 phase through its association with CDK16
            and allows CDK16 to transition to its postmitotic function of
            neurite outgrowth and trafficking of synaptic vesicles.
REFERENCE   5  (residues 1 to 1216)
  AUTHORS   Garwain,O. and Scarlata,S.
  TITLE     Phospholipase Cbeta-TRAX Association Is Required for PC12 Cell
            Differentiation
  JOURNAL   J Biol Chem 291 (44), 22970-22976 (2016)
   PUBMED   27624933
  REMARK    GeneRIF: PLCbeta through its ability to bind TRAX plays a key role
            in switching PC12 cells to their differentiated state.
REFERENCE   6  (residues 1 to 1216)
  AUTHORS   Bahk,Y.Y., Lee,Y.H., Lee,T.G., Seo,J., Ryu,S.H. and Suh,P.G.
  TITLE     Two forms of phospholipase C-beta 1 generated by alternative
            splicing
  JOURNAL   J Biol Chem 269 (11), 8240-8245 (1994)
   PUBMED   7510682
REFERENCE   7  (residues 1 to 1216)
  AUTHORS   Smrcka,A.V. and Sternweis,P.C.
  TITLE     Regulation of purified subtypes of phosphatidylinositol-specific
            phospholipase C beta by G protein alpha and beta gamma subunits
  JOURNAL   J Biol Chem 268 (13), 9667-9674 (1993)
   PUBMED   8387502
REFERENCE   8  (residues 1 to 1216)
  AUTHORS   Mazzoni,M., Bertagnolo,V., Neri,L.M., Carini,C., Marchisio,M.,
            Milani,D., Manzoli,F.A. and Capitani,S.
  TITLE     Discrete subcellular localization of phosphoinositidase C beta,
            gamma and delta in PC12 rat pheochromocytoma cells
  JOURNAL   Biochem Biophys Res Commun 187 (1), 114-120 (1992)
   PUBMED   1325785
REFERENCE   9  (residues 1 to 1216)
  AUTHORS   Berstein,G., Blank,J.L., Jhon,D.Y., Exton,J.H., Rhee,S.G. and
            Ross,E.M.
  TITLE     Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11,
            its physiologic regulator
  JOURNAL   Cell 70 (3), 411-418 (1992)
   PUBMED   1322796
REFERENCE   10 (residues 1 to 1216)
  AUTHORS   Suh,P.G., Ryu,S.H., Moon,K.H., Suh,H.W. and Rhee,S.G.
  TITLE     Cloning and sequence of multiple forms of phospholipase C
  JOURNAL   Cell 54 (2), 161-169 (1988)
   PUBMED   3390863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000003.1.
            
            On or before Jun 4, 2021 this sequence version replaced
            XP_017446955.1, XP_342525.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643298.18853.1,
                                           SRR26643297.13105.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760383, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1216
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q36"
     Protein         1..1216
                     /product="1-phosphatidylinositol 4,5-bisphosphate
                     phosphodiesterase beta-1"
                     /EC_number="3.1.4.11"
                     /note="PLC-I; PLC-154; PLC-beta-1; phosphoinositide
                     phospholipase C; phospholipase C-I; phosphoinositide
                     phospholipase C-beta-1; Phospholipase C-beta1;
                     phospholipase C, beta 1 (phosphoinositide-specific)"
                     /calculated_mol_wt=138214
     Region          22..148
                     /region_name="PH_PLC_beta"
                     /note="Phospholipase C-beta (PLC-beta) pleckstrin homology
                     (PH) domain; cd13361"
                     /db_xref="CDD:270167"
     Site            order(27,29,40,57,122)
                     /site_type="other"
                     /note="Rac1 binding site [polypeptide binding]"
                     /db_xref="CDD:270167"
     Site            order(30,32,37,39,41,56..57)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270167"
     Region          153..303
                     /region_name="EFh_PI-PLCbeta1"
                     /note="EF-hand motif found in phosphoinositide
                     phospholipase C beta 1 (PI-PLC-beta1); cd16208"
                     /db_xref="CDD:320038"
     Region          153..182
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Region          186..215
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Region          224..253
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     Region          270..303
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Region          316..643
                     /region_name="PI-PLCc_beta"
                     /note="Catalytic domain of metazoan
                     phosphoinositide-specific phospholipase C-beta; cd08591"
                     /db_xref="CDD:176533"
     Site            order(331..332,361,363,378,412,479,481,569,596,598)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176533"
     Site            order(331,378)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176533"
     Site            order(332,361,363,412)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:176533"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     Region          469..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10687.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     Site            582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     Region          677..796
                     /region_name="C2_PLC_like"
                     /note="C2 domain present in Phosphoinositide-specific
                     phospholipases C (PLC); cd00275"
                     /db_xref="CDD:175974"
     Site            order(694,720,751,753,755,757)
                     /site_type="other"
                     /note="Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175974"
     Region          834..891
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10687.1)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P10894; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     Region          903..939
                     /region_name="DUF1154"
                     /note="Protein of unknown function (DUF1154); pfam06631"
                     /db_xref="CDD:461969"
     Region          967..989
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10687.1)"
     Site            978
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     Site            987
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     Region          1003..1170
                     /region_name="PLC-beta_C"
                     /note="PLC-beta C terminal; pfam08703"
                     /db_xref="CDD:462571"
     Region          1072..1095
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10687.1)"
     Region          1172..1216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10687.1)"
     Site            1197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     Site            1199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     Site            1200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P10687.1)"
     CDS             1..1216
                     /gene="Plcb1"
                     /gene_synonym="Phosphb; PLC'1; PLCbeta1; RATPHOSPHB"
                     /coded_by="NM_001077641.2:468..4118"
                     /db_xref="GeneID:24654"
                     /db_xref="RGD:3344"
ORIGIN      
        1 magaqpgvha lqlkpvcvsd slkkgtkfvk wdddstivtp iilrtdpqgf ffywtdqnke
       61 telldlslvk darcgkhaka pkdpklrell dvgnighleq rmitvvygpd lvnishlnlv
      121 afqeevakew tnevfslatn llaqnmsrda flekaytklk lqvtpegrip lkniyrlfsa
      181 drkrvetale acslpssrnd sipqedftpd vyrvflnnlc prpeidnifs efgakskpyl
      241 tvdqmmdfin lkqrdprlne ilypplkqeq vqvliekyep nsslakkgqm svdgfmryls
      301 geengvvspe kldlnedmsq plshyfinss hntyltagql agnssvemyr qvllsgcrcv
      361 eldcwkgrta eeepvithgf tmtteisfke vieaiaecaf ktspfpills fenhvdspkq
      421 qakmaeycrl ifgdallmep lekyplesgv plpspmdlmy kilvknkkks hkssegsgkk
      481 klseqasnty sdsssvfeps spgageadte sddddddddc kkssmdegta gseamateem
      541 snlvnyiqpv kfesfetskk rnksfemssf vetkgleqlt kspvefveyn kmqlsriypk
      601 gtrvdssnym pqlfwnagcq mvalnfqtvd lamqinmgmy eyngksgyrl kpefmrrpdk
      661 hfdpftegiv dgivantlsv kiisgqflsd kkvgtyvevd mfglpvdtrr kafktktsqg
      721 navnpvweee pivfkkvvlp slaclriaay eeggkfighr ilpvqairpg yhyiclrner
      781 nqplmlpavf vyievkdyvp dtyadvieal snpiryvnlm eqrakqlaal tledeeevkk
      841 eadpgetsse apsetrttpa engvnhtatl apkppsqaph sqpapgsvka paktedliqs
      901 vlteveaqti eelkqqksfv klqkkhykem kdlvkrhhkk ttelikehtt kyneiqndyl
      961 rrraaleksa kkdskkksep sspdhgssai eqdlaaldae mtqklidlkd kqqqqllnlr
     1021 qeqyysekyq krehiklliq kltdvaeecq nnqlkklkei cekekkelkk kmdkkrqeki
     1081 teakskdksq meeektemir syiqevvqyi krleeaqskr qeklvekhke irqqildekp
     1141 klqmeleqey qdkfkrlple ilefvqeamk gkvsedsnhg sappslasdp akvnlkspss
     1201 eevqgenagr efdtpl
//
