PLCB4_RAT
ID PLCB4_RAT Reviewed; 1175 AA.
AC Q9QW07; O88356; Q9Z0G6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q07722};
DE AltName: Full=Phosphoinositide phospholipase C-beta-4;
DE AltName: Full=Phospholipase C-beta-4;
DE Short=PLC-beta-4;
GN Name=Plcb4 {ECO:0000312|RGD:3345};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8407970; DOI=10.1016/s0021-9258(19)36926-1;
RA Lee C.-W., Park D.J., Lee K.-H., Kim C.G., Rhee S.G.;
RT "Purification, molecular cloning, and sequencing of phospholipase C-beta
RT 4.";
RL J. Biol. Chem. 268:21318-21327(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7688223; DOI=10.1006/bbrc.1993.1879;
RA Kim M.J., Bahk Y.Y., Min D.S., Lee S.J., Ryu S.H., Suh P.G.;
RT "Cloning of cDNA encoding rat phospholipase C-beta 4, a new member of the
RT phospholipase C.";
RL Biochem. Biophys. Res. Commun. 194:706-712(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 447-1175 (ISOFORM C).
RC TISSUE=Brain;
RX PubMed=9931434; DOI=10.1016/s0167-4781(98)00260-7;
RA Adamski F.M., Timms K.M., Shieh B.H.;
RT "A unique isoform of phospholipase Cbeta4 highly expressed in the
RT cerebellum and eye.";
RL Biochim. Biophys. Acta 1444:55-60(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-886, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 This form has a role in retina signal transduction.
CC {ECO:0000250|UniProtKB:Q07722}.
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:0000250|UniProtKB:Q07722};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:Q07722};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC Evidence={ECO:0000250|UniProtKB:Q07722};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:Q07722};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q9QW07-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9QW07-2; Sequence=VSP_004724, VSP_004725;
CC Name=C;
CC IsoId=Q9QW07-3; Sequence=VSP_004726;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the retina.
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DR EMBL; L15556; AAK13557.1; -; mRNA.
DR EMBL; U57836; AAD10403.1; -; mRNA.
DR EMBL; AF031370; AAC98145.1; -; mRNA.
DR EMBL; AF027571; AAC24984.1; -; mRNA.
DR PIR; A48047; A48047.
DR RefSeq; NP_077329.1; NM_024353.1.
DR AlphaFoldDB; Q9QW07; -.
DR SMR; Q9QW07; -.
DR IntAct; Q9QW07; 2.
DR STRING; 10116.ENSRNOP00000045972; -.
DR iPTMnet; Q9QW07; -.
DR PhosphoSitePlus; Q9QW07; -.
DR jPOST; Q9QW07; -.
DR PaxDb; Q9QW07; -.
DR PRIDE; Q9QW07; -.
DR GeneID; 25031; -.
DR KEGG; rno:25031; -.
DR UCSC; RGD:3345; rat. [Q9QW07-1]
DR CTD; 5332; -.
DR RGD; 3345; Plcb4.
DR eggNOG; KOG1265; Eukaryota.
DR InParanoid; Q9QW07; -.
DR BRENDA; 3.1.4.11; 5301.
DR Reactome; R-RNO-112043; PLC beta mediated events.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:Q9QW07; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:RGD.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:RGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0007602; P:phototransduction; NAS:RGD.
DR CDD; cd13361; PH_PLC_beta; 1.
DR Gene3D; 1.20.1230.10; -; 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; IPR016280; PLC-beta.
DR InterPro; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR037862; PLC-beta_PH.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF06631; DUF1154; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PIRSF; PIRSF000956; PLC-beta; 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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Hydrolase; Lipid degradation;
KW Lipid metabolism; Phosphoprotein; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15147"
FT CHAIN 2..1175
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-4"
FT /id="PRO_0000088496"
FT DOMAIN 313..463
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 565..681
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 684..809
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 487..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15147"
FT MOD_RES 886
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1013..1022
FT /note="VKEIVAQHTK -> GKQRDASPSG (in isoform B)"
FT /evidence="ECO:0000303|PubMed:7688223"
FT /id="VSP_004724"
FT VAR_SEQ 1023..1175
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:7688223"
FT /id="VSP_004725"
FT VAR_SEQ 1154..1175
FT /note="AKEMQQMVKLEAEMDRRPATVV -> LLKSCHAVSQTQGEGDAADGEIGSRD
FT GPQTSNSSMKLQNAN (in isoform C)"
FT /evidence="ECO:0000303|PubMed:9931434"
FT /id="VSP_004726"
FT CONFLICT 255
FT /note="L -> M (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="R -> A (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="Q -> E (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="E -> K (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="A -> AA (in Ref. 1; AAK13557)"
FT /evidence="ECO:0000305"
FT CONFLICT 545..546
FT /note="EQ -> DE (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="I -> L (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="R -> H (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="L -> M (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="D -> N (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 828
FT /note="F -> L (in Ref. 1; AAK13557)"
FT /evidence="ECO:0000305"
FT CONFLICT 843
FT /note="S -> Y (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 852
FT /note="L -> M (in Ref. 3; AAC24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="Q -> T (in Ref. 2; AAD10403/AAC98145)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="W -> C (in Ref. 3; AAC24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 1043
FT /note="L -> M (in Ref. 3; AAC24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057
FT /note="A -> V (in Ref. 3; AAC24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 1067
FT /note="L -> V (in Ref. 3; AAC24984)"
FT /evidence="ECO:0000305"
FT CONFLICT 1084
FT /note="S -> C (in Ref. 3; AAC24984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1175 AA; 134497 MW; 7379C6BB95B8FCED CRC64;
MAKPYEFNWQ KEVPSFLQEG AVFDRYEEES FVFEPNCLFK VDEFGFFLTW KSEGKEGQVL
ECSLINSIRL AAIPKDPKIL AALESVGKSE NDLEGRILCV CSGTDLVNIG FTYMVAENPE
ITKQWVEGLR SIIHNFRANN VSPMTCLKKH WMKLAFLTNT SGKIPVRSIT RTFASGKTEK
VIFQALKELG LPSGKNDEIE PAAFTYEKFY ELTQKICPRT DIEDLFKKIN GDKTDYLTVD
QLVSFLNEHQ RDPRLNEILF PFYDAKRAMQ IIEMYEPDEE LKKKGLISSD GFCRYLMSDE
NAPVFLDRLE LYQEMDHPLA HYFISSSHNT YLTGRQFGGK SSVEMYRQVL LAGCRCVELD
CWDGKGEDQE PIITHGKAMC TDILFKDVIQ AIKETAFVTS EYPVILSFEN HCSKYQQYQM
SKYCEDLFGD LLLKQALESH PLEPGRLLPS PNDLKRKILI KNKRLKPEVE KKQLEALKSM
MEAGESAAPA SILEDDNEEE IESADQEEEA HPEYKFGNEL SADDFSHKEA VANSVKKGLV
TVEDEQAWMA SYKYVGATTN IHPYLSTMIN YAQPVKFQGF HVAEERNIHY NMSSFNESVG
LGYLKTHAIE FVNYNKRQMS RIYPKGGRVD SSNYMPQIFW NAGCQMVSLN YQTPDLAMQL
NQGKFEYNGS CGYLLKPDFM RRPDRTFDPF SETPVDGVIA ATCSVQVISG QFLSDKKIGT
YVEVDMYGLP TDTIRKEFRT RMVMNNGLNP VYNEESFVFR KVILPDLAVL RIAVYDDNNK
LIGQRILPLD GLQAGYRHIS LRNEGNKPLS LPTIFCNIVL KTYVPDGFGD IVDALSDPKK
FLSITEKRAD QLRAMGIETS DIADVPSDTS KNDKKGKANP AKANVTPQSS SELRPTTTAA
LGSGQEAKKG IELIPQVRIE DLKQMKAYLK HLKKQQKELN SLKKKHAKEH STMQKLHCTQ
VDKIVAQYDK EKSTHEKILE KAMKKKGGSN CLEIKKETEI KIQTLTSDHK SKVKEIVAQH
TKEWSEMINT HSAEEQEIRD LHLSQQCELL RKLLINAHEQ QTQQLKLSHD RESKEMRAHQ
AKISMENSKA ISQDKSIKNK AERERRVREL NSSNTKKFLE ERKRLAMKQS KEMDQLKKVQ
LEHLEFLEKQ NEQAKEMQQM VKLEAEMDRR PATVV
