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Q9Z1B3 (PLCB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1

EC=3.1.4.11
Alternative name(s):
PLC-154
Phosphoinositide phospholipase C-beta-1
Phospholipase C-beta-1
Short name=PLC-beta-1
Gene names
Name:Plcb1
Synonyms:Plcb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1216 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 By similarity.

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactor

Calcium By similarity.

Subunit structure

Interacts with DGKQ By similarity.

Subcellular location

Nucleus membrane. Cytoplasm By similarity. Note: Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes By similarity. Ref.7

Miscellaneous

The receptor-mediated activation of PLC-beta-1 is mediated by two G-protein alpha subunits, alpha-Q and alpha-11.

Sequence similarities

Contains 1 C2 domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandCalcium
   Molecular functionHydrolase
Transducer
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled acetylcholine receptor signaling pathway

Inferred from mutant phenotype PubMed 9305844. Source: BHF-UCL

G2/M transition of mitotic cell cycle

Inferred from direct assay PubMed 19028838. Source: BHF-UCL

activation of meiosis involved in egg activation

Inferred from direct assay PubMed 14499343. Source: BHF-UCL

brain development

Non-traceable author statement PubMed 18493969. Source: BHF-UCL

cell adhesion

Inferred by curator PubMed 15849202. Source: BHF-UCL

cerebral cortex development

Inferred from mutant phenotype PubMed 11224545. Source: BHF-UCL

erythrocyte differentiation

Traceable author statement PubMed 19159640. Source: BHF-UCL

fat cell differentiation

Inferred from direct assay PubMed 19385066. Source: BHF-UCL

glutamate receptor signaling pathway

Inferred from mutant phenotype PubMed 11224545. Source: BHF-UCL

insulin receptor signaling pathway

Traceable author statement PubMed 19159640. Source: BHF-UCL

insulin-like growth factor receptor signaling pathway

Inferred from direct assay PubMed 9187110. Source: BHF-UCL

interleukin-1-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

interleukin-12-mediated signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

interleukin-15-mediated signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Traceable author statement PubMed 9159640. Source: BHF-UCL

macrophage differentiation

Non-traceable author statement PubMed 19850892. Source: BHF-UCL

memory

Inferred from mutant phenotype PubMed 18493969. Source: BHF-UCL

negative regulation of monocyte extravasation

Inferred from direct assay PubMed 19687358. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12031797PubMed 17022104. Source: BHF-UCL

oocyte maturation

Non-traceable author statement PubMed 17725492. Source: BHF-UCL

phosphatidylinositol metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of CD24 biosynthetic process

Inferred from direct assay PubMed 15849202. Source: BHF-UCL

positive regulation of G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 10913438. Source: BHF-UCL

positive regulation of JNK cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of acrosome reaction

Inferred from mutant phenotype PubMed 11464583. Source: BHF-UCL

positive regulation of developmental growth

Inferred from mutant phenotype PubMed 15474310. Source: BHF-UCL

positive regulation of embryonic development

Inferred from mutant phenotype PubMed 11464583. Source: BHF-UCL

positive regulation of interleukin-12 production

Inferred from mutant phenotype PubMed 9444325. Source: BHF-UCL

positive regulation of myoblast differentiation

Inferred from direct assay PubMed 15174099. Source: BHF-UCL

positive regulation of sodium:proton antiporter activity

Non-traceable author statement PubMed 15864321. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15849202. Source: BHF-UCL

regulation of G-protein coupled receptor protein signaling pathway

Inferred from mutant phenotype PubMed 18493969. Source: BHF-UCL

regulation of fertilization

Inferred from mutant phenotype PubMed 11464583. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 19159640. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15849202PubMed 17725492. Source: BHF-UCL

nuclear chromatin

Inferred from direct assay PubMed 19028838. Source: BHF-UCL

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from direct assay PubMed 17022104. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 10913438PubMed 14499343PubMed 15174099PubMed 15849202PubMed 17725492. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionGTPase activator activity

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from electronic annotation. Source: InterPro

calmodulin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

enzyme binding

Inferred from sequence or structural similarity. Source: BHF-UCL

lamin binding

Inferred from physical interaction PubMed 19028838. Source: BHF-UCL

phosphatidylinositol phospholipase C activity

Inferred from direct assay PubMed 9762362. Source: BHF-UCL

phosphatidylinositol-4,5-bisphosphate binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 17022104. Source: BHF-UCL

protein homodimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9Z1B3-1)

Also known as: C-beta-1a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q9Z1B3-2)

Also known as: C-beta-1b;

The sequence of this isoform differs from the canonical sequence as follows:
     1142-1216: LQTELEQEYQ...NPGREFDTPL → GEGPSSVLSEGCHEDPSVPPNFTPPNPQALKW
Isoform C (identifier: Q9Z1B3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1199-1216: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 121612161-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
PRO_0000088487

Regions

Domain316 – 467152PI-PLC X-box
Domain540 – 656117PI-PLC Y-box
Domain663 – 76199C2
Compositional bias914 – 1088175Lys-rich

Sites

Active site3311 By similarity
Active site3781 By similarity

Amino acid modifications

Modified residue8871Phosphoserine; by PKC By similarity

Natural variations

Alternative sequence1142 – 121675LQTEL…FDTPL → GEGPSSVLSEGCHEDPSVPP NFTPPNPQALKW in isoform B.
VSP_008917
Alternative sequence1199 – 121618Missing in isoform C.
VSP_008918

Experimental info

Sequence conflict281F → L in AAD00571. Ref.1
Sequence conflict281F → L in AAD00572. Ref.1
Sequence conflict281F → L in AAD00573. Ref.1
Sequence conflict411I → T in AAD00571. Ref.1
Sequence conflict411I → T in AAD00572. Ref.1
Sequence conflict411I → T in AAD00573. Ref.1
Sequence conflict671S → T in AAD01749. Ref.5
Sequence conflict791K → E in AAD00571. Ref.1
Sequence conflict791K → E in AAD00572. Ref.1
Sequence conflict791K → E in AAD00573. Ref.1
Sequence conflict1121V → A in AAD00571. Ref.1
Sequence conflict1121V → A in AAD00572. Ref.1
Sequence conflict1121V → A in AAD00573. Ref.1
Sequence conflict5611R → I in CAA64637. Ref.6
Sequence conflict6131L → I in CAA64637. Ref.6
Sequence conflict6221V → M in AAD00571. Ref.1
Sequence conflict6221V → M in AAD00572. Ref.1
Sequence conflict6221V → M in AAD00573. Ref.1
Sequence conflict7141K → T in AAD00571. Ref.1
Sequence conflict7141K → T in AAD00572. Ref.1
Sequence conflict7141K → T in AAD00573. Ref.1
Sequence conflict7951V → D in AAD00571. Ref.1
Sequence conflict7951V → D in AAD00572. Ref.1
Sequence conflict7951V → D in AAD00573. Ref.1
Sequence conflict9231Q → H in AAD00571. Ref.1
Sequence conflict9231Q → H in AAD00572. Ref.1
Sequence conflict9231Q → H in AAD00573. Ref.1
Sequence conflict9571N → I in AAD00571. Ref.1
Sequence conflict9571N → I in AAD00572. Ref.1
Sequence conflict9571N → I in AAD00573. Ref.1
Sequence conflict10841K → T in AAD00571. Ref.1
Sequence conflict10841K → T in AAD00572. Ref.1
Sequence conflict10841K → T in AAD00573. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A (C-beta-1a) [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: CC751D49895A47D0

FASTA1,216138,396
        10         20         30         40         50         60 
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE 

        70         80         90        100        110        120 
TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV 

       130        140        150        160        170        180 
AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA 

       190        200        210        220        230        240 
DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL 

       250        260        270        280        290        300 
TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS 

       310        320        330        340        350        360 
GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV 

       370        380        390        400        410        420 
ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ 

       430        440        450        460        470        480 
QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK 

       490        500        510        520        530        540 
KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM 

       550        560        570        580        590        600 
SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK 

       610        620        630        640        650        660 
GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK 

       670        680        690        700        710        720 
HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG 

       730        740        750        760        770        780 
NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER 

       790        800        810        820        830        840 
NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK 

       850        860        870        880        890        900 
EADPGETSSE APSETRTTPA ENGVNHTASL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS 

       910        920        930        940        950        960 
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL 

       970        980        990       1000       1010       1020 
RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR 

      1030       1040       1050       1060       1070       1080 
QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI 

      1090       1100       1110       1120       1130       1140 
TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHNE IRQQILDEKP 

      1150       1160       1170       1180       1190       1200 
KLQTELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPPSLASDA AKVNLKSPSS 

      1210 
EEIERENPGR EFDTPL 

« Hide

Isoform B (C-beta-1b) [UniParc].

Checksum: 5AA8EEB1FCED1D93
Show »

FASTA1,173133,327
Isoform C [UniParc].

Checksum: E95E5F34E58C48CA
Show »

FASTA1,198136,309

References

« Hide 'large scale' references
[1]"Cloning of PI-specific phospholipase C's from 3T3 cells. Expression and membrane targeting of a novel phospholipase C-beta-1 isoform."
Bai J., Wu K., Marks D.L., Machamer C., Pagano R.E.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
Strain: Swiss.
[2]"High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
Strain: ILS and ISS.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: C57BL/6.
Tissue: Brain.
[5]"Patterns of expression for the mRNA corresponding to the four isoforms of phospholipase Cbeta in mouse brain."
Watanabe M., Nakamura M., Sato K., Kano M., Simon M.I., Inoue Y.
Eur. J. Neurosci. 10:2016-2025(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-145.
Strain: C57BL/6.
[6]"Phospholipase C in mouse oocytes: characterization of beta and gamma isoforms and their possible involvement in sperm-induced Ca2+ spiking."
Dupont G., McGuinness O.M., Johnson M.H., Berridge M.J., Borgese F.
Biochem. J. 316:583-591(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 428-615.
Tissue: Oocyte.
[7]"Nuclear alpha1-adrenergic receptors signal activated ERK localization to caveolae in adult cardiac myocytes."
Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S., O'Connell T.D.
Circ. Res. 103:992-1000(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85712 mRNA. Translation: AAD00571.1.
U85713 mRNA. Translation: AAD00572.1.
U85714 mRNA. Translation: AAD00573.1.
AF498249 mRNA. Translation: AAM22966.1.
AF498250 mRNA. Translation: AAM22967.1.
AL928635 expand/collapse EMBL AC list , AL840635, AL928956, AL935278 Genomic DNA. Translation: CAM23602.1.
AL840635 expand/collapse EMBL AC list , AL928635, AL928956, AL935278 Genomic DNA. Translation: CAM23766.1.
AL928956 expand/collapse EMBL AC list , AL840635, AL928635, AL935278 Genomic DNA. Translation: CAM26804.1.
AL935278 expand/collapse EMBL AC list , AL840635, AL928635, AL928956 Genomic DNA. Translation: CAM27130.1.
BC058710 mRNA. Translation: AAH58710.1.
AF022801 mRNA. Translation: AAD01749.1.
X95344 mRNA. Translation: CAA64637.1.
CCDSCCDS16787.1. [Q9Z1B3-2]
CCDS50729.1. [Q9Z1B3-1]
PIRS68256.
RefSeqNP_001139302.1. NM_001145830.1. [Q9Z1B3-1]
NP_062651.2. NM_019677.2. [Q9Z1B3-2]
UniGeneMm.330607.

3D structure databases

ProteinModelPortalQ9Z1B3.
SMRQ9Z1B3. Positions 11-830, 890-1170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202232. 1 interaction.
IntActQ9Z1B3. 4 interactions.
MINTMINT-4107696.

PTM databases

PhosphoSiteQ9Z1B3.

Proteomic databases

MaxQBQ9Z1B3.
PaxDbQ9Z1B3.
PRIDEQ9Z1B3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070724; ENSMUSP00000064844; ENSMUSG00000051177. [Q9Z1B3-2]
ENSMUST00000110116; ENSMUSP00000105743; ENSMUSG00000051177. [Q9Z1B3-1]
GeneID18795.
KEGGmmu:18795.
UCSCuc008mny.2. mouse. [Q9Z1B3-1]

Organism-specific databases

CTD23236.
MGIMGI:97613. Plcb1.

Phylogenomic databases

eggNOGNOG149692.
GeneTreeENSGT00730000110266.
HOVERGENHBG053609.
InParanoidQ6PDH1.
KOK05858.
OMAMMDFINL.
OrthoDBEOG7WDN1N.
TreeFamTF313216.

Enzyme and pathway databases

BRENDA3.1.4.11. 3474.
ReactomeREACT_188937. Metabolism.

Gene expression databases

ArrayExpressQ9Z1B3.
BgeeQ9Z1B3.
CleanExMM_PLCB1.
GenevestigatorQ9Z1B3.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR016280. PLC-beta.
IPR028400. PLC-beta1.
IPR014815. PLC-beta_C.
IPR009535. PLC-beta_CS.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
[Graphical view]
PANTHERPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF12. PTHR10336:SF12. 1 hit.
PfamPF00168. C2. 1 hit.
PF06631. DUF1154. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF08703. PLC-beta_C. 1 hit.
[Graphical view]
PIRSFPIRSF000956. PLC-beta. 1 hit.
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLCB1. mouse.
NextBio295080.
PROQ9Z1B3.
SOURCESearch...

Entry information

Entry namePLCB1_MOUSE
AccessionPrimary (citable) accession number: Q9Z1B3
Secondary accession number(s): Q62075 expand/collapse secondary AC list , Q6PDH1, Q8K5A5, Q8K5A6, Q9Z0E5, Q9Z2T5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot