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P10687 (PLCB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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-I
Short name=PLC-I
Phospholipase C-beta-1
Short name=PLC-beta-1
Gene names
Name:Plcb1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1216 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. Ref.2

Cofactor

Calcium.

Subunit structure

Interacts with DGKQ By similarity.

Subcellular location

Nucleus membrane By similarity. Cytoplasm. Note: Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes By similarity. Ref.2

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. Ref.2

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
   LigandCalcium
   Molecular functionHydrolase
Transducer
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of meiosis involved in egg activation

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

cerebral cortex development

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

glutamate receptor signaling pathway

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

insulin-like growth factor receptor signaling pathway

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

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

learning

Inferred from expression pattern PubMed 15159145. Source: RGD

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

memory

Inferred from expression pattern PubMed 15159145. Source: RGD

negative regulation of monocyte extravasation

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

negative regulation of transcription, DNA-templated

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

phosphatidylinositol metabolic process

Inferred from expression pattern PubMed 12786971. Source: RGD

positive regulation of CD24 biosynthetic process

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

positive regulation of G1/S transition of mitotic cell cycle

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

positive regulation of developmental growth

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

positive regulation of interleukin-12 production

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

positive regulation of myoblast differentiation

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

positive regulation of transcription, DNA-templated

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

regulation of G-protein coupled receptor protein signaling pathway

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

response to monosaccharide

Inferred from direct assay PubMed 11377826. Source: BHF-UCL

response to organonitrogen compound

Inferred from expression pattern PubMed 12850505. Source: RGD

response to peptide hormone

Inferred from direct assay PubMed 11377826. Source: BHF-UCL

   Cellular_componentcytoplasm

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

cytosol

Inferred from direct assay PubMed 15159145. Source: RGD

membrane

Inferred from direct assay PubMed 15159145. Source: RGD

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

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

nucleus

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

   Molecular_functioncalcium ion binding

Inferred from direct assay PubMed 11377826. Source: BHF-UCL

phosphatidylinositol phospholipase C activity

Inferred from direct assay PubMed 15159145. Source: RGD

protein binding

Inferred from physical interaction PubMed 11161216. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 16763092. Source: RGD

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 121612161-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
PRO_0000088488

Regions

Domain316 – 467152PI-PLC X-box
Domain540 – 656117PI-PLC Y-box
Domain663 – 76199C2

Sites

Active site3311 By similarity
Active site3781 By similarity

Amino acid modifications

Modified residue8871Phosphoserine; by PKC By similarity

Sequences

Sequence LengthMass (Da)Tools
P10687 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 92F23691781F788E

FASTA1,216138,344
        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 KFESFETSKK 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 
NQPLMLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK 

       850        860        870        880        890        900 
EADPGETSSE APSETRTTPA ENGVNHTATL 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 QEKLVEKHKE IRQQILDEKP 

      1150       1160       1170       1180       1190       1200 
KLQMELEQEY QDKFKRLPLE ILEFVQEAMK GKVSEDSNHG SAPPSLASDP AKVNLKSPSS 

      1210 
EEVQGENAGR EFDTPL 

« Hide

References

[1]"Cloning and sequence of multiple forms of phospholipase C."
Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.
Cell 54:161-169(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning, sequencing, purification, and Gq-dependent activation of phospholipase C-beta 3."
Jhon D.-Y., Lee H.-H., Park D., Lee C.-W., Lee K.-H., Yoo O.J., Rhee S.G.
J. Biol. Chem. 268:6654-6661(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20636 mRNA. Translation: AAA41885.1.
PIRA28821.
RefSeqNP_001071109.1. NM_001077641.1.
UniGeneRn.45523.

3D structure databases

ProteinModelPortalP10687.
SMRP10687. Positions 18-797.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246789. 162 interactions.
MINTMINT-1342819.
STRING10116.ENSRNOP00000042533.

Chemistry

BindingDBP10687.

PTM databases

PhosphoSiteP10687.

Proteomic databases

PaxDbP10687.
PRIDEP10687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24654.
KEGGrno:24654.
UCSCRGD:3344. rat.

Organism-specific databases

CTD23236.
RGD3344. Plcb1.

Phylogenomic databases

eggNOGNOG149692.
HOGENOMHOG000232046.
HOVERGENHBG053609.
InParanoidP10687.
KOK05858.
PhylomeDBP10687.
TreeFamTF313216.

Enzyme and pathway databases

BRENDA3.1.4.11. 5301.

Gene expression databases

GenevestigatorP10687.

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.
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.
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

NextBio603984.
PROP10687.

Entry information

Entry namePLCB1_RAT
AccessionPrimary (citable) accession number: P10687
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 11, 2014
This is version 136 of the entry and version 1 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