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P10894 (PLCB1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 122. 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-beta-1
Short name=PLC-beta-1
Gene names
Name:PLCB1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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.

Cofactor

Calcium.

Subunit structure

Interacts with DGKQ By similarity.

Subcellular location

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

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
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled acetylcholine receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

activation of meiosis involved in egg activation

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

glutamate receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

insulin-like growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

interleukin-1-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

interleukin-12-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

interleukin-15-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of monocyte extravasation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of CD24 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of JNK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of acrosome reaction

Inferred from electronic annotation. Source: Ensembl

positive regulation of developmental growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of embryonic development

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-12 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of myoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of G-protein coupled receptor protein signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of fertilization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: AgBase

cytosol

Traceable author statement. Source: Reactome

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTPase activator activity

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from electronic annotation. Source: InterPro

phosphatidylinositol phospholipase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphatidylinositol-4,5-bisphosphate binding

Inferred from electronic annotation. Source: Ensembl

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_0000088485

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 Ref.2

Sequences

Sequence LengthMass (Da)Tools
P10894 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: BEF809177F1B7ABB

FASTA1,216138,715
        10         20         30         40         50         60 
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WEDDSTVVTP IILRTDPQGF FFYWTDQNKE 

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

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

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

       250        260        270        280        290        300 
TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NNSLAKKGQI 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 LDKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK 

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

       550        560        570        580        590        600 
SNLVNYIQPV KFESFEISKK RNRSFEMSSF 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 
NAVNPIWEEE PIVFKKVVLP SLACLRIAVY EEGGKFIGHR ILPVQAIRPG YHYICLRNER 

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

       850        860        870        880        890        900 
EADPGETPSE APSEARPTPA ENGVNHTTSL TPKPPSQALH SQPAPGSVKA PAKTEDLIQS 

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

       970        980        990       1000       1010       1020 
RRRAALEKTA KKDNKKKSEP SSPDHVSSTI EQDLAALDAE MTQKLVDLKD 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 
KLQVELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHS SAPPLMTSDS GKLNQKPPSS 

      1210 
EELEGENPGK EFDTPL 

« Hide

References

[1]"Determination of the primary structure of PLC-154 demonstrates diversity of phosphoinositide-specific phospholipase C activities."
Katan M., Kriz R.W., Totty N., Philp R., Meldrum E., Aldape R.A., Knopf J.L., Parker P.J.
Cell 54:171-177(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Feedback regulation of phospholipase C-beta by protein kinase C."
Ryu S.H., Kim U.H., Wahl M.I., Brown A.B., Carpenter G., Huang K.P., Rhee S.G.
J. Biol. Chem. 265:17941-17945(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 879-889, PHOSPHORYLATION AT SER-887.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03137 mRNA. Translation: AAA30702.1.
PIRA28822.
RefSeqNP_777242.1. NM_174817.1.
UniGeneBt.448.

3D structure databases

ProteinModelPortalP10894.
SMRP10894. Positions 18-797.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid160009. 1 interaction.
MINTMINT-144720.
STRING9913.ENSBTAP00000046644.

Proteomic databases

PRIDEP10894.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000049812; ENSBTAP00000046644; ENSBTAG00000008338.
GeneID287026.
KEGGbta:287026.

Organism-specific databases

CTD23236.

Phylogenomic databases

eggNOGNOG149692.
GeneTreeENSGT00730000110266.
HOGENOMHOG000232046.
HOVERGENHBG053609.
InParanoidP10894.
KOK05858.
OMAMMDFINL.
OrthoDBEOG7WDN1N.
TreeFamTF313216.

Enzyme and pathway databases

ReactomeREACT_214353. Signal Transduction.

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.
PfamPF06631. 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

NextBio20806548.

Entry information

Entry namePLCB1_BOVIN
AccessionPrimary (citable) accession number: P10894
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 14, 2014
This is version 122 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