1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1

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P10687 (PLCB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1216 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Lipid degradation Lipid metabolism
Cellular component	Cytoplasm Membrane Nucleus
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G1 phase Inferred from sequence or structural similarity. Source: BHF-UCL activation 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-dependent 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 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-dependent 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 stimulus Inferred from direct assay PubMed 11377826. Source: BHF-UCL response to peptide hormone stimulus Inferred from direct assay PubMed 11377826. Source: BHF-UCL
Cellular_component	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
Molecular_function	calcium ion binding Inferred from direct assay PubMed 11377826. Source: BHF-UCL phosphatidylinositol phospholipase C activity Inferred from direct assay PubMed 15159145. Source: RGD 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1216

1216

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1

PRO_0000088488

Regions

Domain

316 – 467

152

PI-PLC X-box

Domain

540 – 656

117

PI-PLC Y-box

Domain

663 – 761

Sites

Active site

331

By similarity

Active site

378

By similarity

Amino acid modifications

Modified residue

333

Phosphothreonine By similarity

Modified residue

334

Phosphotyrosine By similarity

Modified residue

336

Phosphothreonine By similarity

Modified residue

887

Phosphoserine; by PKC By similarity

Modified residue

1197

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P10687 [UniParc].

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

1,216

138,344

        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

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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.
IPI	IPI00192534.
PIR	A28821.
RefSeq	NP_001071109.1. NM_001077641.1.
UniGene	Rn.45523.
3D structure databases
ProteinModelPortal	P10687.
SMR	P10687. Positions 18-797.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1342819.
STRING	10116.ENSRNOP00000042533.
PTM databases
PhosphoSite	P10687.
Proteomic databases
PaxDb	P10687.
PRIDE	P10687.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	24654.
KEGG	rno:24654.
UCSC	RGD:3344. rat.
Organism-specific databases
CTD	23236.
RGD	3344. Plcb1.
Phylogenomic databases
eggNOG	NOG149692.
HOGENOM	HOG000232046.
HOVERGEN	HBG053609.
InParanoid	P10687.
KO	K05858.
OMA	YRVFLNN.
OrthoDB	EOG40S0DW.
Enzyme and pathway databases
BRENDA	3.1.4.11. 5301.
Gene expression databases
ArrayExpress	P10687.
Genevestigator	P10687.
GermOnline	ENSRNOG00000004810. Rattus norvegicus.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 3.20.20.190. 2 hits.
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR001192. Pinositol_PLipase_C. IPR016280. PLC-beta. 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]
PANTHER	PTHR10336. PTHR10336. 1 hit.
Pfam	PF00168. C2. 1 hit. PF06631. DUF1154. 1 hit. PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. PF08703. PLC-beta_C. 1 hit. [Graphical view]
PIRSF	PIRSF000956. PLC-beta. 1 hit.
PRINTS	PR00390. PHPHLIPASEC.
SMART	SM00239. C2. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P10687.
NextBio	603984.

Entry information

Entry name

PLCB1_RAT

Accession

Primary (citable) accession number: P10687

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents