1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2

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O89040 (PLCB2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. History...

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

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·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-2
EC=3.1.4.11

Alternative name(s):
Phosphoinositide phospholipase C-beta-2
Phospholipase C-beta-2
Short name=PLC-beta-2

Gene names

Name:

Plcb2

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	1183 AA.
Sequence status	Complete.
Protein existence	Evidence 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. This protein may be involved in the transduction of bitter taste stimuli. Ref.1 UniProtKB Q00722
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H₂O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. UniProtKB Q00722
Cofactor	Binds 1 calcium ion per subunit By similarity. UniProtKB Q00722
Subunit structure	Interacts with RAC1 By similarity. UniProtKB Q00722
Tissue specificity	Expressed in the gustatory cells of the circumvallate papillae. Not detected in non-sensory lingual epithelium, brain, parotid gland, liver, uterus, lung, heart, adrenal gland, ovary, spleen, pancreas, intestine, thymus, kidney or muscle. Ref.1 Ref.2
Miscellaneous	The receptor-mediated activation of PLC-beta-2 is most effectively mediated by one G-protein alpha subunit, alpha-16. UniProtKB Q00722
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
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Transducer
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	detection of chemical stimulus involved in sensory perception of bitter taste Inferred from direct assay Ref.1. Source: UniProtKB intracellular signal transduction Inferred from direct assay Ref.1. Source: UniProtKB phospholipid catabolic process Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	G-protein beta/gamma-subunit complex Inferred from direct assay PubMed 9931017. Source: RGD Golgi apparatus Inferred from direct assay PubMed 10070498. Source: RGD cytosol Inferred from direct assay PubMed 12176394. Source: RGD plasma membrane Inferred from direct assay PubMed 12176394. Source: RGD
Molecular_function	G-protein beta/gamma-subunit complex binding Inferred from direct assay PubMed 9931017. Source: RGD calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol phospholipase C activity Non-traceable author statement Ref.1. Source: UniProtKB phospholipid binding Inferred from direct assay PubMed 9931017. Source: RGD signal transducer activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select] Note: A number of isoforms may be produced.

Isoform 1 Ref.1 (identifier: O89040-1) 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1183

1183

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2

PRO_0000088490

Regions

Domain

312 – 463

152

PI-PLC X-box

Domain

550 – 666

117

PI-PLC Y-box

Domain

673 – 771

Coiled coil

1077 – 1146

Potential

Compositional bias

492 – 549

Glu-rich

Sites

Active site

327

By similarity UniProtKB P10688

Active site

374

By similarity UniProtKB P10688

Metal binding

328

Calcium By similarity UniProtKB Q00722

Metal binding

357

Calcium By similarity UniProtKB Q00722

Metal binding

359

Calcium By similarity UniProtKB Q00722

Metal binding

408

Calcium By similarity UniProtKB Q00722

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: BA3AD63FE074A18C
Show »

FASTA

1,183

134,883

        10         20         30         40         50         60 
MSLLNPVLLP PKVKAYLSQG ERFIKWDDET SIASPVILRV DPKGYYLYWT HQSKEMEFLD 

        70         80         90        100        110        120 
VTSIRDTRFG KFAKIPKSQK LREVFNMDFP DNHFLLKTFT VVSGPDMVGL TFHNFVSYKE 

       130        140        150        160        170        180 
NVGKDWAEDV LALAKHPMTA NASRSTFLDK ILVKLKMQLS PEGKIPVKNF FQMFPADRKR 

       190        200        210        220        230        240 
VEAALSACHL AKGKNDAINP EDFPESVYKS FLMSLCPRPE IDEIFTSYHA KAKPYMTKEH 

       250        260        270        280        290        300 
LTKFINQKQR DPRLNSLLFP PARPEQVQAL IDKYEPSGIN VQRGQLSPEG MVWFLCGPEN 

       310        320        330        340        350        360 
SVLAHDTLRI HQDMTQPLNH YFINSSHNTY LTAGQFSGPS SAEMYRQVLL SGCRCVELDC 

       370        380        390        400        410        420 
WKGKPPDEEP IITHGFTMTT DILFKEAVEA IAESAFKTSP YPVILSFENH VDSPRQQAKM 

       430        440        450        460        470        480 
AEYCRTMFGE TLLTEPLENF PLKPGMPLPS PEDLRGKILI KNKKNQFSGP ASPNKKPDGV 

       490        500        510        520        530        540 
SEGGFPSSVP VEEDTGWTAE DRTEVEEGEE EEEVEEEEEE ESGNLDEEEI KKMQSDEGTA 

       550        560        570        580        590        600 
GLEVTAYEEM SSLVNYIQPT KFISFEFSAQ KNRSYLVSSF TELKAYELLS KASMQFVDYN 

       610        620        630        640        650        660 
KRQMSRVYPK GTRMDSSNYM PQMFWNAGCQ MVALNFQTMD LPMQQNMALF EFNGQSGYLL 

       670        680        690        700        710        720 
KHEFMRRQDK QFNPFSVDRI DVVVATTLSI TVISGQFLSE RSVRTYVEVE LFGLPGDPKR 

       730        740        750        760        770        780 
RYRTKLSPTA NSINPVWKEE PFIFEKILVP ELASLRIAVM EEGGKFIGHR IIPINALHSG 

       790        800        810        820        830        840 
YHHLCLRSES NMPLTMPALF VFLEMKDYVP DTWADLTVAL ANPIKYFSAH DKKSVKLKEV 

       850        860        870        880        890        900 
TGSLPEKLFS GIPVASQSNG APVSAGNGST APGTKAKEEA TKEVAEPQTT SLEELRELKG 

       910        920        930        940        950        960 
VVKLQRRHEK ELRELERRGA RRWEELLQRG AAQLAELQDP AASCKLRPGK GSRKKRIVPC 

       970        980        990       1000       1010       1020 
EETIVVPREV LEGPDPRVQD LKDRLEQELQ QQGEEQYRSV LKRKEQHVTE QIAKMMELAR 

      1030       1040       1050       1060       1070       1080 
EKQAAELKSF KETSETDTKE MKKKLEAKRL ERIQAMTKVT TDKVAQERLK REINNSHIQE 

      1090       1100       1110       1120       1130       1140 
VVQAVKQMTE TLERHQEKLE EKQTACLEQI QAMEKQFQEK ALAEYEAKMK GLEAEVKESM 

      1150       1160       1170       1180 
RACFKACFPT EAEEKPERPC EASEESCPQE PLVNKTDTQE SRL

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References

[1]	"Identification of a phospholipase C beta subtype in rat taste cells." Roessler P., Kroner C., Freitag J., Noe J., Breer H. Eur. J. Cell Biol. 77:253-261(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Circumvallate papilla.
[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: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ011035 mRNA. Translation: CAA09465.1.
IPI	IPI00203756.
RefSeq	NP_445930.1. NM_053478.1.
UniGene	Rn.30033.
3D structure databases
ProteinModelPortal	O89040.
SMR	O89040. Positions 11-807.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000011911.
PTM databases
PhosphoSite	O89040.
Proteomic databases
PaxDb	O89040.
PRIDE	O89040.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	85240.
KEGG	rno:85240.
UCSC	RGD:621004. rat.
Organism-specific databases
CTD	5330.
RGD	621004. Plcb2.
Phylogenomic databases
eggNOG	NOG149692.
HOGENOM	HOG000232046.
HOVERGEN	HBG053609.
KO	K05858.
OrthoDB	EOG4894KQ.
Gene expression databases
ArrayExpress	O89040.
Genevestigator	O89040.
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. 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. 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
NextBio	617292.

Entry information

Entry name

PLCB2_RAT

Accession

Primary (citable) accession number: O89040

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2003
Last sequence update:	November 1, 1998
Last modified:	April 3, 2013
This is version 95 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents