PLCB2

Protein identityUniProt · HPA

UniProt accession

Q00722

Gene

PLCB2

Ensembl

ENSG00000137841

Chromosome

15

Canonical length

1185 aa

Protein class

Enzymes, Metabolic proteins, Predicted intracellular proteins

Subcellular location

Golgi apparatus,Plasma membrane,Basal body,Cytosol

OverviewNCBI Gene

The protein encoded by this gene is a phosphodiesterase that catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate to the second messengers inositol 1,4,5-trisphosphate (IP3) and diacylglycerol. The encoded protein is activated by G proteins and has been shown to be involved in the type 2 taste receptor signal transduction pathway. In addition, nuclear factor kappa B can regulate the transcription of this gene, whose protein product is also an important regulator of platelet responses. [provided by RefSeq, Jan 2017]

Canonical amino-acid sequenceUniProt

1185 residues, UniProt reviewed canonical sequence.

>Q00722|PLCB2
     1  MSLLNPVLLP PKVKAYLSQG ERFIKWDDET TVASPVILRV DPKGYYLYWT YQSKEMEFLD
    61  ITSIRDTRFG KFAKMPKSQK LRDVFNMDFP DNSFLLKTLT VVSGPDMVDL TFHNFVSYKE
   121  NVGKAWAEDV LALVKHPLTA NASRSTFLDK ILVKLKMQLN SEGKIPVKNF FQMFPADRKR
   181  VEAALSACHL PKGKNDAINP EDFPEPVYKS FLMSLCPRPE IDEIFTSYHA KAKPYMTKEH
   241  LTKFINQKQR DSRLNSLLFP PARPDQVQGL IDKYEPSGIN AQRGQLSPEG MVWFLCGPEN
   301  SVLAQDKLLL HHDMTQPLNH YFINSSHNTY LTAGQFSGLS SAEMYRQVLL SGCRCVELDC
   361  WKGKPPDEEP IITHGFTMTT DIFFKEAIEA IAESAFKTSP YPIILSFENH VDSPRQQAKM
   421  AEYCRTIFGD MLLTEPLEKF PLKPGVPLPS PEDLRGKILI KNKKNQFSGP TSSSKDTGGE
   481  AEGSSPPSAP AGEGTVWAGE EGTELEEEEV EEEEEEESGN LDEEEIKKMQ SDEGTAGLEV
   541  TAYEEMSSLV NYIQPTKFVS FEFSAQKNRS YVISSFTELK AYDLLSKASV QFVDYNKRQM
   601  SRIYPKGTRM DSSNYMPQMF WNAGCQMVAL NFQTMDLPMQ QNMAVFEFNG QSGYLLKHEF
   661  MRRPDKQFNP FSVDRIDVVV ATTLSITVIS GQFLSERSVR TYVEVELFGL PGDPKRRYRT
   721  KLSPSTNSIN PVWKEEPFVF EKILMPELAS LRVAVMEEGN KFLGHRIIPI NALNSGYHHL
   781  CLHSESNMPL TMPALFIFLE MKDYIPGAWA DLTVALANPI KFFSAHDTKS VKLKEAMGGL
   841  PEKPFPLASP VASQVNGALA PTSNGSPAAR AGAREEAMKE AAEPRTASLE ELRELKGVVK
   901  LQRRHEKELR ELERRGARRW EELLQRGAAQ LAELGPPGVG GVGACKLGPG KGSRKKRSLP
   961  REESAGAAPG EGPEGVDGRV RELKDRLELE LLRQGEEQYE CVLKRKEQHV AEQISKMMEL
  1021  AREKQAAELK ALKETSENDT KEMKKKLETK RLERIQGMTK VTTDKMAQER LKREINNSHI
  1081  QEVVQVIKQM TENLERHQEK LEEKQAACLE QIREMEKQFQ KEALAEYEAR MKGLEAEVKE
  1141  SVRACLRTCF PSEAKDKPER ACECPPELCE QDPLIAKADA QESRL

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PLCB2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.32

Highest tissue expression

50 nTPM

Expression across tissuesHPA

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.85

gnomAD pLI

0

gnomAD missense Z

1.51

DepMap mean gene effect

-0.01

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cell chemotaxis
• detection of chemical stimulus involved in sensory perception of bitter taste
• G protein-coupled receptor signaling pathway
• lipid catabolic process
• phosphatidylinositol metabolic process
• phosphatidylinositol-mediated signaling
• phospholipase C-activating G protein-coupled receptor signaling pathway
• phospholipid metabolic process
• release of sequestered calcium ion into cytosol

Molecular functions

• calcium ion binding
• G-protein beta/gamma-subunit complex binding
• phosphatidylinositol phospholipase C activity
• phosphatidylinositol-4,5-bisphosphate phospholipase C activity
• phospholipase C activity
• phospholipid binding

Cellular components

• cytoplasm
• cytosol
• neuronal dense core vesicle
• G-protein beta/gamma-subunit complex

Protein domainsUniProt · Pfam · InterPro

• C2 domain
• Phosphatidylinositol-specific phospholipase C, X domain
• Phosphoinositide phospholipase C family
• Phospholipase C, phosphatidylinositol-specific, Y domain
• EF-hand domain pair
• Phospholipase C-beta, C-terminal domain
• Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase beta
• PLC-like phosphodiesterase, TIM beta/alpha-barrel domain superfamily
• C2 domain superfamily
• PLC-beta, PH domain
• Phospholipase C-beta, C-terminal domain superfamily
• Phosphoinositide phospholipase C beta 1-4-like, EF-hand domain
• C2 domain
• Phosphatidylinositol-specific phospholipase C, Y domain
• Phosphatidylinositol-specific phospholipase C, X domain
• PLC-beta C terminal
• PH domain
• Phosphoinositide phospholipase C beta1-4-like EF-hand domain
• 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, catalytic domain
• 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2, EF-hand domain

KeywordsUniProt

• Calcium
• Coiled coil
• Hydrolase
• Lipid degradation
• Lipid metabolism
• Metal-binding
• Phosphoprotein
• Transducer

InteractionsUniProt · HPA

Protein binding partners of PLCB2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• RAC1