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P10687

- PLCB1_RAT

UniProt

P10687 - PLCB1_RAT

Protein

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

Gene

Plcb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Cofactori

    Calcium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei331 – 3311PROSITE-ProRule annotation
    Active sitei378 – 3781PROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: BHF-UCL
    2. phosphatidylinositol phospholipase C activity Source: RGD
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: RGD
    5. signal transducer activity Source: UniProtKB-KW

    GO - Biological processi

    1. activation of meiosis involved in egg activation Source: BHF-UCL
    2. cerebral cortex development Source: BHF-UCL
    3. glutamate receptor signaling pathway Source: BHF-UCL
    4. insulin-like growth factor receptor signaling pathway Source: BHF-UCL
    5. intracellular signal transduction Source: InterPro
    6. learning Source: RGD
    7. lipid catabolic process Source: UniProtKB-KW
    8. memory Source: RGD
    9. negative regulation of monocyte extravasation Source: BHF-UCL
    10. negative regulation of transcription, DNA-templated Source: BHF-UCL
    11. phosphatidylinositol metabolic process Source: RGD
    12. positive regulation of CD24 biosynthetic process Source: BHF-UCL
    13. positive regulation of developmental growth Source: BHF-UCL
    14. positive regulation of G1/S transition of mitotic cell cycle Source: BHF-UCL
    15. positive regulation of interleukin-12 production Source: BHF-UCL
    16. positive regulation of myoblast differentiation Source: BHF-UCL
    17. positive regulation of transcription, DNA-templated Source: BHF-UCL
    18. regulation of G-protein coupled receptor protein signaling pathway Source: BHF-UCL
    19. response to monosaccharide Source: BHF-UCL
    20. response to organonitrogen compound Source: RGD
    21. response to peptide hormone Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Transducer

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    BRENDAi3.1.4.11. 5301.
    ReactomeiREACT_194690. Ca2+ pathway.
    REACT_196412. Presynaptic function of Kainate receptors.
    REACT_198661. Synthesis of IP3 and IP4 in the cytosol.
    REACT_208646. G beta:gamma signalling through PLC beta.
    REACT_221588. PLC beta mediated events.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:Plcb1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3344. Plcb1.

    Subcellular locationi

    Nucleus membrane By similarity. Cytoplasm 1 Publication
    Note: Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: RGD
    3. membrane Source: RGD
    4. nuclear membrane Source: UniProtKB-SubCell
    5. nuclear speck Source: BHF-UCL
    6. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 121612161-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1PRO_0000088488Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei887 – 8871Phosphoserine; by PKCBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP10687.
    PRIDEiP10687.

    PTM databases

    PhosphoSiteiP10687.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    GenevestigatoriP10687.

    Interactioni

    Subunit structurei

    Interacts with DGKQ.By similarity

    Protein-protein interaction databases

    BioGridi246789. 162 interactions.
    MINTiMINT-1342819.
    STRINGi10116.ENSRNOP00000042533.

    Structurei

    3D structure databases

    ProteinModelPortaliP10687.
    SMRiP10687. Positions 18-797.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini316 – 467152PI-PLC X-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini540 – 656117PI-PLC Y-boxPROSITE-ProRule annotationAdd
    BLAST
    Domaini663 – 76199C2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
    Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG149692.
    HOGENOMiHOG000232046.
    HOVERGENiHBG053609.
    InParanoidiP10687.
    KOiK05858.
    PhylomeDBiP10687.
    TreeFamiTF313216.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    InterProiIPR000008. 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]
    PANTHERiPTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF12. PTHR10336:SF12. 1 hit.
    PfamiPF00168. 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]
    PIRSFiPIRSF000956. PLC-beta. 1 hit.
    PRINTSiPR00390. PHPHLIPASEC.
    SMARTiSM00239. C2. 1 hit.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51695. SSF51695. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P10687-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF     50
    FFYWTDQNKE TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ 100
    RMITVVYGPD LVNISHLNLV AFQEEVAKEW TNEVFSLATN LLAQNMSRDA 150
    FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA DRKRVETALE ACSLPSSRND 200
    SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL TVDQMMDFIN 250
    LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS 300
    GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR 350
    QVLLSGCRCV ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF 400
    KTSPFPILLS FENHVDSPKQ QAKMAEYCRL IFGDALLMEP LEKYPLESGV 450
    PLPSPMDLMY KILVKNKKKS HKSSEGSGKK KLSEQASNTY SDSSSVFEPS 500
    SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM SNLVNYIQPV 550
    KFESFETSKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK 600
    GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL 650
    KPEFMRRPDK HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD 700
    MFGLPVDTRR KAFKTKTSQG NAVNPVWEEE PIVFKKVVLP SLACLRIAAY 750
    EEGGKFIGHR ILPVQAIRPG YHYICLRNER NQPLMLPAVF VYIEVKDYVP 800
    DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK EADPGETSSE 850
    APSETRTTPA ENGVNHTATL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS 900
    VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT 950
    KYNEIQNDYL RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE 1000
    MTQKLIDLKD KQQQQLLNLR QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ 1050
    NNQLKKLKEI CEKEKKELKK KMDKKRQEKI TEAKSKDKSQ MEEEKTEMIR 1100
    SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP KLQMELEQEY 1150
    QDKFKRLPLE ILEFVQEAMK GKVSEDSNHG SAPPSLASDP AKVNLKSPSS 1200
    EEVQGENAGR EFDTPL 1216
    Length:1,216
    Mass (Da):138,344
    Last modified:July 1, 1989 - v1
    Checksum:i92F23691781F788E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20636 mRNA. Translation: AAA41885.1.
    PIRiA28821.
    RefSeqiNP_001071109.1. NM_001077641.1.
    UniGeneiRn.45523.

    Genome annotation databases

    GeneIDi24654.
    KEGGirno:24654.
    UCSCiRGD:3344. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20636 mRNA. Translation: AAA41885.1 .
    PIRi A28821.
    RefSeqi NP_001071109.1. NM_001077641.1.
    UniGenei Rn.45523.

    3D structure databases

    ProteinModelPortali P10687.
    SMRi P10687. Positions 18-797.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246789. 162 interactions.
    MINTi MINT-1342819.
    STRINGi 10116.ENSRNOP00000042533.

    Chemistry

    BindingDBi P10687.

    PTM databases

    PhosphoSitei P10687.

    Proteomic databases

    PaxDbi P10687.
    PRIDEi P10687.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24654.
    KEGGi rno:24654.
    UCSCi RGD:3344. rat.

    Organism-specific databases

    CTDi 23236.
    RGDi 3344. Plcb1.

    Phylogenomic databases

    eggNOGi NOG149692.
    HOGENOMi HOG000232046.
    HOVERGENi HBG053609.
    InParanoidi P10687.
    KOi K05858.
    PhylomeDBi P10687.
    TreeFami TF313216.

    Enzyme and pathway databases

    BRENDAi 3.1.4.11. 5301.
    Reactomei REACT_194690. Ca2+ pathway.
    REACT_196412. Presynaptic function of Kainate receptors.
    REACT_198661. Synthesis of IP3 and IP4 in the cytosol.
    REACT_208646. G beta:gamma signalling through PLC beta.
    REACT_221588. PLC beta mediated events.

    Miscellaneous databases

    NextBioi 603984.
    PROi P10687.

    Gene expression databases

    Genevestigatori P10687.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    2.60.40.150. 1 hit.
    3.20.20.190. 2 hits.
    InterProi IPR000008. 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 ]
    PANTHERi PTHR10336. PTHR10336. 1 hit.
    PTHR10336:SF12. PTHR10336:SF12. 1 hit.
    Pfami PF00168. 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 ]
    PIRSFi PIRSF000956. PLC-beta. 1 hit.
    PRINTSi PR00390. PHPHLIPASEC.
    SMARTi SM00239. C2. 1 hit.
    SM00148. PLCXc. 1 hit.
    SM00149. PLCYc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51695. SSF51695. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS50007. PIPLC_X_DOMAIN. 1 hit.
    PS50008. PIPLC_Y_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPLCB1_RAT
    AccessioniPrimary (citable) accession number: P10687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The receptor-mediated activation of PLC-beta-1 is mediated by two G-protein alpha subunits, alpha-Q and alpha-11.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3