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P10687

- PLCB1_RAT

UniProt

P10687 - PLCB1_RAT

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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

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

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 homodimerization activity Source: RGD
  4. 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BRENDAi3.1.4.11. 5301.

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 speck Source: BHF-UCL
  5. nucleus Source: BHF-UCL
Complete GO annotation...

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

        10         20         30         40         50
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF
60 70 80 90 100
FFYWTDQNKE TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ
110 120 130 140 150
RMITVVYGPD LVNISHLNLV AFQEEVAKEW TNEVFSLATN LLAQNMSRDA
160 170 180 190 200
FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA DRKRVETALE ACSLPSSRND
210 220 230 240 250
SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL TVDQMMDFIN
260 270 280 290 300
LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS
310 320 330 340 350
GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR
360 370 380 390 400
QVLLSGCRCV ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF
410 420 430 440 450
KTSPFPILLS FENHVDSPKQ QAKMAEYCRL IFGDALLMEP LEKYPLESGV
460 470 480 490 500
PLPSPMDLMY KILVKNKKKS HKSSEGSGKK KLSEQASNTY SDSSSVFEPS
510 520 530 540 550
SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM SNLVNYIQPV
560 570 580 590 600
KFESFETSKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
610 620 630 640 650
GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL
660 670 680 690 700
KPEFMRRPDK HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD
710 720 730 740 750
MFGLPVDTRR KAFKTKTSQG NAVNPVWEEE PIVFKKVVLP SLACLRIAAY
760 770 780 790 800
EEGGKFIGHR ILPVQAIRPG YHYICLRNER NQPLMLPAVF VYIEVKDYVP
810 820 830 840 850
DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK EADPGETSSE
860 870 880 890 900
APSETRTTPA ENGVNHTATL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS
910 920 930 940 950
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT
960 970 980 990 1000
KYNEIQNDYL RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE
1010 1020 1030 1040 1050
MTQKLIDLKD KQQQQLLNLR QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ
1060 1070 1080 1090 1100
NNQLKKLKEI CEKEKKELKK KMDKKRQEKI TEAKSKDKSQ MEEEKTEMIR
1110 1120 1130 1140 1150
SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP KLQMELEQEY
1160 1170 1180 1190 1200
QDKFKRLPLE ILEFVQEAMK GKVSEDSNHG SAPPSLASDP AKVNLKSPSS
1210
EEVQGENAGR EFDTPL
Length:1,216
Mass (Da):138,344
Last modified:July 1, 1989 - v1
Checksum:i92F23691781F788E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20636 mRNA. Translation: AAA41885.1.
PIRiA28821.
RefSeqiNP_001071109.1. NM_001077641.1.
XP_008760469.1. XM_008762247.1.
UniGeneiRn.45523.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20636 mRNA. Translation: AAA41885.1 .
PIRi A28821.
RefSeqi NP_001071109.1. NM_001077641.1.
XP_008760469.1. XM_008762247.1.
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.

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.

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: November 26, 2014
This is version 140 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