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P10894

- PLCB1_BOVIN

UniProt

P10894 - PLCB1_BOVIN

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Protein

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

Gene

PLCB1

Organism
Bos taurus (Bovine)
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.

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: InterPro
  2. GTPase activator activity Source: Ensembl
  3. phosphatidylinositol-4,5-bisphosphate binding Source: Ensembl
  4. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
  5. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of meiosis involved in egg activation Source: Ensembl
  2. cerebral cortex development Source: Ensembl
  3. fat cell differentiation Source: Ensembl
  4. glutamate receptor signaling pathway Source: Ensembl
  5. G-protein coupled acetylcholine receptor signaling pathway Source: Ensembl
  6. insulin-like growth factor receptor signaling pathway Source: Ensembl
  7. interleukin-12-mediated signaling pathway Source: Ensembl
  8. interleukin-15-mediated signaling pathway Source: Ensembl
  9. interleukin-1-mediated signaling pathway Source: Ensembl
  10. intracellular signal transduction Source: InterPro
  11. lipid catabolic process Source: UniProtKB-KW
  12. memory Source: Ensembl
  13. negative regulation of monocyte extravasation Source: Ensembl
  14. negative regulation of transcription, DNA-templated Source: Ensembl
  15. positive regulation of acrosome reaction Source: Ensembl
  16. positive regulation of CD24 biosynthetic process Source: Ensembl
  17. positive regulation of developmental growth Source: Ensembl
  18. positive regulation of embryonic development Source: Ensembl
  19. positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  20. positive regulation of interleukin-12 production Source: Ensembl
  21. positive regulation of JNK cascade Source: Ensembl
  22. positive regulation of myoblast differentiation Source: Ensembl
  23. positive regulation of transcription, DNA-templated Source: Ensembl
  24. regulation of fertilization Source: Ensembl
  25. regulation of G-protein coupled receptor protein signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_202864. Acetylcholine regulates insulin secretion.
REACT_209521. G alpha (q) signalling events.
REACT_209727. Ca2+ pathway.
REACT_213422. PLC beta mediated events.
REACT_216130. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
REACT_217228. Presynaptic function of Kainate receptors.
REACT_224596. G beta:gamma signalling through PLC beta.
REACT_225102. Synthesis of IP3 and IP4 in the cytosol.

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-beta-1
Short name:
PLC-beta-1
Gene namesi
Name:PLCB1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 13

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: AgBase
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: Ensembl
  4. membrane Source: UniProtKB-KW
  5. nuclear chromatin Source: Ensembl
  6. nuclear speck Source: Ensembl
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_0000088485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei887 – 8871Phosphoserine; by PKC1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP10894.

Interactioni

Subunit structurei

Interacts with DGKQ.By similarity

Protein-protein interaction databases

BioGridi160009. 1 interaction.
MINTiMINT-144720.
STRINGi9913.ENSBTAP00000046644.

Structurei

3D structure databases

ProteinModelPortaliP10894.
SMRiP10894. 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.
GeneTreeiENSGT00760000118936.
HOGENOMiHOG000232046.
HOVERGENiHBG053609.
InParanoidiP10894.
KOiK05858.
OMAiMMDFINL.
OrthoDBiEOG7WDN1N.
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.
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]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF12. PTHR10336:SF12. 1 hit.
PfamiPF06631. DUF1154. 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.

P10894-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WEDDSTVVTP IILRTDPQGF
60 70 80 90 100
FFYWTDQNKE TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGRLEH
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
SIPQEDFTPE VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL TVDQMMDFIN
260 270 280 290 300
LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NNSLAKKGQI 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 LDKYPLESGV
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
KFESFEISKK RNRSFEMSSF 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 NAVNPIWEEE PIVFKKVVLP SLACLRIAVY
760 770 780 790 800
EEGGKFIGHR ILPVQAIRPG YHYICLRNER NQPLMLPALF VYIEVKDYVP
810 820 830 840 850
DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK EADPGETPSE
860 870 880 890 900
APSEARPTPA ENGVNHTTSL TPKPPSQALH SQPAPGSVKA PAKTEDLIQS
910 920 930 940 950
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTDLIKEHTT
960 970 980 990 1000
KYNEIQNDYL RRRAALEKTA KKDNKKKSEP SSPDHVSSTI EQDLAALDAE
1010 1020 1030 1040 1050
MTQKLVDLKD KQQQQLLNLR QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ
1060 1070 1080 1090 1100
NNQLKKLKEI CEKEKKELKK KMDKKRQEKI TEAKSKDKSQ MEEEKTEMIR
1110 1120 1130 1140 1150
SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP KLQVELEQEY
1160 1170 1180 1190 1200
QDKFKRLPLE ILEFVQEAMK GKISEDSNHS SAPPLMTSDS GKLNQKPPSS
1210
EELEGENPGK EFDTPL
Length:1,216
Mass (Da):138,715
Last modified:July 1, 1989 - v1
Checksum:iBEF809177F1B7ABB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03137 mRNA. Translation: AAA30702.1.
PIRiA28822.
RefSeqiNP_777242.1. NM_174817.1.
UniGeneiBt.448.

Genome annotation databases

EnsembliENSBTAT00000049812; ENSBTAP00000046644; ENSBTAG00000008338.
GeneIDi287026.
KEGGibta:287026.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03137 mRNA. Translation: AAA30702.1 .
PIRi A28822.
RefSeqi NP_777242.1. NM_174817.1.
UniGenei Bt.448.

3D structure databases

ProteinModelPortali P10894.
SMRi P10894. Positions 18-797.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 160009. 1 interaction.
MINTi MINT-144720.
STRINGi 9913.ENSBTAP00000046644.

Proteomic databases

PRIDEi P10894.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000049812 ; ENSBTAP00000046644 ; ENSBTAG00000008338 .
GeneIDi 287026.
KEGGi bta:287026.

Organism-specific databases

CTDi 23236.

Phylogenomic databases

eggNOGi NOG149692.
GeneTreei ENSGT00760000118936.
HOGENOMi HOG000232046.
HOVERGENi HBG053609.
InParanoidi P10894.
KOi K05858.
OMAi MMDFINL.
OrthoDBi EOG7WDN1N.
TreeFami TF313216.

Enzyme and pathway databases

Reactomei REACT_202864. Acetylcholine regulates insulin secretion.
REACT_209521. G alpha (q) signalling events.
REACT_209727. Ca2+ pathway.
REACT_213422. PLC beta mediated events.
REACT_216130. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
REACT_217228. Presynaptic function of Kainate receptors.
REACT_224596. G beta:gamma signalling through PLC beta.
REACT_225102. Synthesis of IP3 and IP4 in the cytosol.

Miscellaneous databases

NextBioi 20806548.

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.
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 ]
PANTHERi PTHR10336. PTHR10336. 1 hit.
PTHR10336:SF12. PTHR10336:SF12. 1 hit.
Pfami PF06631. DUF1154. 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. "Determination of the primary structure of PLC-154 demonstrates diversity of phosphoinositide-specific phospholipase C activities."
    Katan M., Kriz R.W., Totty N., Philp R., Meldrum E., Aldape R.A., Knopf J.L., Parker P.J.
    Cell 54:171-177(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Feedback regulation of phospholipase C-beta by protein kinase C."
    Ryu S.H., Kim U.H., Wahl M.I., Brown A.B., Carpenter G., Huang K.P., Rhee S.G.
    J. Biol. Chem. 265:17941-17945(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 879-889, PHOSPHORYLATION AT SER-887.

Entry informationi

Entry nameiPLCB1_BOVIN
AccessioniPrimary (citable) accession number: P10894
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 126 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3