Reviewed, UniProtKB/Swiss-Prot P10687 (PLCB1_RAT)

Names and origin

Protein names

Recommended name:
    1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
    EC=3.1.4.11
Alternative name(s):
    Phosphoinositide phospholipase C
    Phospholipase C-beta-1
      Short name=PLC-beta-1
    PLC-I
    PLC-154

Gene names

Name:

Plcb1

Organism

Rattus norvegicus (Rat)

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	1216 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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.
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol. Ref.2
Cofactor	Calcium.
Subunit structure	Interacts with DGKQ By similarity.
Subcellular location	Cytoplasm. Membrane. Note: And particulate fractions. Ref.2
Tissue specificity	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. Ref.2
Miscellaneous	The receptor-mediated activation of PLC-beta-1 is mediated by two G-protein alpha subunits, alpha-Q and alpha-11.
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
Cellular component	Cytoplasm Membrane
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro learning Inferred from expression pattern. Source: RGD lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW memory Inferred from expression pattern. Source: RGD oxygen and reactive oxygen species metabolic process Inferred from expression pattern. Source: RGD phosphoinositide metabolic process Inferred from expression pattern. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Inferred from direct assay. Source: RGD
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide phospholipase C activity Inferred from direct assay. Source: RGD protein binding Inferred from physical interaction. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1216	1216	1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1		PRO_0000088488
Regions
	Domain	316 – 467	152	PI-PLC X-box
	Domain	540 – 656	117	PI-PLC Y-box
	Domain	663 – 761	99	C2
Sites
	Active site	331	1	By similarity
	Active site	378	1	By similarity
Amino acid modifications
	Modified residue	333	1	Phosphothreonine By similarity
	Modified residue	334	1	Phosphotyrosine By similarity
	Modified residue	336	1	Phosphothreonine By similarity
	Modified residue	569	1	Phosphoserine By similarity
	Modified residue	573	1	Phosphothreonine By similarity
	Modified residue	887	1	Phosphoserine; by PKC By similarity
	Modified residue	972	1	N6-acetyllysine By similarity
	Modified residue	976	1	N6-acetyllysine By similarity
	Modified residue	1197	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P10687-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 92F23691781F788E	FASTA	1,216	138,344
	10 20 30 40 50 60 MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE 70 80 90 100 110 120 TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV 130 140 150 160 170 180 AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA 190 200 210 220 230 240 DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL 250 260 270 280 290 300 TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS 310 320 330 340 350 360 GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV 370 380 390 400 410 420 ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ 430 440 450 460 470 480 QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK 490 500 510 520 530 540 KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM 550 560 570 580 590 600 SNLVNYIQPV KFESFETSKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK 610 620 630 640 650 660 GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK 670 680 690 700 710 720 HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG 730 740 750 760 770 780 NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER 790 800 810 820 830 840 NQPLMLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK 850 860 870 880 890 900 EADPGETSSE APSETRTTPA ENGVNHTATL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS 910 920 930 940 950 960 VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL 970 980 990 1000 1010 1020 RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR 1030 1040 1050 1060 1070 1080 QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI 1090 1100 1110 1120 1130 1140 TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP 1150 1160 1170 1180 1190 1200 KLQMELEQEY QDKFKRLPLE ILEFVQEAMK GKVSEDSNHG SAPPSLASDP AKVNLKSPSS 1210 EEVQGENAGR EFDTPL

References

[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: 3390863] [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: 8454637] [Abstract] Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M20636 mRNA. Translation: AAA41885.1.
IPI	IPI00192534.
PIR	A28821.
RefSeq	NP_001071109.1.
UniGene	Rn.45523
3D structure databases
HSSP	HSSP built from PDB template 1DJX based on UniProtKB P10688.
ModBase	Search...
Protein-protein interaction databases
STRING	P10687.
PTM databases
PhosphoSite	P10687.
Genome annotation databases
Ensembl	ENSRNOT00000051184; ENSRNOP00000042533; ENSRNOG00000004810; Rattus norvegicus. [Genome view]
GeneID	24654.
KEGG	rno:24654.
UCSC	M20636. rat.
Organism-specific databases
CTD	24654.
RGD	3344. Plcb1.
Phylogenomic databases
HOVERGEN	P10687.
OMA	EDMSQPL.
Enzyme and pathway databases
BRENDA	3.1.4.11. 248.
Gene expression databases
Genevestigator	P10687.
GermOnline	ENSRNOG00000004810. Rattus norvegicus.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR018029. C2_membr_targeting. IPR011992. EF-Hand_type. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR000909. Phospholipase_C_Pinositol-sp_X. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR016280. PLC-beta. IPR014815. PLC-beta_C. IPR017946. PLC-like_Pdiesterase_TIM-brl. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 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.
ProDom	PD001202. PI_PLC_Y. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00239. C2. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
PROSITE	PS50004. C2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	603984.

Entry information

Entry name

PLCB1_RAT

Accession

Primary (citable) accession number: P10687

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	November 3, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)