P10894 (PLCB1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

PLCB1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1216 AA.
Sequence status	Complete.
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.
Cofactor	Calcium.
Subunit structure	Interacts with DGKQ By similarity.
Subcellular location	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.
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 Lipid metabolism
Cellular component	Cytoplasm Membrane Nucleus
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled acetylcholine receptor signaling pathway Inferred from electronic annotation. Source: Compara G1 phase Inferred from electronic annotation. Source: Compara activation of meiosis involved in egg activation Inferred from electronic annotation. Source: Compara cerebral cortex development Inferred from electronic annotation. Source: Compara fat cell differentiation Inferred from electronic annotation. Source: Compara glutamate receptor signaling pathway Inferred from electronic annotation. Source: Compara insulin-like growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara interleukin-1-mediated signaling pathway Inferred from electronic annotation. Source: Compara interleukin-12-mediated signaling pathway Inferred from electronic annotation. Source: Compara interleukin-15-mediated signaling pathway Inferred from electronic annotation. Source: Compara intracellular signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW memory Inferred from electronic annotation. Source: Compara negative regulation of monocyte extravasation Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara positive regulation of CD24 biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of JNK cascade Inferred from electronic annotation. Source: Compara positive regulation of acrosome reaction Inferred from electronic annotation. Source: Compara positive regulation of developmental growth Inferred from electronic annotation. Source: Compara positive regulation of embryonic development Inferred from electronic annotation. Source: Compara positive regulation of interleukin-12 production Inferred from electronic annotation. Source: Compara positive regulation of myoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara regulation of G-protein coupled receptor protein signaling pathway Inferred from electronic annotation. Source: Compara regulation of fertilization Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear chromatin Inferred from electronic annotation. Source: Compara nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear speck Inferred from electronic annotation. Source: Compara
Molecular_function	GTPase activator activity Inferred from electronic annotation. Source: Compara calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol phospholipase C activity Inferred from electronic annotation. Source: EC phosphatidylinositol-4,5-bisphosphate binding Inferred from electronic annotation. Source: Compara 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_0000088485
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	887	1	Phosphoserine; by PKC Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P10894 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: BEF809177F1B7ABB	FASTA	1,216	138,715
	10 20 30 40 50 60 MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WEDDSTVVTP IILRTDPQGF FFYWTDQNKE 70 80 90 100 110 120 TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGRLEH RMITVVYGPD LVNISHLNLV 130 140 150 160 170 180 AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA 190 200 210 220 230 240 DRKRVETALE ACSLPSSRND SIPQEDFTPE VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL 250 260 270 280 290 300 TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NNSLAKKGQI 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 LDKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK 490 500 510 520 530 540 KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM 550 560 570 580 590 600 SNLVNYIQPV KFESFEISKK RNRSFEMSSF 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 NAVNPIWEEE PIVFKKVVLP SLACLRIAVY EEGGKFIGHR ILPVQAIRPG YHYICLRNER 790 800 810 820 830 840 NQPLMLPALF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK 850 860 870 880 890 900 EADPGETPSE APSEARPTPA ENGVNHTTSL TPKPPSQALH SQPAPGSVKA PAKTEDLIQS 910 920 930 940 950 960 VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTDLIKEHTT KYNEIQNDYL 970 980 990 1000 1010 1020 RRRAALEKTA KKDNKKKSEP SSPDHVSSTI EQDLAALDAE MTQKLVDLKD 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 KLQVELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHS SAPPLMTSDS GKLNQKPPSS 1210 EELEGENPGK EFDTPL

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03137 mRNA. Translation: AAA30702.1.
IPI	IPI00691479.
PIR	A28822.
RefSeq	NP_777242.1. NM_174817.1.
UniGene	Bt.448.
3D structure databases
ProteinModelPortal	P10894.
SMR	P10894. Positions 18-797.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-144720.
STRING	9913.ENSBTAP00000046644.
Proteomic databases
PRIDE	P10894.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000049812; ENSBTAP00000046644; ENSBTAG00000008338.
GeneID	287026.
KEGG	bta:287026.
Organism-specific databases
CTD	23236.
Phylogenomic databases
eggNOG	NOG149692.
GeneTree	ENSGT00700000104415.
HOGENOM	HOG000232046.
HOVERGEN	HBG053609.
InParanoid	P10894.
KO	K05858.
OMA	YRVFLNN.
OrthoDB	EOG40S0DW.
Enzyme and pathway databases
BioCyc	CATTLE:287026-MONOMER.
Reactome	REACT_114534. Signal Transduction.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 3.20.20.190. 2 hits.
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR001192. Pinositol_PLipase_C. IPR016280. PLC-beta. 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]
PANTHER	PTHR10336. PTHR10336. 1 hit.
Pfam	PF06631. DUF1154. 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.
SMART	SM00239. C2. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20806548.

Entry information

Entry name

PLCB1_BOVIN

Accession

Primary (citable) accession number: P10894

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 29, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program