1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3

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Reviewed, UniProtKB/Swiss-Prot Q01970 (PLCB3_HUMAN)

Last modified February 9, 2010. Version 97. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
    EC=3.1.4.11
Alternative name(s):
    Phosphoinositide phospholipase C-beta-3
    Phospholipase C-beta-3
      Short name=PLC-beta-3

Gene names

Name:

PLCB3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	1234 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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 SHANK2 By similarity. Interacts with LPAR2. Ref.6
Subcellular location	Membrane; Peripheral membrane protein.
Sequence similarities	Contains 1 C2 domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain.

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Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from Experiment. Source: Reactome extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide phospholipase C activity Inferred from electronic annotation. Source: EC signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 1234

1233

1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3

PRO_0000088491

Regions

Domain

318 – 468

151

PI-PLC X-box

Domain

590 – 706

117

PI-PLC Y-box

Domain

713 – 810

Region

1231 – 1234

Interaction with SHANK2 By similarity

Sites

Active site

332

By similarity

Active site

379

By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.11

Modified residue

537

Phosphoserine Ref.7 Ref.9

Modified residue

926

Phosphoserine Ref.9

Modified residue

931

Phosphoserine Ref.9

Modified residue

934

Phosphoserine Ref.9

Modified residue

1122

Phosphothreonine Ref.8

Natural variations

Natural variant

483

R → H: dbSNP rs12146487.

VAR_029229

Experimental info

Sequence conflict

845

S → L in CAA78903. Ref.5

Sequence conflict

881

G → E in CAA85776. Ref.2

Sequence conflict

1089 – 1119

REKKE…HKKEA → SWPSWPRSVRSSGRGSPRRS AGACWARCRRG in CAA85776. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q01970-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: C5106EFBA8037788
Show »

FASTA

1,234

138,799

        10         20         30         40         50         60 
MAGAQPGVHA LQLEPPTVVE TLRRGSKFIK WDEETSSRNL VTLRVDPNGF FLYWTGPNME 

        70         80         90        100        110        120 
VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDARLE EKLMTVVSGP DPVNTVFLNF 

       130        140        150        160        170        180 
MAVQDDTAKV WSEELFKLAM NILAQNASRN TFLRKAYTKL KLQVNQDGRI PVKNILKMFS 

       190        200        210        220        230        240 
ADKKRVETAL ESCGLKFNRS ESIRPDEFSL EIFERFLNKL CLRPDIDKIL LEIGAKGKPY 

       250        260        270        280        290        300 
LTLEQLMDFI NQKQRDPRLN EVLYPPLRPS QARLLIEKYE PNQQFLERDQ MSMEGFSRYL 

       310        320        330        340        350        360 
GGEENGILPL EALDLSTDMT QPLSAYFINS SHNTYLTAGQ LAGTSSVEMY RQALLWGCRC 

       370        380        390        400        410        420 
VELDVWKGRP PEEEPFITHG FTMTTEVPLR DVLEAIAETA FKTSPYPVIL SFENHVDSAK 

       430        440        450        460        470        480 
QQAKMAEYCR SIFGDALLIE PLDKYPLAPG VPLPSPQDLM GRILVKNKKR HRPSAGGPDS 

       490        500        510        520        530        540 
AGRKRPLEQS NSALSESSAA TEPSSPQLGS PSSDSCPGLS NGEEVGLEKP SLEPQKSLGD 

       550        560        570        580        590        600 
EGLNRGPYVL GPADREDEEE DEEEEEQTDP KKPTTDEGTA SSEVNATEEM STLVNYIEPV 

       610        620        630        640        650        660 
KFKSFEAARK RNKCFEMSSF VETKAMEQLT KSPMEFVEYN KQQLSRIYPK GTRVDSSNYM 

       670        680        690        700        710        720 
PQLFWNVGCQ LVALNFQTLD VAMQLNAGVF EYNGRSGYLL KPEFMRRPDK SFDPFTEVIV 

       730        740        750        760        770        780 
DGIVANALRV KVISGQFLSD RKVGIYVEVD MFGLPVDTRR KYRTRTSQGN SFNPVWDEEP 

       790        800        810        820        830        840 
FDFPKVVLPT LASLRIAAFE EGGKFVGHRI LPVSAIRSGY HYVCLRNEAN QPLCLPALLI 

       850        860        870        880        890        900 
YTEASDYIPD DHQDYAEALI NPIKHVSLMD QRARQLAALI GESEAQAGQE TCQDTQSQQL 

       910        920        930        940        950        960 
GSQPSSNPTP SPLDASPRRP PGPTTSPAST SLSSPGQRDD LIASILSEVA PTPLDELRGH 

       970        980        990       1000       1010       1020 
KALVKLRSRQ ERDLRELRKK HQRKAVTLTR RLLDGLAQAQ AEGRCRLRPG ALGGAADVED 

      1030       1040       1050       1060       1070       1080 
TKEGEDEAKR YQEFQNRQVQ SLLELREAQV DAEAQRRLEH LRQALQRLRE VVLDANTTQF 

      1090       1100       1110       1120       1130       1140 
KRLKEMNERE KKELQKILDR KRHNSISEAK MRDKHKKEAE LTEINRRHIT ESVNSIRRLE 

      1150       1160       1170       1180       1190       1200 
EAQKQRHDRL VAGQQQVLQQ LAEEEPKLLA QLAQECQEQR ARLPQEIRRS LLGEMPEGLG 

      1210       1220       1230 
DGPLVACASN GHAPGSSGHL SGADSESQEE NTQL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural organization and expression of the human phosphatidylinositol-specific phospholipase C beta-3 gene." Mazuruk K., Schoen T.J., Chader G.J., Rodriguez I.R. Biochem. Biophys. Res. Commun. 212:190-195(1995) [PubMed: 7612006] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genomic organization and complete cDNA sequence of the human phosphoinositide-specific phospholipase C beta 3 gene (PLCB3)." Lagercrantz J., Carson E., Phelan C., Grimmond S., Rosen A., Dare E., Nordenskjoeld M., Hayward N.K., Larsson C., Weber G. Genomics 26:467-472(1995) [PubMed: 7607669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily." Carozzi A.J., Kriz R.W., Webster C., Parker P.J. Eur. J. Biochem. 210:521-529(1992) [PubMed: 1333955] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 184-1234.
[6]	"NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-beta3 activation." Oh Y.-S., Jo N.W., Choi J.W., Kim H.S., Seo S.-W., Kang K.-O., Hwang J.-I., Heo K., Kim S.-H., Kim Y.-H., Kim I.-H., Kim J.H., Banno Y., Ryu S.H., Suh P.-G. Mol. Cell. Biol. 24:5069-5079(2004) [PubMed: 15143197] [Abstract] Cited for: INTERACTION WITH LPAR2.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1122, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537; SER-926; SER-931 AND SER-934, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	U26425 Genomic DNA. Translation: AAA77683.1. Z37544 Z37574 Genomic DNA. Translation: CAA85776.1. CH471076 Genomic DNA. Translation: EAW74230.1. BC142681 mRNA. Translation: AAI42682.1. Z16411 mRNA. Translation: CAA78903.1.
IPI	IPI00010400.
PIR	I38994. S27002. S52099.
RefSeq	NP_000923.1.
UniGene	Hs.591953
3D structure databases
SMR	Q01970. Positions 16-846, 946-1198.
ModBase	Search...
Protein-protein interaction databases
STRING	Q01970.
PTM databases
PhosphoSite	Q01970.
Proteomic databases
PRIDE	Q01970.
Genome annotation databases
Ensembl	ENST00000279230; ENSP00000279230; ENSG00000149782; Homo sapiens. [Genome view]
GeneID	5331.
KEGG	hsa:5331.
UCSC	uc001nzb.2. human.
Organism-specific databases
CTD	5331.
GeneCards	GC11P063775.
H-InvDB	HIX0009758.
HGNC	HGNC:9056. PLCB3.
HPA	CAB009257.
MIM	600230. gene.
PharmGKB	PA33386.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG19477.
HOGENOM	HBG315986.
HOVERGEN	Q01970.
InParanoid	Q01970.
OMA	KEMNERE.
PhylomeDB	Q01970.
Enzyme and pathway databases
BRENDA	3.1.4.11. 247.
Pathway_Interaction_DB	lysophospholipid_pathway. LPA receptor mediated events.
Reactome	REACT_14797. Signaling by GPCR. REACT_15295. Opioid Signalling. REACT_15380. Diabetes pathways.
Gene expression databases
ArrayExpress	Q01970.
Bgee	Q01970.
CleanEx	HS_PLCB3.
Genevestigator	Q01970.
GermOnline	ENSG00000149782. Homo sapiens.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR016280. PLC-beta. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR000909. PLipase_C_PInositol-sp_X_dom. [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. [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]
PROSITE	PS50004. C2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	20644.
SOURCE	Search...

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Entry information

Entry name

PLCB3_HUMAN

Accession

Primary (citable) accession number: Q01970
Secondary accession number(s): A5PKZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 1, 1996
Last modified:	February 9, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents