Q01970 (PLCB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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

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.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW synaptic transmission Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro calmodulin binding Inferred from physical interaction. Source: BHF-UCL phosphatidylinositol phospholipase C activity Traceable author statement. Source: Reactome 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

Initiator methionine

1

1

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

98

C2

Region

1231 – 1234

4

Interaction with SHANK2 By similarity

Sites

Active site

332

1

By similarity

Active site

379

1

By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10

Modified residue

537

1

Phosphoserine Ref.7 Ref.9

Modified residue

926

1

Phosphoserine Ref.9

Modified residue

931

1

Phosphoserine Ref.9

Modified residue

934

1

Phosphoserine Ref.9

Modified residue

1122

1

Phosphothreonine Ref.8

Natural variations

Natural variant

483

1

R → H.
Corresponds to variant rs12146487 [ dbSNP | Ensembl ].

VAR_029229

Experimental info

Sequence conflict

845

1

S → L in CAA78903. Ref.5

Sequence conflict

881

1

G → E in CAA85776. Ref.2

Sequence conflict

1089 – 1119

31

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

Secondary structure

1

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1234

Helix Strand Turn

Details...

Helix

20 – 23

4

Beta strand

27 – 31

5

Beta strand

40 – 45

6

Beta strand

51 – 55

5

Beta strand

62 – 65

4

Helix

66 – 68

3

Beta strand

71 – 73

3

Helix

84 – 88

5

Beta strand

103 – 108

6

Helix

112 – 114

3

Beta strand

116 – 126

11

Helix

127 – 140

14

Helix

142 – 145

4

Helix

149 – 162

14

Helix

172 – 177

6

Helix

180 – 182

3

Helix

183 – 191

9

Helix

205 – 207

3

Helix

210 – 220

11

Helix

224 – 232

9

Helix

243 – 253

11

Turn

261 – 263

3

Helix

269 – 279

11

Helix

283 – 287

5

Turn

297 – 299

3

Helix

310 – 313

4

Helix

323 – 325

3

Beta strand

326 – 328

3

Beta strand

331 – 333

3

Helix

348 – 355

8

Beta strand

360 – 366

7

Helix

389 – 399

11

Beta strand

408 – 415

8

Helix

421 – 432

12

Turn

456 – 459

4

Beta strand

463 – 466

4

Helix

588 – 591

4

Helix

605 – 611

7

Beta strand

616 – 621

6

Helix

622 – 631

10

Helix

633 – 642

10

Beta strand

645 – 648

4

Helix

662 – 665

4

Helix

681 – 686

6

Helix

703 – 705

3

Beta strand

726 – 734

9

Beta strand

746 – 752

7

Turn

755 – 757

3

Beta strand

781 – 787

7

Helix

789 – 791

3

Beta strand

793 – 799

7

Beta strand

809 – 812

4

Turn

813 – 815

3

Beta strand

821 – 826

6

Beta strand

832 – 846

15

Helix

850 – 852

3

Helix

853 – 860

8

Helix

862 – 875

14

Turn

876 – 879

4

Sequences

	Sequence		Length	Mass (Da)
	Q01970 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: C5106EFBA8037788	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

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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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: Cervix carcinoma.
[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: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[10]	"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. Tissue: Embryonic kidney.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U26425 Genomic DNA. Translation: AAA77683.1.
Z37544 , Z37545, Z37546, Z37547, Z37548, Z37549, Z37550, Z37551, Z37552, Z37553, Z37554, Z37555, Z37556, Z37557, Z37558, Z37559, Z37560, Z37561, Z37562, Z37564, Z37565, Z37566, Z37567, Z37568, Z37569, Z37570, Z37571, Z37572, Z37573, 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. NM_000932.2.

UniGene

Hs.523761.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OHM	X-ray	2.70	B	10-886	[»]

ProteinModelPortal

Q01970.

SMR

Q01970. Positions 12-882.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41928N.

MINT

MINT-4999151.

STRING

Q01970.

PTM databases

PhosphoSite

Q01970.

Polymorphism databases

DMDM

1730573.

Proteomic databases

PRIDE

Q01970.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000279230; ENSP00000279230; ENSG00000149782.

GeneID

5331.

KEGG

hsa:5331.

UCSC

uc001nzb.2. human.

Organism-specific databases

CTD

5331.

GeneCards

GC11P064019.

H-InvDB

HIX0009758.

HGNC

HGNC:9056. PLCB3.

HPA

CAB009257.

MIM

600230. gene.

neXtProt

NX_Q01970.

PharmGKB

PA33386.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19477.

GeneTree

ENSGT00600000084213.

HOGENOM

HBG315986.

HOVERGEN

HBG053609.

InParanoid

Q01970.

OMA

KEMNERE.

PhylomeDB

Q01970.

Enzyme and pathway databases

BRENDA

3.1.4.11. 2681.

Pathway_Interaction_DB

lysophospholipid_pathway. LPA receptor mediated events.

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_13685. Neuronal System.

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.
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]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 2 hits.

KO

K05858.

Pfam

PF00168. C2. 1 hit.
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

20644.

SOURCE

Search...

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:	January 25, 2012
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.