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P51432 (PLCB3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1234 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subunit structure

Interacts with SHANK2 and LPAR2 By similarity.

Subcellular location

Nucleus Ref.1.

Tissue specificity

Highly expressed in kidney, skeletal muscle, liver, lung, heart and brain.

Sequence similarities

Contains 1 C2 domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Ontologies

Keywords
   Biological processLipid degradation
   Cellular componentNucleus
   LigandCalcium
   Molecular functionHydrolase
Transducer
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processintracellular signal transduction

Inferred from electronic annotation. Source: InterPro

lipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

phosphatidylinositol phospholipase C activity

Inferred from electronic annotation. Source: EC

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 123412331-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
PRO_0000088492

Regions

Domain318 – 468151PI-PLC X-box
Domain591 – 707117PI-PLC Y-box
Domain714 – 81198C2
Region1231 – 12344Interaction with SHANK2 By similarity

Sites

Active site3321 By similarity
Active site3791 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue5371Phosphoserine By similarity
Modified residue9271Phosphoserine By similarity
Modified residue9321Phosphoserine By similarity
Modified residue9351Phosphoserine By similarity
Modified residue11221Phosphothreonine By similarity

Experimental info

Sequence conflict161P → S in AAA85199. Ref.1
Sequence conflict201E → K in AAA85199. Ref.1
Sequence conflict6091A → S in AAA85199. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51432 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: E055744A33C5F6B0

FASTA1,234139,487
        10         20         30         40         50         60 
MAGARPGVHA LQLEPPTVVE TLRRGSKFIK WDEEASSRNL VTLRVDPNGF FLYWTGPNME 

        70         80         90        100        110        120 
VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDTRLE EKLMTVVAGP DPVNTTFLNF 

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

       190        200        210        220        230        240 
ADKKRVETAL ESCGLNFNRS ESIRPDEFPL EIFERFLNKL CLRPDIDKIL LEIGAKGKPY 

       250        260        270        280        290        300 
LTLEQLMDFI NQKQRDPRLN EVLYPPLRSS QARLLIEKYE TNKQFLERDQ MSMEGFSRYL 

       310        320        330        340        350        360 
GGEENGILPL EALDLSMDMT QPLSAYFINS SHNTYLTAGQ LAGPSSVEMY RQALLWGCRC 

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

       430        440        450        460        470        480 
QQAKMAEYCR SIFGDALLID PLDKYPLSAG IPLPSPQDLM GRILVKNKKR HRPSTGVPDS 

       490        500        510        520        530        540 
SVRKRPLEQS NSALSESSAA TEPSSPQLGS PSSDSCPGLS NGEEVGLEKT SLEPQKSLGE 

       550        560        570        580        590        600 
ESLSREPNVP MPDRDREDEE EDEEEEETTD PKKPTTDEGT ASSEVNATEE MSTLVNYVEP 

       610        620        630        640        650        660 
VKFKSFEAAR KRNKCFEMSS FVETKAMEQL TKSPMEFVEY NKQQLSRIYP KGTRVDSSNY 

       670        680        690        700        710        720 
MPQLFWNVGC QLVALNFQTL DLPMQLNAGV FEYNGRSGYL LKPEFMRRPD KSFDPFTEVI 

       730        740        750        760        770        780 
VDGIVANALR VKVISGQFLS DKKVGIYVEV DMFGLPVDTR RKYRTRTSQG NSFNPVWDEE 

       790        800        810        820        830        840 
PFDFPKVVLP TLASLRIAAF EEGGKFVGHR ILPVSAIRSG YHYVCLRNEA NQPLCLPALL 

       850        860        870        880        890        900 
IYTEASDYIP DDHQDYAEAL INPIKHVSLM DQRAKQLAAL IGESEAQAST ETYQETPCQQ 

       910        920        930        940        950        960 
PGSQLPSNPT PNPLDASPRW PPGPTTSSTS SSLSSPGQRD DLIASILSEV TPTPLEELRS 

       970        980        990       1000       1010       1020 
HKAMVKLRSR QDRDLRELHK KHQRKAVALT RRLLDGLAQA RAEGKCRPSP SALGKATNSE 

      1030       1040       1050       1060       1070       1080 
DVKEEEEAKQ YREFQNRQVQ SLLELREAQA DVETKRKLEH LRQAHQRLKE VVLDTHTTQF 

      1090       1100       1110       1120       1130       1140 
KRLKELNERE KKELQKILDR KRNNSISEAK TREKHKKEVE LTEINRRHIT ESVNSIRRLE 

      1150       1160       1170       1180       1190       1200 
EAQKQRHERL VAGQQQVLQQ LEEEEPKLLA QLTQECQEQR ERLPQEIRRC LLGETAEGLG 

      1210       1220       1230 
DGPLVACASN GHAPGSGGHL SSADSESQEE NTQL

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a cDNA encoding mouse phospholipase C-beta3."
Wang S., Zhou Y., Lukinius A., Oberg K., Skogseid B., Gobl A.
Biochim. Biophys. Acta 1393:173-178(1998) [PubMed: 9714794] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Strain: BALB/c.
Tissue: Kidney.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U43144 mRNA. Translation: AAA85199.1.
AK146793 mRNA. Translation: BAE27436.1.
CH466612 Genomic DNA. Translation: EDL33267.1.
IPIIPI00311203.
UniGeneMm.273204.

3D structure databases

ProteinModelPortalP51432.
SMRP51432. Positions 12-883.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-126696.
STRINGP51432.

PTM databases

PhosphoSiteP51432.

Proteomic databases

PRIDEP51432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025912; ENSMUSP00000025912; ENSMUSG00000024960.

Organism-specific databases

MGIMGI:104778. Plcb3.

Phylogenomic databases

eggNOGroNOG12610.
HOGENOMHBG315986.
HOVERGENHBG053609.
InParanoidP51432.
OrthoDBEOG41RPT7.
PhylomeDBP51432.

Gene expression databases

ArrayExpressP51432.
BgeeP51432.
CleanExMM_PLCB3.
GenevestigatorP51432.
GermOnlineENSMUSG00000024960. Mus musculus.

Family and domain databases

InterProIPR000008. 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]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 2 hits.
PfamPF00168. 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]
PIRSFPIRSF000956. PLC-beta. 1 hit.
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry namePLCB3_MOUSE
AccessionPrimary (citable) accession number: P51432
Secondary accession number(s): Q3UIS0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: November 16, 2011
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents