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Reviewed, UniProtKB/Swiss-Prot Q15147 (PLCB4_HUMAN)

Last modified November 25, 2008. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
    EC=3.1.4.11
Alternative name(s):
    Phosphoinositide phospholipase C
    Phospholipase C-beta-4
      Short name=PLC-beta-4
Gene names
Name: PLCB4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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. This form has a role in retina signal transduction.

Catalytic activity

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactor

Calcium.

Tissue specificity

Preferentially expressed in the retina.

Sequence similarities

Contains 1 C2 domain.

Contains 1 PI-PLC X-box domain.

Contains 1 PI-PLC Y-box domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GRIN1Q055861EBI-998637,EBI-998542

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Notes: Additional isoforms seem to exist.
Isoform 2 (identifier: Q15147-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: Q15147-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
     154-167: LAFMTNTNGKIPVR → MNNNWNVCFFLFCP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 117511751-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
PRO_0000088495

Regions

Domain313 – 463151PI-PLC X-box
Domain565 – 681117PI-PLC Y-box
Domain688 – 78699C2

Sites

Active site3281 By similarity
Active site3751 By similarity

Amino acid modifications

Modified residue6201Phosphoserine
Modified residue6231Phosphotyrosine
Modified residue8901Phosphoserine

Natural variations

Alternative sequence1 – 153153Missing in isoform 1.
VSP_004721
Alternative sequence154 – 16714LAFMT…KIPVR → MNNNWNVCFFLFCP in isoform 1.
VSP_004722

Experimental info

Sequence conflict211A → T in AAI17459. Ref.3
Sequence conflict4471A → P in AAB02027. Ref.1
Sequence conflict7571F → L in AAB02027. Ref.1
Sequence conflict7871L → P in AAB02027. Ref.1
Sequence conflict8401K → T in AAB02027. Ref.1
Sequence conflict9021A → P in AAB02027. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified December 5, 2001. Version 3.
Checksum: AB2C8EB99EF57357

FASTA1,175134,464
        10         20         30         40         50         60 
MAKPYEFNWQ KEVPSFLQEG AVFDRYEEES FVFEPNCLFK VDEFGFFLTW RSEGKEGQVL 

        70         80         90        100        110        120 
ECSLINSIRS GAIPKDPKIL AALEAVGKSE NDLEGRIVCV CSGTDLVNIS FTYMVAENPE 

       130        140        150        160        170        180 
VTKQWVEGLR SIIHNFRANN VSPMTCLKKH WMKLAFMTNT NGKIPVRSIT RTFASGKTEK 

       190        200        210        220        230        240 
VIFQALKELG LPSGKNDEIE PTAFSYEKFY ELTQKICPRT DIEDLFKKIN GDKTDYLTVD 

       250        260        270        280        290        300 
QLVSFLNEHQ RDPRLNEILF PFYDAKRAMQ IIEMYEPDED LKKKGLISSD GFCRYLMSDE 

       310        320        330        340        350        360 
NAPVFLDRLE LYQEMDHPLA HYFISSSHNT YLTGRQFGGK SSVEMYRQVL LAGCRCVELD 

       370        380        390        400        410        420 
CWDGKGEDQE PIITHGKAMC TDILFKDVIQ AIKETAFVTS EYPVILSFEN HCSKYQQYKM 

       430        440        450        460        470        480 
SKYCEDLFGD LLLKQALESH PLEPGRALPS PNDLKRKILI KNKRLKPEVE KKQLEALRSM 

       490        500        510        520        530        540 
MEAGESASPA NILEDDNEEE IESADQEEEA HPEFKFGNEL SADDLGHKEA VANSVKKGLV 

       550        560        570        580        590        600 
TVEDEQAWMA SYKYVGATTN IHPYLSTMIN YAQPVKFQGF HVAEERNIHY NMSSFNESVG 

       610        620        630        640        650        660 
LGYLKTHAIE FVNYNKRQMS RIYPKGGRVD SSNYMPQIFW NAGCQMVSLN YQTPDLAMQL 

       670        680        690        700        710        720 
NQGKFEYNGS CGYLLKPDFM RRPDRTFDPF SETPVDGVIA ATCSVQVISG QFLSDKKIGT 

       730        740        750        760        770        780 
YVEVDMYGLP TDTIRKEFRT RMVMNNGLNP VYNEESFVFR KVILPDLAVL RIAVYDDNNK 

       790        800        810        820        830        840 
LIGQRILPLD GLQAGYRHIS LRNEGNKPLS LPTIFCNIVL KTYVPDGFGD IVDALSDPKK 

       850        860        870        880        890        900 
FLSITEKRAD QMRAMGIETS DIADVPSDTS KNDKKGKANT AKANVTPQSS SELRPTTTAA 

       910        920        930        940        950        960 
LASGVEAKKG IELIPQVRIE DLKQMKAYLK HLKKQQKELN SLKKKHAKEH STMQKLHCTQ 

       970        980        990       1000       1010       1020 
VDKIVAQYDK EKSTHEKILE KAMKKKGGSN CLEMKKETEI KIQTLTSDHK SKVKEIVAQH 

      1030       1040       1050       1060       1070       1080 
TKEWSEMINT HSAEEQEIRD LHLSQQCELL KKLLINAHEQ QTQQLKLSHD RESKEMRAHQ 

      1090       1100       1110       1120       1130       1140 
AKISMENSKA ISQDKSIKNK AERERRVREL NSSNTKKFLE ERKRLAMKQS KEMDQLKKVQ 

      1150       1160       1170 
LEHLEFLEKQ NEQAKEMQQM VKLEAEMDRR PATVV 

« Hide

Isoform 1 [UniParc].

Checksum: 4A6A14188161A46C
Show »

1,022117,162

References

« Hide 'large scale' references
[1]"cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4)."
Alvarez R.A., Ghalayini A.J., Xu P., Hardcastle A., Bhattacharya S., Rao P.N., Pettenati M.J., Anderson R.E., Baehr W.
Genomics 29:53-61(1995) [PubMed: 8530101] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Retina.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 2).
Tissue: Brain.
[4]"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 SER-620 AND TYR-623, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, MASS SPECTROMETRY.

Cross-references

Sequence databases

L41349 mRNA. Translation: AAB02027.1.
AL031652, AL023805 Genomic DNA. Translation: CAI42213.1.
AL023805, AL031652 Genomic DNA. Translation: CAI43087.1.
BC117458 mRNA. Translation: AAI17459.1.
RefSeqNP_000924.2.
NP_877949.1.
UniGeneHs.472101

3D structure databases

HSSPHSSP built from PDB template 1DJX based on UniProtKB P10688.
ModBaseSearch...

Protein-protein interaction databases

IntActQ15147.

PTM databases

PhosphoSiteQ15147.

Genome annotation databases

EnsemblENSG00000101333. Homo sapiens. [Contig view]
GeneID5332.
KEGGhsa:5332.

Organism-specific databases

H-InvDBHIX0015635.
HGNCHGNC:9059. PLCB4.
MIM600810. gene.
PharmGKBPA33387.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ15147.

Gene expression databases

ArrayExpressQ15147.
GermOnlineENSG00000101333. Homo sapiens.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR009535. DUF1154.
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.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
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.
[Graphical view]
PIRSFPIRSF000956. PLC-beta. 1 hit.
PRINTSPR00390. PHPHLIPASEC.
ProDomPD001202. PI_PLC_Y. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
PROSITEPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio20648.
SOURCESearch...

Entry information

Entry namePLCB4_HUMAN
AccessionPrimary (citable) accession number: Q15147
Secondary accession number(s): Q17R56 expand/collapse secondary AC list , Q5JYS8, Q5JYT0, Q5JYT4, Q9BQW5, Q9BQW6, Q9BQW8, Q9UJQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: December 5, 2001
Last modified: November 25, 2008
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

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