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Reviewed, UniProtKB/Swiss-Prot Q7TME0 (LPPR4_MOUSE)

Last modified June 16, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lipid phosphate phosphatase-related protein type 4
    EC=3.1.3.4
Alternative name(s):
    Plasticity-related gene 1 protein
      Short name=PRG-1
    Brain-specific phosphatidic acid phosphatase-like protein 1
Gene names
Name: Lppr4
Synonyms: D3Bwg0562e, Kiaa0455, Prg1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length766 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Hydrolyzes lysophosphatidic acid (LPA). Facilitates axonal outgrowth during development and regenerative sprouting. In the outgrowing axons acts as an ecto-enzyme and attenuates phospholipid-induced axon collapse in neurons and facilitates outgrowth in the hippocampus By similarity.

Catalytic activity

A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the PA-phosphatase related phosphoesterase family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
   Molecular functionHydrolase
   PTMGlycoprotein
Phosphoprotein
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphosphatidate phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 766766Lipid phosphate phosphatase-related protein type 4
PRO_0000317437

Regions

Transmembrane68 – 8821 Potential
Transmembrane120 – 14021 Potential
Transmembrane179 – 19921 Potential
Transmembrane248 – 26821 Potential
Transmembrane277 – 29721 Potential
Transmembrane309 – 32921 Potential
Compositional bias698 – 7014Poly-His

Amino acid modifications

Modified residue2181Phosphoserine Ref.5
Modified residue3471Phosphoserine Ref.6
Modified residue4171Phosphothreonine Ref.6
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Glycosylation5451N-linked (GlcNAc...) Potential
Glycosylation5701N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict4511Q → R in BAC32865. Ref.3
Sequence conflict495 – 4962DH → ED in AAH24711. Ref.4
Sequence conflict5001G → S in AAH24711. Ref.4
Sequence conflict5431Q → K in BAC32865. Ref.3
Sequence conflict5681A → D in AAP41099. Ref.1
Sequence conflict5681A → D in AAP41100. Ref.1
Sequence conflict5681A → D in AAP57768. Ref.1
Sequence conflict6531K → E in BAC37711. Ref.3
Sequence conflict6541A → V in AAP41099. Ref.1
Sequence conflict6541A → V in AAP41100. Ref.1
Sequence conflict6541A → V in AAP57768. Ref.1
Sequence conflict7371I → V in BAC32865. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q7TME0-1 [UniParc].

Last modified February 5, 2008. Version 2.
Checksum: 371D9FA1A829B5B1

FASTA76683,290
        10         20         30         40         50         60 
MQRAGSSGAR GECDISGAGR LRLEQAARLG GRTVHTSPGG GLGARQAAGM SAKERPKGKV 

        70         80         90        100        110        120 
IKDSVTLLPC FYFVELPILA SSVVSLYFLE LTDVFKPVHS GFSCYDRSLS MPYIEPTQEA 

       130        140        150        160        170        180 
IPFLMLLSLA FAGPAITIMV GEGILYCCLS KRRNGAGLEP NINAGGCNFN SFLRRAVRFV 

       190        200        210        220        230        240 
GVHVFGLCST ALITDIIQLS TGYQAPYFLT VCKPNYTSLN VSCKENSYIV EDICSGSDLT 

       250        260        270        280        290        300 
VINSGRKSFP SQHATLAAFA AVYVSMYFNS TLTDSSKLLK PLLVFTFIIC GIICGLTRIT 

       310        320        330        340        350        360 
QYKNHPVDVY CGFLIGGGIA LYLGLYAVGN FLPSEDSMLQ HRDALRSLTD LNQDPSRVLS 

       370        380        390        400        410        420 
AKNGSSGDGI AHTEGILNRN HRDASSLTNL KRANADVEII TPRSPMGKES MVTFSNTLPR 

       430        440        450        460        470        480 
ANTPSVEDPV RRNASIHASM DSARSKQLLT QWKSKNESRK MSLQVMDTEP EGQSPPRSIE 

       490        500        510        520        530        540 
MRSSSEPSRV GVNGDHHVPG NQYLKIQPGT VPGCNNSMPG GPRVSIQSRP GSSQLVHIPE 

       550        560        570        580        590        600 
ETQENISTSP KSSSARAKWL KAAEKTVACN RSNNQPRIMQ VIAMSKQQGV LQSSPKNAEG 

       610        620        630        640        650        660 
STVTCTGSIR YKTLTDHEPS GIVRVEAHPE NNRPIIQIPS STEGEGSGSW KWKAPEKSSL 

       670        680        690        700        710        720 
RQTYELNDLN RDSESCESLK DSFGSGDRKR SNIDSNEHHH HGITTIRVTP VEGSEIGSET 

       730        740        750        760 
LSVSSSRDST LRRKGNIILI PERSNSPENT RNIFYKGTSP TRAYKD 

« Hide

References

« Hide 'large scale' references
[1]"A new phospholipid phosphatase, PRG-1, is involved in axon growth and regenerative sprouting."
Braeuer A.U., Savaskan N.E., Kuehn H., Prehn S., Ninnemann O., Nitsch R.
Nat. Neurosci. 6:572-578(2003) [PubMed: 12730698] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/J and BALB/c.
Tissue: Brain and Testis.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed: 14621295] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"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].
Strain: C57BL/6J.
Tissue: Medulla oblongata and Spinal cord.
[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] OF 412-766.
Strain: Czech II.
Tissue: Mammary tumor.
[5]"Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line."
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.
Mol. Cell. Proteomics 3:279-286(2004) [PubMed: 14729942] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, MASS SPECTROMETRY.
Tissue: B-cell.
[6]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-417, MASS SPECTROMETRY.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

AY266266 mRNA. Translation: AAP41099.1.
AY266267 mRNA. Translation: AAP41100.1.
AF541279 mRNA. Translation: AAP57768.1.
AK129149 mRNA. Translation: BAC97959.1. Different initiation.
AK046782 mRNA. Translation: BAC32865.1.
AK079635 mRNA. Translation: BAC37711.1. Different initiation.
BC024711 mRNA. Translation: AAH24711.1.
IPIIPI00420590.
RefSeqNP_808332.3.
UniGeneMm.140138

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000044667. Mus musculus. [Contig view]
GeneID229791.
KEGGmmu:229791.

Organism-specific databases

MGIMGI:106530. D3Bwg0562e.
RougeSearch...

Phylogenomic databases

HOVERGENQ7TME0.
OMAQ7TME0. SSDGIAH.

Enzyme and pathway databases

BRENDA3.1.3.4. 244.

Gene expression databases

ArrayExpressQ7TME0.
BgeeQ7TME0.

Family and domain databases

InterProIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio379679.
SOURCESearch...

Entry information

Entry nameLPPR4_MOUSE
AccessionPrimary (citable) accession number: Q7TME0
Secondary accession number(s): Q6ZQA8 expand/collapse secondary AC list , Q8BV73, Q8BXK2, Q8R3R6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: June 16, 2009
This is version 37 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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