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P59644 (PI5PA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 80. 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:
Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
EC=3.1.3.56
Alternative name(s):
Inositol polyphosphate 5-phosphatase J
Gene names
Name:Inpp5j
Synonyms:Pib5pa
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 length1003 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles By similarity.

Catalytic activity

D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate.

1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.

Subcellular location

Cytoplasm. Note: Predominantly localized to membrane ruffles. Ref.4

Domain

The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute binding sites for the 14-3-3 protein. Ref.4

Sequence similarities

Belongs to the inositol-1,4,5-trisphosphate 5-phosphatase type II family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10031003Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
PRO_0000209739

Regions

Region422 – 725304Catalytic Potential
Region726 – 837112Required for ruffle localization
Motif6 – 116RSXSXX motif 1
Motif346 – 3516SH3-binding Potential
Motif351 – 3566RSXSXX motif 2
Motif871 – 8766RSXSXX motif 3
Motif882 – 8876RSXSXX motif 4
Motif908 – 9136RSXSXX motif 5
Compositional bias50 – 374325Pro-rich
Compositional bias837 – 93498Ser-rich

Amino acid modifications

Modified residue3481Phosphoserine Ref.5
Modified residue3501Phosphoserine Ref.5

Experimental info

Sequence conflict3431P → R in BAC28654. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P59644 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 3D2E1F6B3D060B4B

FASTA1,003107,544
        10         20         30         40         50         60 
MEGQTRSGSA RPGTRTGLGP LPGTHGVLQA EIPSKKVNSS FQLPAKNSGP ASSEPRLTLA 

        70         80         90        100        110        120 
PVGPRAAVSP PSERPRLVLS SPRPVLAPLS IAGEQKRPPP PHSSNRAAKS VGQLVVSAAA 

       130        140        150        160        170        180 
ASKPPPVASV SILAPKSLGQ LVISASAMPR PSPAPLGSVL TPTSRDQKQL SPTSVGPKPA 

       190        200        210        220        230        240 
LATSGLSLAL ASQEQPPQSP SSPSPVPSPV LSPSQEGHLA AASVTSTPAS ERQLPARQKD 

       250        260        270        280        290        300 
TAVPRPTPPA DKCLYTPERA AGPATSPPRA QAFSDPRLSP SFRARPEAPR HSPEDPVLPP 

       310        320        330        340        350        360 
PPQTLPLDVS PGLPESGTRS PGLLSPTFRP GIPSSQTVPP PLPKPPRSPS RSPSRSPNRS 

       370        380        390        400        410        420 
PCLPPAPEVA LPKPVTQAAG SGRCPSPNLQ AQESPAAATT TTSPTSSWSA QPTCKSDPGF 

       430        440        450        460        470        480 
RITVVTWNVG TAMPPDDVTS LLHLGSGHDN DGADMIAIGL QEVNSMINKR LKDALFTDQW 

       490        500        510        520        530        540 
SELFMDALGP FNFVLVSTVR MQGVILLLFA KYYHLPFLRD VQTDCTRTGL GGYWGNKGGV 

       550        560        570        580        590        600 
SVRLAAFGHM LCFLNCHLPA HMDKAEQRKD NFQTILSLQQ FQGPGAHGIL DHDLVFWFGD 

       610        620        630        640        650        660 
LNFRIESYDL HFVKFAIDSN QLHQLWEKDQ LNMAKNTWPI LKGFQEGPLN FAPTFKFDVG 

       670        680        690        700        710        720 
TNKYDTSAKK RKPAWTDRIL WKVKAPSGGP SPSGRESHRL QVTQHSYRSH MEYTVSDHKP 

       730        740        750        760        770        780 
VAAQFILQFA FRDDVPLVRL EVADEWARPE QAVVRYRVET VFARSSWDWI GLYRVGFRHC 

       790        800        810        820        830        840 
KDYVAYVWAK HEEVDGNIYQ VTFSEESLPK GHGDFILGYY SHHHSILIGV TEPFQISLPT 

       850        860        870        880        890        900 
SESASSSTDS SGTSSEGEDD STLELLAPKS RSPSPGKSKR HRSRSPGLAR FPSLALHPSS 

       910        920        930        940        950        960 
RERRGGSRSP SPQSRQLPRV APDRGHSSSS RGSSEEGPSG LPGPWAFPPS VPRSLGLLPA 

       970        980        990       1000 
LRLETVDPGG GGSWGADQEA PDPNSLSPSP QGRLGLEEGG LGP

« Hide

References

« Hide 'large scale' references
[1]"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 and NOD.
Tissue: Diencephalon.
[2]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].
[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].
[4]"Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase SKIP localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation."
Gurung R., Tan A., Ooms L.M., McGrath M.J., Huysmans R.D., Munday A.D., Prescott M., Whisstock J.C., Mitchell C.A.
J. Biol. Chem. 278:11376-11385(2003) [PubMed: 12536145] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION OF DOMAIN REQUIRED FOR MEMBRANE RUFFLE LOCALIZATION.
[5]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348 AND SER-350, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK034272 mRNA. Translation: BAC28654.1.
AK170114 mRNA. Translation: BAE41572.1.
BC131634 mRNA. Translation: AAI31635.1.
BC131635 mRNA. Translation: AAI31636.1.
CH466574 Genomic DNA. Translation: EDL40427.1.
IPIIPI00173277.
RefSeqNP_766027.2. NM_172439.3.
UniGeneMm.24313.

3D structure databases

ProteinModelPortalP59644.
SMRP59644. Positions 417-734.
ModBaseSearch...

Protein-protein interaction databases

STRINGP59644.

PTM databases

PhosphoSiteP59644.

Proteomic databases

PRIDEP59644.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044507; ENSMUSP00000046625; ENSMUSG00000034570.
GeneID170835.
KEGGmmu:170835.

Organism-specific databases

CTD27124.
MGIMGI:2158663. Inpp5j.

Phylogenomic databases

HOGENOMHBG125086.
HOVERGENHBG082135.
InParanoidP59644.
OrthoDBEOG4HDSTN.
PhylomeDBP59644.

Gene expression databases

ArrayExpressP59644.
BgeeP59644.
GenevestigatorP59644.
GermOnlineENSMUSG00000034570. Mus musculus.

Family and domain databases

InterProIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
KOK01106.
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMSSF56219. Exo_endo_phos. 1 hit.
ProtoNetSearch...

Other

NextBio370509.
SOURCESearch...

Entry information

Entry namePI5PA_MOUSE
AccessionPrimary (citable) accession number: P59644
Secondary accession number(s): Q3TDM9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 80 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