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Protein

Type I inositol 3,4-bisphosphate 4-phosphatase

Gene

Inpp4a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Involved in the regulation of megakaryocyte and fibroblast proliferation. Regulates cell growth downstream of transcription factor GATA-1.1 Publication

Catalytic activityi

1-phosphatidyl-myo-inositol 3,4-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate.

Pathwayi: phosphatidylinositol signaling pathway

This protein is involved in the pathway phosphatidylinositol signaling pathway, which is part of Signal transduction.
View all proteins of this organism that are known to be involved in the pathway phosphatidylinositol signaling pathway and in Signal transduction.

GO - Molecular functioni

GO - Biological processi

  • phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
  • polyphosphate catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

UniPathwayiUPA00944.

Chemistry

SwissLipidsiSLP:000000901.

Names & Taxonomyi

Protein namesi
Recommended name:
Type I inositol 3,4-bisphosphate 4-phosphatase (EC:3.1.3.66)
Alternative name(s):
Inositol polyphosphate 4-phosphatase type I
Gene namesi
Name:Inpp4a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1931123. Inpp4a.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 939939Type I inositol 3,4-bisphosphate 4-phosphatasePRO_0000190233Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei355 – 3551PhosphotyrosineBy similarity
Modified residuei488 – 4881PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9EPW0.
MaxQBiQ9EPW0.
PaxDbiQ9EPW0.
PRIDEiQ9EPW0.

PTM databases

iPTMnetiQ9EPW0.
PhosphoSiteiQ9EPW0.
SwissPalmiQ9EPW0.

Expressioni

Tissue specificityi

Spleen, skeletal muscle, lung and uterus.1 Publication

Gene expression databases

BgeeiQ9EPW0.
CleanExiMM_INPP4A.

Interactioni

Subunit structurei

Interacts with INPP5F.1 Publication

Protein-protein interaction databases

IntActiQ9EPW0. 2 interactions.
MINTiMINT-4128906.
STRINGi10090.ENSMUSP00000027287.

Structurei

3D structure databases

ProteinModelPortaliQ9EPW0.
SMRiQ9EPW0. Positions 47-158.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 13792C2Add
BLAST

Sequence similaritiesi

Contains 1 C2 domain.Curated

Phylogenomic databases

eggNOGiKOG4428. Eukaryota.
ENOG410YV83. LUCA.
HOGENOMiHOG000113075.
HOVERGENiHBG081796.
InParanoidiQ9EPW0.
KOiK01109.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9EPW0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTAREHSPRH GARARAMQRA STIDVAADMV GLSLAGNIQD PDEPILEFSL
60 70 80 90 100
ACSELHTPSL DRKPNSFVAV SVTTPPQAFW TKHAQTEIIE GTNNPIFLSS
110 120 130 140 150
IAFFQDSLIN QMTQIKLSVY DVKDRSQGTM YLLGSGTFVV KDLLQDRHHR
160 170 180 190 200
LHLTLRSAES DRVGNITVIG WQMEEKSDQQ PPVTRFLDTV NGRMVLPVDE
210 220 230 240 250
SLTEALGIRS KYAFLRKDSL LKAVFGGAIC RMYRFPTTDG NHLRILEQMA
260 270 280 290 300
ESVLSLHVPR QFVKLLLEED AARVCELEEL GELSPCWESL RRQIVTQYQT
310 320 330 340 350
IILTYQENLT DLHQYKGPSF KASSLKADKK LEFVPTNLHI QRMRVQDDGG
360 370 380 390 400
SDQNYDVVTI GAPAAHCQGF KSGGLRKKLH KFEEAKKHSF EECCTSSSGQ
410 420 430 440 450
SIIYIPQDIT RAKEIIAQIN TLKTQVSYYA ERLSRAAKDR SATGLERTLA
460 470 480 490 500
ILADKTRQLV TVCDCKLLAN SIHGLNAARP DYIASKASPT STEEEQVMLR
510 520 530 540 550
NDQDTLMARW AGRSSRSSLQ VDWHEEEWQK VWLNVDKSLE CIIQRVDKLL
560 570 580 590 600
QKDRLHGEGC EDAFPCSSTC SSKKDCSPPP EESSPGEWSE ALYPLLTTLT
610 620 630 640 650
DCVAMMSDKA KAAMVFLLMQ DSAPTIASYL SLQYRRDVVF CQTLTALICG
660 670 680 690 700
FIIKLRNCLH DGGFLRQLYT IGLLAQFESL LSTYGEELAM LEDMSLGIMD
710 720 730 740 750
LRNVTFKVTQ ATSNASSDML PVITGNRDGF NVRIPLPGPL VDSFPREIQS
760 770 780 790 800
GMLLRVQPVL FNVGINEQQT LAERFGDTSL QEGINGESLV RVNSYFEQFK
810 820 830 840 850
EVLPEDCLPR SRSQTCLPEL LRFLGQNVHA RKNKNVDILW QAAEVCRRLN
860 870 880 890 900
GVRFTSCKSA KDRTAMSVTL EQCLILQHEH GMAPQVFTQA LECMRSEGCR
910 920 930
RENTMKNVGS RKYAFNSLQL KAFPKHYRPP EGTYGKVET
Length:939
Mass (Da):105,540
Last modified:March 1, 2001 - v1
Checksum:iFBF3750836FA8962
GO
Isoform 2 (identifier: Q9EPW0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-265: Missing.
     266-272: LLEEDAA → MCVCFAC
     575-585: Missing.
     897-939: EGCRRENTMK...PEGTYGKVET → IGTREVVTQK...AYLVTKLRCK

Show »
Length:679
Mass (Da):76,356
Checksum:iAC4B87C45EB19C78
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti529 – 5291Q → E in BAC29220 (PubMed:16141072).Curated
Sequence conflicti553 – 5531D → E in BAC29220 (PubMed:16141072).Curated
Sequence conflicti717 – 7171S → N in BAC29220 (PubMed:16141072).Curated
Sequence conflicti741 – 7411V → F in BAC29220 (PubMed:16141072).Curated
Sequence conflicti744 – 7441F → L in BAC29220 (PubMed:16141072).Curated
Sequence conflicti783 – 7831G → V in BAC29220 (PubMed:16141072).Curated
Sequence conflicti786 – 7861G → V in BAC29220 (PubMed:16141072).Curated
Sequence conflicti792 – 7921V → L in BAC29220 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 265265Missing in isoform 2. 1 PublicationVSP_015243Add
BLAST
Alternative sequencei266 – 2727LLEEDAA → MCVCFAC in isoform 2. 1 PublicationVSP_015244
Alternative sequencei575 – 58511Missing in isoform 2. 1 PublicationVSP_015245Add
BLAST
Alternative sequencei897 – 93943EGCRR…GKVET → IGTREVVTQKNLSGLVPIRD LRLDPSLLCSIPLLALSPNL LIVWLFLSIAYLVTKLRCK in isoform 2. 1 PublicationVSP_015246Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF317838 mRNA. Translation: AAG40778.1.
AK035867 mRNA. Translation: BAC29220.1.
CCDSiCCDS35539.1. [Q9EPW0-1]
CCDS78570.1. [Q9EPW0-2]
RefSeqiNP_001277726.1. NM_001290797.1.
NP_001277727.1. NM_001290798.1.
NP_001277728.1. NM_001290799.1.
NP_084542.2. NM_030266.4.
NP_766559.2. NM_172971.3.
UniGeneiMm.5294.

Genome annotation databases

GeneIDi269180.
KEGGimmu:269180.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF317838 mRNA. Translation: AAG40778.1.
AK035867 mRNA. Translation: BAC29220.1.
CCDSiCCDS35539.1. [Q9EPW0-1]
CCDS78570.1. [Q9EPW0-2]
RefSeqiNP_001277726.1. NM_001290797.1.
NP_001277727.1. NM_001290798.1.
NP_001277728.1. NM_001290799.1.
NP_084542.2. NM_030266.4.
NP_766559.2. NM_172971.3.
UniGeneiMm.5294.

3D structure databases

ProteinModelPortaliQ9EPW0.
SMRiQ9EPW0. Positions 47-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9EPW0. 2 interactions.
MINTiMINT-4128906.
STRINGi10090.ENSMUSP00000027287.

Chemistry

SwissLipidsiSLP:000000901.

PTM databases

iPTMnetiQ9EPW0.
PhosphoSiteiQ9EPW0.
SwissPalmiQ9EPW0.

Proteomic databases

EPDiQ9EPW0.
MaxQBiQ9EPW0.
PaxDbiQ9EPW0.
PRIDEiQ9EPW0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi269180.
KEGGimmu:269180.

Organism-specific databases

CTDi3631.
MGIiMGI:1931123. Inpp4a.

Phylogenomic databases

eggNOGiKOG4428. Eukaryota.
ENOG410YV83. LUCA.
HOGENOMiHOG000113075.
HOVERGENiHBG081796.
InParanoidiQ9EPW0.
KOiK01109.

Enzyme and pathway databases

UniPathwayiUPA00944.

Miscellaneous databases

PROiQ9EPW0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EPW0.
CleanExiMM_INPP4A.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Inositol polyphosphate 4-phosphatase type I regulates cell growth downstream of transcription factor GATA-1."
    Vyas P., Norris F.A., Joseph R., Majerus P.W., Orkin S.H.
    Proc. Natl. Acad. Sci. U.S.A. 97:13696-13701(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Strain: C57BL/6J.
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. "Identification of a novel spliceoform of inositol polyphosphate 4-phosphatase type Ialpha expressed in human platelets: structure of human inositol polyphosphate 4-phosphatase type I gene."
    Shearn C.T., Walker J., Norris F.A.
    Biochem. Biophys. Res. Commun. 286:119-125(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Testis.
  5. "Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic pathway."
    Nakatsu F., Messa M., Nandez R., Czapla H., Zou Y., Strittmatter S.M., De Camilli P.
    J. Cell Biol. 209:85-95(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INPP5F.

Entry informationi

Entry nameiINP4A_MOUSE
AccessioniPrimary (citable) accession number: Q9EPW0
Secondary accession number(s): Q8CBJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.