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Protein

Multiple inositol polyphosphate phosphatase 1

Gene

Minpp1

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

Functioni

Acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate (By similarity). Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). May play a role in bone development (endochondral ossification).By similarity1 Publication

Catalytic activityi

Myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate.1 Publication
2,3-bisphospho-D-glycerate + H2O = 2-phospho-D-glycerate + phosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei89 – 891Sequence Analysis

GO - Molecular functioni

  1. acid phosphatase activity Source: InterPro
  2. bisphosphoglycerate 3-phosphatase activity Source: MGI
  3. inositol hexakisphosphate 2-phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. dephosphorylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.1.3.62. 3474.
ReactomeiREACT_291479. Synthesis of IPs in the ER lumen.

Names & Taxonomyi

Protein namesi
Recommended name:
Multiple inositol polyphosphate phosphatase 1 (EC:3.1.3.62)
Alternative name(s):
2,3-bisphosphoglycerate 3-phosphatase (EC:3.1.3.80)
Short name:
2,3-BPG phosphatase
Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase
Short name:
Ins(1,3,4,5)P(4) 3-phosphatase
Gene namesi
Name:Minpp1
Synonyms:Mipp
ORF Names:MNCb-1572
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1336159. Minpp1.

Subcellular locationi

  1. Endoplasmic reticulum lumen PROSITE-ProRule annotation
  2. Cell membrane 1 Publication

  3. Note: Also attached to the plasma membrane in erythrocytes.Curated

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: MGI
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891H → A: Loss of phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 481451Multiple inositol polyphosphate phosphatase 1PRO_0000019583Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9Z2L6.
PaxDbiQ9Z2L6.
PRIDEiQ9Z2L6.

PTM databases

PhosphoSiteiQ9Z2L6.

Expressioni

Tissue specificityi

Widely expressed with highest levels in kidney, intestine, thymus and liver.

Developmental stagei

Expressed in different stages of embryogenesis, from E7.5 through E14.5. The highest levels of expression is found in the visceral endoderm at E7.5 and E8.5 and in the fetal liver at E12.5 and E14.5.1 Publication

Gene expression databases

BgeeiQ9Z2L6.
GenevestigatoriQ9Z2L6.

Interactioni

Protein-protein interaction databases

IntActiQ9Z2L6. 2 interactions.
MINTiMINT-4119928.
STRINGi10090.ENSMUSP00000025827.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2L6.
SMRiQ9Z2L6. Positions 79-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi478 – 4814Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG260296.
GeneTreeiENSGT00390000018409.
HOGENOMiHOG000113591.
HOVERGENiHBG052872.
InParanoidiQ9Z2L6.
KOiK03103.
OMAiHTSEECE.
OrthoDBiEOG7992QC.
TreeFamiTF324072.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z2L6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRGARSHLP ASVAPAAVLA AALLSSFARC SLPGRGDPVA SVLSPYFGTK
60 70 80 90 100
TRYEDANPWL LVDPVAPRRD PELLAGTCTP VQLVALIRHG TRYPTTKQIR
110 120 130 140 150
KLKQLQGLLQ TRESRDGGSQ VAAALAEWPL WYGDWMDGQL VEKGRQDMRQ
160 170 180 190 200
LALRLAALFP DLFSRENYDR LRLITSSKHR CVDSSAAFLQ GLWQHYHPGL
210 220 230 240 250
PPPDVSDMEC GPPRINDKLM RFFDHCEKFL TDVERNETAL YHVEAFKTGP
260 270 280 290 300
EMQKVLKKVA ATLQVPMNSL NADLIQVAFF TCSFDLAIKG VHSPWCDVFD
310 320 330 340 350
VDDARVLEYL NDLKQYWKRS YGYTINSRSS CNLFQDIFLH LDKAVEQKQR
360 370 380 390 400
SQPVSSPVIL QFGHAETLLP LLSLMGYFKD KEPLTAYNFE EQVNRKFRSG
410 420 430 440 450
HIVPYASNLI FVLYHCDNAQ SPEEQFQIQL LLNEKVLPLA HSQRPVGLYE
460 470 480
ELKTHYRDIL QSCQTSKECS PPKANITSDE L
Length:481
Mass (Da):54,537
Last modified:July 27, 2011 - v3
Checksum:i7CE78356B11F4606
GO

Sequence cautioni

The sequence BAA95058.1 differs from that shown. Reason: Frameshift at positions 14 and 176. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111G → D in AAH21437 (PubMed:15489334).Curated
Sequence conflicti257 – 2571K → Q in AAH21437 (PubMed:15489334).Curated
Sequence conflicti267 – 2671M → V in AAH21437 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF046908 mRNA. Translation: AAD02434.1.
AB041574 mRNA. Translation: BAA95058.1. Frameshift.
AK151486 mRNA. Translation: BAE30439.1.
BC021437 mRNA. Translation: AAH21437.1.
CCDSiCCDS29751.1.
RefSeqiNP_034929.1. NM_010799.2.
UniGeneiMm.255116.

Genome annotation databases

EnsembliENSMUST00000025827; ENSMUSP00000025827; ENSMUSG00000024896.
GeneIDi17330.
KEGGimmu:17330.
UCSCiuc008hfk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF046908 mRNA. Translation: AAD02434.1.
AB041574 mRNA. Translation: BAA95058.1. Frameshift.
AK151486 mRNA. Translation: BAE30439.1.
BC021437 mRNA. Translation: AAH21437.1.
CCDSiCCDS29751.1.
RefSeqiNP_034929.1. NM_010799.2.
UniGeneiMm.255116.

3D structure databases

ProteinModelPortaliQ9Z2L6.
SMRiQ9Z2L6. Positions 79-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z2L6. 2 interactions.
MINTiMINT-4119928.
STRINGi10090.ENSMUSP00000025827.

PTM databases

PhosphoSiteiQ9Z2L6.

Proteomic databases

MaxQBiQ9Z2L6.
PaxDbiQ9Z2L6.
PRIDEiQ9Z2L6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025827; ENSMUSP00000025827; ENSMUSG00000024896.
GeneIDi17330.
KEGGimmu:17330.
UCSCiuc008hfk.2. mouse.

Organism-specific databases

CTDi9562.
MGIiMGI:1336159. Minpp1.

Phylogenomic databases

eggNOGiNOG260296.
GeneTreeiENSGT00390000018409.
HOGENOMiHOG000113591.
HOVERGENiHBG052872.
InParanoidiQ9Z2L6.
KOiK03103.
OMAiHTSEECE.
OrthoDBiEOG7992QC.
TreeFamiTF324072.

Enzyme and pathway databases

BRENDAi3.1.3.62. 3474.
ReactomeiREACT_291479. Synthesis of IPs in the ER lumen.

Miscellaneous databases

NextBioi291902.
PROiQ9Z2L6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2L6.
GenevestigatoriQ9Z2L6.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple inositol polyphosphate phosphatase: evolution as a distinct group within the histidine phosphatase family and chromosomal localization of the human and mouse genes to chromosomes 10q23 and 19."
    Chi H., Tiller G.E., Dasouki M.J., Romano P.R., Wang J., O'keefe R.J., Puzas J.E., Rosier R.N., Reynolds P.R.
    Genomics 56:324-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-89.
    Strain: 129.
  2. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
    Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    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.
    , 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].
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  5. "Targeted deletion of Minpp1 provides new insight into the activity of multiple inositol polyphosphate phosphatase in vivo."
    Chi H., Yang X., Kingsley P.D., O'Keefe R.J., Puzas J.E., Rosier R.N., Shears S.B., Reynolds P.R.
    Mol. Cell. Biol. 20:6496-6507(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiMINP1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2L6
Secondary accession number(s): Q3UA76, Q8VDR0, Q9JJD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 104 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.