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Q9Z2L6 (MINP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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

Names and origin

Protein namesRecommended name:
Multiple inositol polyphosphate phosphatase 1

EC=3.1.3.62
Alternative name(s):
2,3-bisphosphoglycerate 3-phosphatase
Short name=2,3-BPG phosphatase
EC=3.1.3.80
Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase
Short name=Ins(1,3,4,5)P(4) 3-phosphatase
Gene names
Name:Minpp1
Synonyms:Mipp
ORF Names:MNCb-1572
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.5

Catalytic activity

Myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate. Ref.1

2,3-bisphospho-D-glycerate + H2O = 2-phospho-D-glycerate + phosphate. Ref.1

Subcellular location

Endoplasmic reticulum lumen By similarity. Cell membrane Probable. Note: Also attached to the plasma membrane in erythrocytes Probable. Ref.5

Tissue specificity

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

Developmental stage

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. Ref.5

Sequence similarities

Belongs to the histidine acid phosphatase family. MINPP1 subfamily.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 481451Multiple inositol polyphosphate phosphatase 1
PRO_0000019583

Regions

Motif478 – 4814Prevents secretion from ER Potential

Sites

Active site891 Potential

Amino acid modifications

Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation4751N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis891H → A: Loss of phosphatase activity. Ref.1
Sequence conflict2111G → D in AAH21437. Ref.4
Sequence conflict2571K → Q in AAH21437. Ref.4
Sequence conflict2671M → V in AAH21437. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9Z2L6 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 7CE78356B11F4606

FASTA48154,537
        10         20         30         40         50         60 
MLRGARSHLP ASVAPAAVLA AALLSSFARC SLPGRGDPVA SVLSPYFGTK TRYEDANPWL 

        70         80         90        100        110        120 
LVDPVAPRRD PELLAGTCTP VQLVALIRHG TRYPTTKQIR KLKQLQGLLQ TRESRDGGSQ 

       130        140        150        160        170        180 
VAAALAEWPL WYGDWMDGQL VEKGRQDMRQ LALRLAALFP DLFSRENYDR LRLITSSKHR 

       190        200        210        220        230        240 
CVDSSAAFLQ GLWQHYHPGL PPPDVSDMEC GPPRINDKLM RFFDHCEKFL TDVERNETAL 

       250        260        270        280        290        300 
YHVEAFKTGP EMQKVLKKVA ATLQVPMNSL NADLIQVAFF TCSFDLAIKG VHSPWCDVFD 

       310        320        330        340        350        360 
VDDARVLEYL NDLKQYWKRS YGYTINSRSS CNLFQDIFLH LDKAVEQKQR SQPVSSPVIL 

       370        380        390        400        410        420 
QFGHAETLLP LLSLMGYFKD KEPLTAYNFE EQVNRKFRSG HIVPYASNLI FVLYHCDNAQ 

       430        440        450        460        470        480 
SPEEQFQIQL LLNEKVLPLA HSQRPVGLYE ELKTHYRDIL QSCQTSKECS PPKANITSDE 


L 

« Hide

References

« Hide 'large scale' references
[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. 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] [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF046908 mRNA. Translation: AAD02434.1.
AB041574 mRNA. Translation: BAA95058.1. Frameshift.
AK151486 mRNA. Translation: BAE30439.1.
BC021437 mRNA. Translation: AAH21437.1.
RefSeqNP_034929.1. NM_010799.2.
UniGeneMm.255116.

3D structure databases

ProteinModelPortalQ9Z2L6.
SMRQ9Z2L6. Positions 71-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Z2L6. 2 interactions.
MINTMINT-4119928.
STRING10090.ENSMUSP00000025827.

PTM databases

PhosphoSiteQ9Z2L6.

Proteomic databases

PaxDbQ9Z2L6.
PRIDEQ9Z2L6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025827; ENSMUSP00000025827; ENSMUSG00000024896.
GeneID17330.
KEGGmmu:17330.
UCSCuc008hfk.2. mouse.

Organism-specific databases

CTD9562.
MGIMGI:1336159. Minpp1.

Phylogenomic databases

eggNOGNOG260296.
GeneTreeENSGT00390000018409.
HOGENOMHOG000113591.
HOVERGENHBG052872.
InParanoidQ3UA76.
KOK03103.
OMAADMECGP.
OrthoDBEOG7992QC.
TreeFamTF324072.

Enzyme and pathway databases

BRENDA3.1.3.62. 3474.

Gene expression databases

BgeeQ9Z2L6.
GenevestigatorQ9Z2L6.

Family and domain databases

InterProIPR000560. His_Pase_superF_clade-2.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFPIRSF000894. Acid_phosphatase. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio291902.
PROQ9Z2L6.
SOURCESearch...

Entry information

Entry nameMINP1_MOUSE
AccessionPrimary (citable) accession number: Q9Z2L6
Secondary accession number(s): Q3UA76, Q8VDR0, Q9JJD5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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