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O35217 (MINP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:Mipp1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also 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. May play a role in bone development (endochondral ossification). Ref.3

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 Ref.2.

Tissue specificity

Widely expressed with highest levels in kidney and liver. Expressed in chondrocytes with an elevated expression in hypertrophic chondrocytes. Ref.1 Ref.3

Sequence similarities

Belongs to the histidine acid phosphatase family. MINPP1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=6.9 µM for Ins(1,3,4,5)P4 Ref.1

Vmax=302 pmol/min/µg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 481451Multiple inositol polyphosphate phosphatase 1
PRO_0000019585

Regions

Motif478 – 4814Prevents secretion from ER Potential

Sites

Active site891 Potential

Amino acid modifications

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

Experimental info

Sequence conflict331P → H AA sequence Ref.1
Sequence conflict3571S → P AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
O35217 [UniParc].

Last modified June 1, 2003. Version 3.
Checksum: 44E7BC000129DB47

FASTA48154,589
        10         20         30         40         50         60 
MLRGARSHLS ASVALAAVLA AALLSSFARC SLPGRGDPVA SVLSPYFGTK TRYEDVNPWL 

        70         80         90        100        110        120 
LGDPVAPRRD PELLAGTCTP VQLVALIRHG TRYPTTKQIR KLRQLQGLLQ TRESVDGGSR 

       130        140        150        160        170        180 
VAAALDQWPL WYDDWMDGQL VEKGRQDMRQ LALRLAALFP DLFCRENYGR LRLITSSKHR 

       190        200        210        220        230        240 
CVDSSAAFLQ GLWQHYHPGL PPPDVSDMEC DPPRVNDKLM RFFDHCEKFL TEVERNATAL 

       250        260        270        280        290        300 
YHVEAFKTGP EMQTVLKKVA ATLQVPVNNL NADLIQVAFF TCSFDLAIQG VHSPWCDVFD 

       310        320        330        340        350        360 
VDDAKVLEYL NDLKQYWKRS YGYAINSRSS CNLFQDIFLH LDKAVEQKQR SQPVSSSVIL 

       370        380        390        400        410        420 
QFGHAETLLP LLSLMGYFKD KEPLTAYNFE EQVHREFRSG HIVPYASNLI FVLYHCEDAQ 

       430        440        450        460        470        480 
TPQEKFQIQM LLNEKVLPLA HSQKTVALYE DLKNHYQDIL QSCQTSKECN LPKVNITSDE 


L

« Hide

References

[1]"Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase."
Craxton A., Caffrey J.J., Burkhart W., Safrany S.T., Shears S.B.
Biochem. J. 328:75-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Liver.
[2]"Hepatic Ins(1,3,4,5)P4 3-phosphatase is compartmentalized inside endoplasmic reticulum."
Ali N., Craxton A., Shears S.B.
J. Biol. Chem. 268:6161-6167(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[3]"The human and rat forms of multiple inositol polyphosphate phosphatase: functional homology with a histidine acid phosphatase up-regulated during endochondral ossification."
Caffrey J.J., Hidaka K., Matsuda M., Hirata M., Shears S.B.
FEBS Lett. 442:99-104(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF012714 mRNA. Translation: AAC53453.2.
IPIIPI00876578.
RefSeqNP_062136.1. NM_019263.1.
UniGeneRn.27882.

3D structure databases

ProteinModelPortalO35217.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000015017.

Proteomic databases

PRIDEO35217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29688.
KEGGrno:29688.
UCSCRGD:3089. rat.

Organism-specific databases

CTD9562.
RGD3089. Minpp1.

Phylogenomic databases

eggNOGNOG260296.
HOGENOMHOG000113591.
HOVERGENHBG052872.
InParanoidO35217.
KOK03103.
OrthoDBEOG4X6C85.

Gene expression databases

GenevestigatorO35217.
GermOnlineENSRNOG00000011287. Rattus norvegicus.

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

NextBio610065.

Entry information

Entry nameMINP1_RAT
AccessionPrimary (citable) accession number: O35217
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2003
Last modified: April 3, 2013
This is version 91 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

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