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Protein

Multiple inositol polyphosphate phosphatase 1

Gene

Minpp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 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

Kineticsi

  1. KM=6.9 µM for Ins(1,3,4,5)P41 Publication
  1. Vmax=302 pmol/min/µg enzyme1 Publication

Sites

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

GO - Molecular functioni

GO - Biological processi

  • dephosphorylation Source: GOC
  • phosphatidylinositol-mediated signaling Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

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:Mipp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3089. Minpp1.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 481451Multiple inositol polyphosphate phosphatase 1PRO_0000019585Add
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

PRIDEiO35217.

Expressioni

Tissue specificityi

Widely expressed with highest levels in kidney and liver. Expressed in chondrocytes with an elevated expression in hypertrophic chondrocytes.2 Publications

Gene expression databases

GenevisibleiO35217. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015017.

Structurei

3D structure databases

ProteinModelPortaliO35217.
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.
HOGENOMiHOG000113591.
HOVERGENiHBG052872.
InParanoidiO35217.
KOiK03103.
PhylomeDBiO35217.

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.

O35217-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRGARSHLS ASVALAAVLA AALLSSFARC SLPGRGDPVA SVLSPYFGTK
60 70 80 90 100
TRYEDVNPWL LGDPVAPRRD PELLAGTCTP VQLVALIRHG TRYPTTKQIR
110 120 130 140 150
KLRQLQGLLQ TRESVDGGSR VAAALDQWPL WYDDWMDGQL VEKGRQDMRQ
160 170 180 190 200
LALRLAALFP DLFCRENYGR LRLITSSKHR CVDSSAAFLQ GLWQHYHPGL
210 220 230 240 250
PPPDVSDMEC DPPRVNDKLM RFFDHCEKFL TEVERNATAL YHVEAFKTGP
260 270 280 290 300
EMQTVLKKVA ATLQVPVNNL NADLIQVAFF TCSFDLAIQG VHSPWCDVFD
310 320 330 340 350
VDDAKVLEYL NDLKQYWKRS YGYAINSRSS CNLFQDIFLH LDKAVEQKQR
360 370 380 390 400
SQPVSSSVIL QFGHAETLLP LLSLMGYFKD KEPLTAYNFE EQVHREFRSG
410 420 430 440 450
HIVPYASNLI FVLYHCEDAQ TPQEKFQIQM LLNEKVLPLA HSQKTVALYE
460 470 480
DLKNHYQDIL QSCQTSKECN LPKVNITSDE L
Length:481
Mass (Da):54,589
Last modified:June 1, 2003 - v3
Checksum:i44E7BC000129DB47
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331P → H AA sequence (PubMed:9359836).Curated
Sequence conflicti357 – 3571S → P AA sequence (PubMed:9359836).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012714 mRNA. Translation: AAC53453.2.
RefSeqiNP_062136.1. NM_019263.1.
UniGeneiRn.27882.

Genome annotation databases

GeneIDi29688.
KEGGirno:29688.
UCSCiRGD:3089. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012714 mRNA. Translation: AAC53453.2.
RefSeqiNP_062136.1. NM_019263.1.
UniGeneiRn.27882.

3D structure databases

ProteinModelPortaliO35217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015017.

Proteomic databases

PRIDEiO35217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29688.
KEGGirno:29688.
UCSCiRGD:3089. rat.

Organism-specific databases

CTDi9562.
RGDi3089. Minpp1.

Phylogenomic databases

eggNOGiNOG260296.
HOGENOMiHOG000113591.
HOVERGENiHBG052872.
InParanoidiO35217.
KOiK03103.
PhylomeDBiO35217.

Miscellaneous databases

NextBioi610065.
PROiO35217.

Gene expression databases

GenevisibleiO35217. RN.

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

  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.

Entry informationi

Entry nameiMINP1_RAT
AccessioniPrimary (citable) accession number: O35217
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 101 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, Direct protein sequencing, Reference proteome

Documents

  1. 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.