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O35217

- MINP1_RAT

UniProt

O35217 - MINP1_RAT

Protein

Multiple inositol polyphosphate phosphatase 1

Gene

Minpp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 3 (01 Jun 2003)
      Previous versions | rss
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    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

    Vmax=302 pmol/min/µg enzyme1 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: UniProtKB-EC
    3. inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity Source: RGD
    4. inositol-1,4,5,6-tetrakisphosphate 6-phosphatase activity Source: RGD
    5. inositol hexakisphosphate 2-phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. phosphatidylinositol-mediated signaling Source: RGD

    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: Unplaced

    Organism-specific databases

    RGDi3089. Minpp1.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    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

    GenevestigatoriO35217.

    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

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    MLRGARSHLS ASVALAAVLA AALLSSFARC SLPGRGDPVA SVLSPYFGTK    50
    TRYEDVNPWL LGDPVAPRRD PELLAGTCTP VQLVALIRHG TRYPTTKQIR 100
    KLRQLQGLLQ TRESVDGGSR VAAALDQWPL WYDDWMDGQL VEKGRQDMRQ 150
    LALRLAALFP DLFCRENYGR LRLITSSKHR CVDSSAAFLQ GLWQHYHPGL 200
    PPPDVSDMEC DPPRVNDKLM RFFDHCEKFL TEVERNATAL YHVEAFKTGP 250
    EMQTVLKKVA ATLQVPVNNL NADLIQVAFF TCSFDLAIQG VHSPWCDVFD 300
    VDDAKVLEYL NDLKQYWKRS YGYAINSRSS CNLFQDIFLH LDKAVEQKQR 350
    SQPVSSSVIL QFGHAETLLP LLSLMGYFKD KEPLTAYNFE EQVHREFRSG 400
    HIVPYASNLI FVLYHCEDAQ TPQEKFQIQM LLNEKVLPLA HSQKTVALYE 450
    DLKNHYQDIL QSCQTSKECN LPKVNITSDE L 481
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012714 mRNA. Translation: AAC53453.2 .
    RefSeqi NP_062136.1. NM_019263.1.
    UniGenei Rn.27882.

    3D structure databases

    ProteinModelPortali O35217.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000015017.

    Proteomic databases

    PRIDEi O35217.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 29688.
    KEGGi rno:29688.
    UCSCi RGD:3089. rat.

    Organism-specific databases

    CTDi 9562.
    RGDi 3089. Minpp1.

    Phylogenomic databases

    eggNOGi NOG260296.
    HOGENOMi HOG000113591.
    HOVERGENi HBG052872.
    InParanoidi O35217.
    KOi K03103.
    PhylomeDBi O35217.

    Miscellaneous databases

    NextBioi 610065.
    PROi O35217.

    Gene expression databases

    Genevestigatori O35217.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    InterProi IPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    IPR016274. Histidine_acid_Pase_euk.
    [Graphical view ]
    Pfami PF00328. His_Phos_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000894. Acid_phosphatase. 1 hit.
    SUPFAMi SSF53254. SSF53254. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 98 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