Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9D967 (MGDP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Magnesium-dependent phosphatase 1

Short name=MDP-1
EC=3.1.3.-
EC=3.1.3.48
Gene names
Name:Mdp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Magnesium-dependent phosphatase which may act as a tyrosine phosphatase. Ref.1 Ref.4 Ref.5

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Cofactor

Magnesium. Ref.1

Enzyme regulation

Inhibited by vanadate and zinc, and slightly by calcium. Ref.1

Sequence similarities

Belongs to the HAD-like hydrolase superfamily.

Biophysicochemical properties

Kinetic parameters:

Dephosphorylates ribose-5-phosphate, 2-deoxy-ribose-5-phosphate, phosphotyrosine, arabinose-5-phosphate, fructose-6-phosphate, 5'-CMP, pNPP, 5'-AMP and glucose-6-phosphate with a decreasing relative rate of 1, 0.9, 0.8, 0.6, 0.5, 0.2, 0.2, 0.2 and 0.06. Dephosphorylates phosphotyrosine with a greater than 100 fold rate over phosphoserine or phosphothreonine.

KM=9.5 mM for ribose-5-phosphate Ref.1

KM=5.6 mM for 2-deoxy-ribose-5-phosphate

KM=15 mM for phosphotyrosine

KM=1.1 mM for arabinose-5-phosphate

KM=21 mM for fructose-6-phosphate

KM=12 mM for 5'-CMP

KM=1.7 mM for pNPP

KM=26 mM for 5'-AMP

KM=31 mM for glucose-6-phosphate

pH dependence:

Optimum pH is 5.3.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Magnesium-dependent phosphatase 1
PRO_0000068828

Sites

Active site111Nucleophile Probable
Active site131Proton donor Probable
Metal binding111Magnesium
Metal binding131Magnesium
Metal binding1231Magnesium
Binding site121Phosphate; via amide nitrogen
Binding site131Phosphate; via amide nitrogen
Binding site201Substrate Probable
Binding site691Phosphate
Binding site701Phosphate
Binding site701Substrate Probable
Binding site1001Phosphate

Experimental info

Mutagenesis111D → N or E: Abolishes enzymatic activity. Ref.4
Mutagenesis131D → N: 92% loss of enzymatic activity. Ref.4
Mutagenesis691S → A: Abolishes enzymatic activity. Ref.4
Mutagenesis1001K → R: Abolishes enzymatic activity. Ref.4
Mutagenesis1031H → K or A: 50% decrease in enzymatic activity. Ref.1
Mutagenesis1221D → N: Abolishes enzymatic activity.
Mutagenesis1231D → N: Abolishes enzymatic activity.
Mutagenesis1271N → D: 50% decrease in enzymatic activity.
Mutagenesis1381C → S, A or G: No effect on enzymatic activity. Ref.1

Secondary structure

.................................... 164
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9D967 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 209D39404DCB1930

FASTA16418,582
        10         20         30         40         50         60 
MTRLPKLAVF DLDYTLWPFW VDTHVDPPFH KSSDGTVRDR RGQNIQLYPE VPEVLGRLQS 

        70         80         90        100        110        120 
LGVPVAAASR TSEIQGANQL LELFDLGKYF IQREIYPGSK VTHFERLHHK TGVPFSQMVF 

       130        140        150        160 
FDDENRNIID VGRLGVTCIH IRDGMSLQTL TQGLETFAKA QAGL 

« Hide

References

« Hide 'large scale' references
[1]"MDP-1: a novel eukaryotic magnesium-dependent phosphatase."
Selengut J.D., Levine R.L.
Biochemistry 39:8315-8324(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF HIS-103 AND CYS-138.
[2]"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: Pancreas.
[3]"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].
Tissue: Eye.
[4]"MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases."
Selengut J.D.
Biochemistry 40:12704-12711(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-11; ASP-13; SER-69 AND LYS-100, FUNCTION.
[5]"X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily."
Peisach E., Selengut J.D., Dunaway-Mariano D., Allen K.N.
Biochemistry 43:12770-12779(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-164, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-164 WITH MAGNESIUM AND TUNGSTATE, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF230273 mRNA. Translation: AAK00763.1.
AK007319 mRNA. Translation: BAB24954.1.
AK160438 mRNA. Translation: BAE35788.1.
BC046613 mRNA. Translation: AAH46613.1.
CCDSCCDS27123.1.
RefSeqNP_075886.1. NM_023397.4.
UniGeneMm.24601.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U7OX-ray1.90A1-164[»]
1U7PX-ray1.90A/B/C/D1-164[»]
ProteinModelPortalQ9D967.
SMRQ9D967. Positions 1-164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D967. 1 interaction.
MINTMINT-4127783.

PTM databases

PhosphoSiteQ9D967.

Proteomic databases

MaxQBQ9D967.
PaxDbQ9D967.
PRIDEQ9D967.

Protocols and materials databases

DNASU67881.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002400; ENSMUSP00000002400; ENSMUSG00000002329.
GeneID67881.
KEGGmmu:67881.
UCSCuc007uaa.2. mouse.

Organism-specific databases

CTD145553.
MGIMGI:1915131. Mdp1.

Phylogenomic databases

eggNOGNOG279690.
GeneTreeENSGT00390000004110.
HOGENOMHOG000216653.
HOVERGENHBG081971.
InParanoidQ9D967.
KOK17619.
OMAHVQNGMS.
OrthoDBEOG7PK913.
PhylomeDBQ9D967.
TreeFamTF328413.

Gene expression databases

BgeeQ9D967.
CleanExMM_1810034K20RIK.
GenevestigatorQ9D967.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR023214. HAD-like_dom.
IPR010033. HAD_SF_ppase_IIIC.
IPR024734. MDP_1_eu.
IPR010036. MDP_1_eu_arc.
[Graphical view]
PANTHERPTHR17901. PTHR17901. 1 hit.
PfamPF12689. Acid_PPase. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01681. HAD-SF-IIIC. 1 hit.
TIGR01685. MDP-1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMDP1. mouse.
EvolutionaryTraceQ9D967.
NextBio325825.
PROQ9D967.
SOURCESearch...

Entry information

Entry nameMGDP1_MOUSE
AccessionPrimary (citable) accession number: Q9D967
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 94 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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