Q9D967 (MGDP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Magnesium-dependent phosphatase 1
Short name=MDP-1
EC=3.1.3.-
EC=3.1.3.48

Gene names

Name:

Mdp1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	164 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fructosamine metabolic process Inferred from electronic annotation. Source: Compara peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 164

164

Magnesium-dependent phosphatase 1

PRO_0000068828

Sites

Active site

11

1

Nucleophile Probable

Active site

13

1

Proton donor Probable

Metal binding

11

1

Magnesium

Metal binding

13

1

Magnesium

Metal binding

123

1

Magnesium

Binding site

12

1

Phosphate; via amide nitrogen

Binding site

13

1

Phosphate; via amide nitrogen

Binding site

20

1

Substrate Probable

Binding site

69

1

Phosphate

Binding site

70

1

Phosphate

Binding site

70

1

Substrate Probable

Binding site

100

1

Phosphate

Experimental info

Mutagenesis

11

1

D → N or E: Abolishes enzymatic activity. Ref.4

Mutagenesis

13

1

D → N: 92% loss of enzymatic activity. Ref.4

Mutagenesis

69

1

S → A: Abolishes enzymatic activity. Ref.4

Mutagenesis

100

1

K → R: Abolishes enzymatic activity. Ref.4

Mutagenesis

103

1

H → K or A: 50% decrease in enzymatic activity. Ref.1

Mutagenesis

122

1

D → N: Abolishes enzymatic activity.

Mutagenesis

123

1

D → N: Abolishes enzymatic activity.

Mutagenesis

127

1

N → D: 50% decrease in enzymatic activity.

Mutagenesis

138

1

C → S, A or G: No effect on enzymatic activity. Ref.1

Secondary structure

1

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164

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Turn

13 – 15

3

Beta strand

16 – 19

4

Turn

21 – 23

3

Beta strand

29 – 31

3

Beta strand

37 – 39

3

Helix

51 – 60

10

Beta strand

65 – 69

5

Helix

74 – 83

10

Helix

87 – 89

3

Beta strand

90 – 98

9

Helix

100 – 111

12

Helix

115 – 117

3

Beta strand

118 – 123

6

Helix

125 – 132

8

Turn

133 – 135

3

Beta strand

137 – 140

4

Beta strand

142 – 144

3

Helix

147 – 160

14

Turn

161 – 163

3

Sequences

	Sequence		Length	Mass (Da)
	Q9D967 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 209D39404DCB1930	FASTA	164	18,582
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00112138.

RefSeq

NP_075886.1. NM_023397.4.

UniGene

Mm.24601.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U7O	X-ray	1.90	A	1-164	[»]
1U7P	X-ray	1.90	A/B/C/D	1-164	[»]

ProteinModelPortal

Q9D967.

SMR

Q9D967. Positions 1-164.

ModBase

Search...

PTM databases

PhosphoSite

Q9D967.

Proteomic databases

PaxDb

Q9D967.

PRIDE

Q9D967.

Protocols and materials databases

DNASU

67881.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000002400; ENSMUSP00000002400; ENSMUSG00000002329.

GeneID

67881.

KEGG

mmu:67881.

UCSC

uc007uaa.2. mouse.

Organism-specific databases

CTD

145553.

MGI

MGI:1915131. Mdp1.

Phylogenomic databases

eggNOG

NOG279690.

GeneTree

ENSGT00390000004110.

HOGENOM

HOG000216653.

HOVERGEN

HBG081971.

InParanoid

Q9D967.

OMA

NGMSLQT.

OrthoDB

EOG432107.

Gene expression databases

Bgee

Q9D967.

CleanEx

MM_1810034K20RIK.

Genevestigator

Q9D967.

GermOnline

ENSMUSG00000002329. Mus musculus.

Family and domain databases

Gene3D

3.40.50.1000. 1 hit.

InterPro

IPR023214. HAD-like_dom.
IPR010033. HAD_SF_ppase_IIIC.
IPR024734. MDP_1_eu.
IPR010036. MDP_1_eu_arc.
[Graphical view]

PANTHER

PTHR17901. PTHR17901. 1 hit.

Pfam

PF12689. Acid_PPase. 1 hit.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01681. HAD-SF-IIIC. 1 hit.
TIGR01685. MDP-1. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

MDP1. mouse.

EvolutionaryTrace

Q9D967.

NextBio

325825.

SOURCE

Search...

Entry information

Entry name

MGDP1_MOUSE

Accession

Primary (citable) accession number: Q9D967

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program