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Magnesium-dependent phosphatase 1 (MDP-1) (EC 3.1.3.-) (EC 3.1.3.48)

 MGDP1_MOUSE             Reviewed;         164 AA.
Q9D967;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-FEB-2018, entry version 116.
RecName: Full=Magnesium-dependent phosphatase 1;
Short=MDP-1;
EC=3.1.3.-;
EC=3.1.3.48;
Name=Mdp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
COFACTOR, ENZYME REGULATION, AND MUTAGENESIS OF HIS-103 AND CYS-138.
PubMed=10889041; DOI=10.1021/bi0005052;
Selengut J.D., Levine R.L.;
"MDP-1: a novel eukaryotic magnesium-dependent phosphatase.";
Biochemistry 39:8315-8324(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
MUTAGENESIS OF ASP-11; ASP-13; SER-69 AND LYS-100, AND FUNCTION.
PubMed=11601995; DOI=10.1021/bi011405e;
Selengut J.D.;
"MDP-1 is a new and distinct member of the haloacid dehalogenase
family of aspartate-dependent phosphohydrolases.";
Biochemistry 40:12704-12711(2001).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-164, X-RAY CRYSTALLOGRAPHY
(1.9 ANGSTROMS) OF 1-164 WITH MAGNESIUM AND TUNGSTATE, AND FUNCTION.
PubMed=15461449; DOI=10.1021/bi0490688;
Peisach E., Selengut J.D., Dunaway-Mariano D., Allen K.N.;
"X-ray crystal structure of the hypothetical phosphotyrosine
phosphatase MDP-1 of the haloacid dehalogenase superfamily.";
Biochemistry 43:12770-12779(2004).
-!- FUNCTION: Magnesium-dependent phosphatase which may act as a
tyrosine phosphatase. {ECO:0000269|PubMed:10889041,
ECO:0000269|PubMed:11601995, ECO:0000269|PubMed:15461449}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10889041};
-!- ENZYME REGULATION: Inhibited by vanadate and zinc, and slightly by
calcium. {ECO:0000269|PubMed:10889041}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=9.5 mM for ribose-5-phosphate {ECO:0000269|PubMed:10889041};
KM=5.6 mM for 2-deoxy-ribose-5-phosphate
{ECO:0000269|PubMed:10889041};
KM=15 mM for phosphotyrosine {ECO:0000269|PubMed:10889041};
KM=1.1 mM for arabinose-5-phosphate
{ECO:0000269|PubMed:10889041};
KM=21 mM for fructose-6-phosphate {ECO:0000269|PubMed:10889041};
KM=12 mM for 5'-CMP {ECO:0000269|PubMed:10889041};
KM=1.7 mM for pNPP {ECO:0000269|PubMed:10889041};
KM=26 mM for 5'-AMP {ECO:0000269|PubMed:10889041};
KM=31 mM for glucose-6-phosphate {ECO:0000269|PubMed:10889041};
Note=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.;
pH dependence:
Optimum pH is 5.3. {ECO:0000269|PubMed:10889041};
-!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF230273; AAK00763.1; -; mRNA.
EMBL; AK007319; BAB24954.1; -; mRNA.
EMBL; AK160438; BAE35788.1; -; mRNA.
EMBL; BC046613; AAH46613.1; -; mRNA.
CCDS; CCDS27123.1; -.
RefSeq; NP_075886.1; NM_023397.4.
UniGene; Mm.24601; -.
PDB; 1U7O; X-ray; 1.90 A; A=1-164.
PDB; 1U7P; X-ray; 1.90 A; A/B/C/D=1-164.
PDBsum; 1U7O; -.
PDBsum; 1U7P; -.
ProteinModelPortal; Q9D967; -.
SMR; Q9D967; -.
IntAct; Q9D967; 1.
MINT; Q9D967; -.
iPTMnet; Q9D967; -.
PhosphoSitePlus; Q9D967; -.
EPD; Q9D967; -.
MaxQB; Q9D967; -.
PaxDb; Q9D967; -.
PeptideAtlas; Q9D967; -.
PRIDE; Q9D967; -.
DNASU; 67881; -.
Ensembl; ENSMUST00000002400; ENSMUSP00000002400; ENSMUSG00000002329.
GeneID; 67881; -.
KEGG; mmu:67881; -.
UCSC; uc007uaa.2; mouse.
CTD; 145553; -.
MGI; MGI:1915131; Mdp1.
eggNOG; KOG4549; Eukaryota.
eggNOG; ENOG4111PHW; LUCA.
GeneTree; ENSGT00390000004110; -.
HOGENOM; HOG000216653; -.
HOVERGEN; HBG081971; -.
InParanoid; Q9D967; -.
KO; K17619; -.
OMA; RGVWAWR; -.
OrthoDB; EOG091G0SQ5; -.
PhylomeDB; Q9D967; -.
TreeFam; TF328413; -.
SABIO-RK; Q9D967; -.
ChiTaRS; Mdp1; mouse.
EvolutionaryTrace; Q9D967; -.
PRO; PR:Q9D967; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000002329; -.
CleanEx; MM_1810034K20RIK; -.
Genevisible; Q9D967; MM.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0030389; P:fructosamine metabolic process; IEA:Ensembl.
CDD; cd07501; HAD_MDP-1_like; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR010033; HAD_SF_ppase_IIIC.
InterPro; IPR035679; MDP-1_euk.
InterPro; IPR010036; MDP_1_eu_arc.
PANTHER; PTHR17901; PTHR17901; 1.
Pfam; PF12689; Acid_PPase; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR01681; HAD-SF-IIIC; 1.
TIGRFAMs; TIGR01685; MDP-1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding;
Protein phosphatase; Reference proteome.
CHAIN 1 164 Magnesium-dependent phosphatase 1.
/FTId=PRO_0000068828.
ACT_SITE 11 11 Nucleophile. {ECO:0000305}.
ACT_SITE 13 13 Proton donor. {ECO:0000305}.
METAL 11 11 Magnesium.
METAL 13 13 Magnesium.
METAL 123 123 Magnesium.
BINDING 12 12 Phosphate; via amide nitrogen.
BINDING 13 13 Phosphate; via amide nitrogen.
BINDING 20 20 Substrate. {ECO:0000305}.
BINDING 69 69 Phosphate.
BINDING 70 70 Phosphate.
BINDING 70 70 Substrate. {ECO:0000305}.
BINDING 100 100 Phosphate.
MUTAGEN 11 11 D->N,E: Abolishes enzymatic activity.
{ECO:0000269|PubMed:11601995}.
MUTAGEN 13 13 D->N: 92% loss of enzymatic activity.
{ECO:0000269|PubMed:11601995}.
MUTAGEN 69 69 S->A: Abolishes enzymatic activity.
{ECO:0000269|PubMed:11601995}.
MUTAGEN 100 100 K->R: Abolishes enzymatic activity.
{ECO:0000269|PubMed:11601995}.
MUTAGEN 103 103 H->K,A: 50% decrease in enzymatic
activity. {ECO:0000269|PubMed:10889041}.
MUTAGEN 122 122 D->N: Abolishes enzymatic activity.
MUTAGEN 123 123 D->N: Abolishes enzymatic activity.
MUTAGEN 127 127 N->D: 50% decrease in enzymatic activity.
MUTAGEN 138 138 C->S,A,G: No effect on enzymatic
activity. {ECO:0000269|PubMed:10889041}.
STRAND 6 10 {ECO:0000244|PDB:1U7O}.
TURN 13 15 {ECO:0000244|PDB:1U7O}.
STRAND 16 19 {ECO:0000244|PDB:1U7O}.
TURN 21 23 {ECO:0000244|PDB:1U7O}.
STRAND 29 31 {ECO:0000244|PDB:1U7O}.
STRAND 37 39 {ECO:0000244|PDB:1U7O}.
HELIX 51 60 {ECO:0000244|PDB:1U7O}.
STRAND 65 69 {ECO:0000244|PDB:1U7O}.
HELIX 74 83 {ECO:0000244|PDB:1U7O}.
HELIX 87 89 {ECO:0000244|PDB:1U7O}.
STRAND 90 98 {ECO:0000244|PDB:1U7O}.
HELIX 100 111 {ECO:0000244|PDB:1U7O}.
HELIX 115 117 {ECO:0000244|PDB:1U7O}.
STRAND 118 123 {ECO:0000244|PDB:1U7O}.
HELIX 125 132 {ECO:0000244|PDB:1U7O}.
TURN 133 135 {ECO:0000244|PDB:1U7O}.
STRAND 137 140 {ECO:0000244|PDB:1U7O}.
STRAND 142 144 {ECO:0000244|PDB:1U7O}.
HELIX 147 160 {ECO:0000244|PDB:1U7O}.
TURN 161 163 {ECO:0000244|PDB:1U7P}.
SEQUENCE 164 AA; 18582 MW; 209D39404DCB1930 CRC64;
MTRLPKLAVF DLDYTLWPFW VDTHVDPPFH KSSDGTVRDR RGQNIQLYPE VPEVLGRLQS
LGVPVAAASR TSEIQGANQL LELFDLGKYF IQREIYPGSK VTHFERLHHK TGVPFSQMVF
FDDENRNIID VGRLGVTCIH IRDGMSLQTL TQGLETFAKA QAGL


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