MGDP1_MOUSE
ID MGDP1_MOUSE Reviewed; 164 AA.
AC Q9D967;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Magnesium-dependent phosphatase 1;
DE Short=MDP-1;
DE EC=3.1.3.-;
DE EC=3.1.3.48;
GN Name=Mdp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, ACTIVITY REGULATION, AND MUTAGENESIS OF HIS-103 AND CYS-138.
RX PubMed=10889041; DOI=10.1021/bi0005052;
RA Selengut J.D., Levine R.L.;
RT "MDP-1: a novel eukaryotic magnesium-dependent phosphatase.";
RL Biochemistry 39:8315-8324(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP MUTAGENESIS OF ASP-11; ASP-13; SER-69 AND LYS-100, AND FUNCTION.
RX PubMed=11601995; DOI=10.1021/bi011405e;
RA Selengut J.D.;
RT "MDP-1 is a new and distinct member of the haloacid dehalogenase family of
RT aspartate-dependent phosphohydrolases.";
RL Biochemistry 40:12704-12711(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-164, X-RAY CRYSTALLOGRAPHY (1.9
RP ANGSTROMS) OF 1-164 WITH MAGNESIUM AND TUNGSTATE, AND FUNCTION.
RX PubMed=15461449; DOI=10.1021/bi0490688;
RA Peisach E., Selengut J.D., Dunaway-Mariano D., Allen K.N.;
RT "X-ray crystal structure of the hypothetical phosphotyrosine phosphatase
RT MDP-1 of the haloacid dehalogenase superfamily.";
RL Biochemistry 43:12770-12779(2004).
CC -!- FUNCTION: Magnesium-dependent phosphatase which may act as a tyrosine
CC phosphatase. {ECO:0000269|PubMed:10889041, ECO:0000269|PubMed:11601995,
CC ECO:0000269|PubMed:15461449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10889041};
CC -!- ACTIVITY REGULATION: Inhibited by vanadate and zinc, and slightly by
CC calcium. {ECO:0000269|PubMed:10889041}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.5 mM for ribose-5-phosphate {ECO:0000269|PubMed:10889041};
CC KM=5.6 mM for 2-deoxy-ribose-5-phosphate
CC {ECO:0000269|PubMed:10889041};
CC KM=15 mM for phosphotyrosine {ECO:0000269|PubMed:10889041};
CC KM=1.1 mM for arabinose-5-phosphate {ECO:0000269|PubMed:10889041};
CC KM=21 mM for fructose-6-phosphate {ECO:0000269|PubMed:10889041};
CC KM=12 mM for 5'-CMP {ECO:0000269|PubMed:10889041};
CC KM=1.7 mM for pNPP {ECO:0000269|PubMed:10889041};
CC KM=26 mM for 5'-AMP {ECO:0000269|PubMed:10889041};
CC KM=31 mM for glucose-6-phosphate {ECO:0000269|PubMed:10889041};
CC Note=Dephosphorylates ribose-5-phosphate, 2-deoxy-ribose-5-phosphate,
CC phosphotyrosine, arabinose-5-phosphate, fructose-6-phosphate, 5'-CMP,
CC pNPP, 5'-AMP and glucose-6-phosphate with a decreasing relative rate
CC of 1, 0.9, 0.8, 0.6, 0.5, 0.2, 0.2, 0.2 and 0.06. Dephosphorylates
CC phosphotyrosine with a greater than 100 fold rate over phosphoserine
CC or phosphothreonine.;
CC pH dependence:
CC Optimum pH is 5.3. {ECO:0000269|PubMed:10889041};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AF230273; AAK00763.1; -; mRNA.
DR EMBL; AK007319; BAB24954.1; -; mRNA.
DR EMBL; AK160438; BAE35788.1; -; mRNA.
DR EMBL; BC046613; AAH46613.1; -; mRNA.
DR CCDS; CCDS27123.1; -.
DR RefSeq; NP_075886.1; NM_023397.4.
DR PDB; 1U7O; X-ray; 1.90 A; A=1-164.
DR PDB; 1U7P; X-ray; 1.90 A; A/B/C/D=1-164.
DR PDBsum; 1U7O; -.
DR PDBsum; 1U7P; -.
DR AlphaFoldDB; Q9D967; -.
DR SMR; Q9D967; -.
DR BioGRID; 212506; 3.
DR STRING; 10090.ENSMUSP00000002400; -.
DR iPTMnet; Q9D967; -.
DR PhosphoSitePlus; Q9D967; -.
DR CPTAC; non-CPTAC-3839; -.
DR EPD; Q9D967; -.
DR jPOST; Q9D967; -.
DR MaxQB; Q9D967; -.
DR PaxDb; Q9D967; -.
DR PeptideAtlas; Q9D967; -.
DR PRIDE; Q9D967; -.
DR ProteomicsDB; 293468; -.
DR DNASU; 67881; -.
DR Ensembl; ENSMUST00000002400; ENSMUSP00000002400; ENSMUSG00000002329.
DR GeneID; 67881; -.
DR KEGG; mmu:67881; -.
DR UCSC; uc007uaa.2; mouse.
DR CTD; 145553; -.
DR MGI; MGI:1915131; Mdp1.
DR VEuPathDB; HostDB:ENSMUSG00000002329; -.
DR eggNOG; KOG4549; Eukaryota.
DR GeneTree; ENSGT00940000165797; -.
DR HOGENOM; CLU_071162_0_0_1; -.
DR InParanoid; Q9D967; -.
DR OMA; RGVWAWR; -.
DR OrthoDB; 1249213at2759; -.
DR PhylomeDB; Q9D967; -.
DR TreeFam; TF328413; -.
DR SABIO-RK; Q9D967; -.
DR BioGRID-ORCS; 67881; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Mdp1; mouse.
DR EvolutionaryTrace; Q9D967; -.
DR PRO; PR:Q9D967; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9D967; protein.
DR Bgee; ENSMUSG00000002329; Expressed in heart right ventricle and 250 other tissues.
DR Genevisible; Q9D967; MM.
DR GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0030389; P:fructosamine metabolic process; ISO:MGI.
DR CDD; cd07501; HAD_MDP-1_like; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR010033; HAD_SF_ppase_IIIC.
DR InterPro; IPR035679; MDP-1_euk.
DR InterPro; IPR010036; MDP_1_eu_arc.
DR PANTHER; PTHR17901; PTHR17901; 1.
DR Pfam; PF12689; Acid_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01681; HAD-SF-IIIC; 1.
DR TIGRFAMs; TIGR01685; MDP-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..164
FT /note="Magnesium-dependent phosphatase 1"
FT /id="PRO_0000068828"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 13
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 12
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 13
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 69
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT BINDING 70
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 100
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MUTAGEN 11
FT /note="D->N,E: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:11601995"
FT MUTAGEN 13
FT /note="D->N: 92% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:11601995"
FT MUTAGEN 69
FT /note="S->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:11601995"
FT MUTAGEN 100
FT /note="K->R: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:11601995"
FT MUTAGEN 103
FT /note="H->K,A: 50% decrease in enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10889041"
FT MUTAGEN 122
FT /note="D->N: Abolishes enzymatic activity."
FT MUTAGEN 123
FT /note="D->N: Abolishes enzymatic activity."
FT MUTAGEN 127
FT /note="N->D: 50% decrease in enzymatic activity."
FT MUTAGEN 138
FT /note="C->S,A,G: No effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10889041"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1U7O"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1U7O"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1U7O"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1U7O"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1U7O"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1U7O"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:1U7O"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1U7O"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1U7O"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1U7O"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:1U7O"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1U7O"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1U7O"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1U7O"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:1U7O"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1U7O"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1U7O"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1U7O"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:1U7O"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1U7P"
SQ SEQUENCE 164 AA; 18582 MW; 209D39404DCB1930 CRC64;
MTRLPKLAVF DLDYTLWPFW VDTHVDPPFH KSSDGTVRDR RGQNIQLYPE VPEVLGRLQS
LGVPVAAASR TSEIQGANQL LELFDLGKYF IQREIYPGSK VTHFERLHHK TGVPFSQMVF
FDDENRNIID VGRLGVTCIH IRDGMSLQTL TQGLETFAKA QAGL
