ID   MGDP1_HUMAN             Reviewed;         176 AA.
AC   Q86V88; Q86Y84; Q8NAD9;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 153.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Small intestine;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Brain, and Liver;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Magnesium-dependent phosphatase which may act as a tyrosine
CC       phosphatase. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by vanadate and zinc, and slightly by
CC       calcium. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q86V88-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86V88-2; Sequence=VSP_015986, VSP_015987;
CC       Name=3;
CC         IsoId=Q86V88-3; Sequence=VSP_015985, VSP_015988;
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AK092821; BAC03984.1; -; mRNA.
DR   EMBL; BC046912; AAH46912.1; -; mRNA.
DR   EMBL; BC051382; AAH51382.1; -; mRNA.
DR   CCDS; CCDS55908.1; -. [Q86V88-3]
DR   CCDS; CCDS9620.1; -. [Q86V88-1]
DR   RefSeq; NP_001186750.1; NM_001199821.1. [Q86V88-3]
DR   RefSeq; NP_612485.2; NM_138476.3. [Q86V88-1]
DR   PDB; 2WM8; X-ray; 1.75 A; A=1-165.
DR   PDBsum; 2WM8; -.
DR   AlphaFoldDB; Q86V88; -.
DR   SMR; Q86V88; -.
DR   BioGRID; 126921; 54.
DR   STRING; 9606.ENSP00000288087; -.
DR   DEPOD; MDP1; -.
DR   iPTMnet; Q86V88; -.
DR   PhosphoSitePlus; Q86V88; -.
DR   BioMuta; MDP1; -.
DR   DMDM; 74727544; -.
DR   EPD; Q86V88; -.
DR   jPOST; Q86V88; -.
DR   MassIVE; Q86V88; -.
DR   MaxQB; Q86V88; -.
DR   PaxDb; 9606-ENSP00000288087; -.
DR   PeptideAtlas; Q86V88; -.
DR   ProteomicsDB; 69978; -. [Q86V88-1]
DR   ProteomicsDB; 69979; -. [Q86V88-2]
DR   ProteomicsDB; 69980; -. [Q86V88-3]
DR   Pumba; Q86V88; -.
DR   Antibodypedia; 22751; 55 antibodies from 14 providers.
DR   DNASU; 145553; -.
DR   Ensembl; ENST00000288087.12; ENSP00000288087.7; ENSG00000213920.9. [Q86V88-1]
DR   Ensembl; ENST00000396833.2; ENSP00000380045.2; ENSG00000213920.9. [Q86V88-3]
DR   Ensembl; ENST00000644853.1; ENSP00000493831.1; ENSG00000285200.2. [Q86V88-3]
DR   Ensembl; ENST00000646165.2; ENSP00000494235.1; ENSG00000285200.2. [Q86V88-1]
DR   GeneID; 145553; -.
DR   KEGG; hsa:145553; -.
DR   MANE-Select; ENST00000288087.12; ENSP00000288087.7; NM_138476.4; NP_612485.2.
DR   UCSC; uc001wnl.3; human. [Q86V88-1]
DR   AGR; HGNC:28781; -.
DR   CTD; 145553; -.
DR   DisGeNET; 145553; -.
DR   GeneCards; MDP1; -.
DR   HGNC; HGNC:28781; MDP1.
DR   HPA; ENSG00000213920; Low tissue specificity.
DR   neXtProt; NX_Q86V88; -.
DR   OpenTargets; ENSG00000213920; -.
DR   PharmGKB; PA165479165; -.
DR   VEuPathDB; HostDB:ENSG00000213920; -.
DR   eggNOG; KOG4549; Eukaryota.
DR   GeneTree; ENSGT00390000004110; -.
DR   HOGENOM; CLU_071162_0_0_1; -.
DR   InParanoid; Q86V88; -.
DR   OMA; GVWAWRK; -.
DR   OrthoDB; 1327738at2759; -.
DR   PhylomeDB; Q86V88; -.
DR   TreeFam; TF328413; -.
DR   PathwayCommons; Q86V88; -.
DR   BioGRID-ORCS; 145553; 14 hits in 1158 CRISPR screens.
DR   EvolutionaryTrace; Q86V88; -.
DR   GenomeRNAi; 145553; -.
DR   Pharos; Q86V88; Tbio.
DR   PRO; PR:Q86V88; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q86V88; Protein.
DR   Bgee; ENSG00000213920; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 96 other cell types or tissues.
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:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07501; HAD_MDP-1_like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01681; HAD-SF-IIIC; 1.
DR   NCBIfam; TIGR01685; MDP-1; 1.
DR   PANTHER; PTHR17901:SF14; MAGNESIUM-DEPENDENT PHOSPHATASE 1; 1.
DR   PANTHER; PTHR17901; MAGNESIUM-DEPENDENT PHOSPHATASE 1 MDP1; 1.
DR   Pfam; PF12689; Acid_PPase; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDF00041; mdp-1; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   Genevisible; Q86V88; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Hydrolase; Magnesium; Metal-binding;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..176
FT                   /note="Magnesium-dependent phosphatase 1"
FT                   /id="PRO_0000068827"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        13
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         89..122
FT                   /note="YFVHREIYPGSKITHFERLQQKTGIPFSQMIFFD -> CYLHSHPEWNESSN
FT                   SKSRVRDICEGPNWAFEVQP (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015985"
FT   VAR_SEQ         107..127
FT                   /note="LQQKTGIPFSQMIFFDDERRN -> YAEIREEQGEKVSERPGKPRY (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_015986"
FT   VAR_SEQ         123..176
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015988"
FT   VAR_SEQ         128..176
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_015987"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   TURN            13..15
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   STRAND          16..19
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   TURN            21..23
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   HELIX           51..61
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   HELIX           74..83
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   STRAND          90..98
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   HELIX           100..111
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   STRAND          118..123
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   HELIX           125..132
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   STRAND          137..140
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:2WM8"
FT   HELIX           147..159
FT                   /evidence="ECO:0007829|PDB:2WM8"
SQ   SEQUENCE   176 AA;  20109 MW;  B0A33BD02458B2EF CRC64;
     MARLPKLAVF DLDYTLWPFW VDTHVDPPFH KSSDGTVRDR RGQDVRLYPE VPEVLKRLQS
     LGVPGAAASR TSEIEGANQL LELFDLFRYF VHREIYPGSK ITHFERLQQK TGIPFSQMIF
     FDDERRNIVD VSKLGVTCIH IQNGMNLQTL SQGLETFAKA QTGPLRSSLE ESPFEA
//