MGDP1_HUMAN
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 03-AUG-2022, entry version 147.
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; 53.
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; Q86V88; -.
DR PeptideAtlas; Q86V88; -.
DR PRIDE; Q86V88; -.
DR ProteomicsDB; 69978; -. [Q86V88-1]
DR ProteomicsDB; 69979; -. [Q86V88-2]
DR ProteomicsDB; 69980; -. [Q86V88-3]
DR Antibodypedia; 22751; 56 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 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; RGVWAWR; -.
DR OrthoDB; 1249213at2759; -.
DR PhylomeDB; Q86V88; -.
DR TreeFam; TF328413; -.
DR PathwayCommons; Q86V88; -.
DR BioGRID-ORCS; 145553; 11 hits in 1068 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 prefrontal cortex and 94 other tissues.
DR Genevisible; Q86V88; HS.
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; -; 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; 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
