ID PPTC7_HUMAN Reviewed; 304 AA.
AC Q8NI37; B3KWC5; Q68DZ7; Q6UY82;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=Protein phosphatase PTC7 homolog;
DE EC=3.1.3.16 {ECO:0000255|PROSITE-ProRule:PRU01082, ECO:0000269|PubMed:30267671};
DE AltName: Full=T-cell activation protein phosphatase 2C;
DE Short=TA-PP2C;
DE AltName: Full=T-cell activation protein phosphatase 2C-like;
DE Flags: Precursor;
GN Name=PPTC7; Synonyms=TAPP2C;
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 [MRNA], AND INDUCTION.
RX PubMed=15177553; DOI=10.1016/j.ygeno.2003.12.019;
RA Mao M., Biery M.C., Kobayashi S.V., Ward T., Schimmack G., Burchard J.,
RA Schelter J.M., Dai H., He Y.D., Linsley P.S.;
RT "T lymphocyte activation gene identification by coregulated expression on
RT DNA microarrays.";
RL Genomics 83:989-999(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Zhou G., Zhong G., Yu R., Li H., Shen C., Li M., Ke R., Xiao W., Zheng G.,
RA Lin L., Yang S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-304.
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=29043977; DOI=10.7554/elife.27356;
RA Mishra A., Oules B., Pisco A.O., Ly T., Liakath-Ali K., Walko G.,
RA Viswanathan P., Tihy M., Nijjher J., Dunn S.J., Lamond A.I., Watt F.M.;
RT "A protein phosphatase network controls the temporal and spatial dynamics
RT of differentiation commitment in human epidermis.";
RL Elife 6:0-0(2017).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=30267671; DOI=10.1016/j.bbabio.2018.09.369;
RA Gonzalez-Mariscal I., Martin-Montalvo A., Vazquez-Fonseca L.,
RA Pomares-Viciana T., Sanchez-Cuesta A., Fernandez-Ayala D.J., Navas P.,
RA Santos-Ocana C.;
RT "The mitochondrial phosphatase PPTC7 orchestrates mitochondrial metabolism
RT regulating coenzyme Q10 biosynthesis.";
RL Biochim. Biophys. Acta 1859:1235-1248(2018).
CC -!- FUNCTION: Protein phosphatase which positively regulates biosynthesis
CC of the ubiquinone, coenzyme Q (PubMed:30267671). Dephosphorylates the
CC ubiquinone biosynthesis protein COQ7 which is likely to lead to its
CC activation (PubMed:30267671). {ECO:0000269|PubMed:30267671}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:30267671};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:30267671};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:30267671};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU01082};
CC -!- ACTIVITY REGULATION: Inhibited by sodium orthovanadate.
CC {ECO:0000269|PubMed:30267671}.
CC -!- INTERACTION:
CC Q8NI37; P41182: BCL6; NbExp=3; IntAct=EBI-9089276, EBI-765407;
CC Q8NI37; Q12983: BNIP3; NbExp=8; IntAct=EBI-9089276, EBI-749464;
CC Q8NI37; G5E9A7: DMWD; NbExp=3; IntAct=EBI-9089276, EBI-10976677;
CC Q8NI37; P07196: NEFL; NbExp=3; IntAct=EBI-9089276, EBI-475646;
CC Q8NI37; Q96AQ6: PBXIP1; NbExp=3; IntAct=EBI-9089276, EBI-740845;
CC Q8NI37; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-9089276, EBI-5235340;
CC Q8NI37; O76024: WFS1; NbExp=3; IntAct=EBI-9089276, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:30267671}.
CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level).
CC {ECO:0000269|PubMed:29043977}.
CC -!- INDUCTION: By hydrogen peroxide and nutrional stress (such as low
CC glucose) (PubMed:30267671). Up-regulated during lymphocyte activation
CC (PubMed:15177553). {ECO:0000269|PubMed:15177553,
CC ECO:0000269|PubMed:30267671}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AF385435; AAM43836.1; -; mRNA.
DR EMBL; AY357944; AAQ57274.1; -; mRNA.
DR EMBL; AK124744; BAG54087.1; -; mRNA.
DR EMBL; CH471054; EAW97928.1; -; Genomic_DNA.
DR EMBL; BC111551; AAI11552.1; -; mRNA.
DR EMBL; CR749216; CAH18073.1; -; mRNA.
DR CCDS; CCDS9149.1; -.
DR RefSeq; NP_644812.1; NM_139283.1.
DR AlphaFoldDB; Q8NI37; -.
DR SMR; Q8NI37; -.
DR BioGRID; 127764; 76.
DR IntAct; Q8NI37; 50.
DR STRING; 9606.ENSP00000346255; -.
DR DEPOD; PPTC7; -.
DR iPTMnet; Q8NI37; -.
DR PhosphoSitePlus; Q8NI37; -.
DR BioMuta; PPTC7; -.
DR DMDM; 74715714; -.
DR EPD; Q8NI37; -.
DR jPOST; Q8NI37; -.
DR MassIVE; Q8NI37; -.
DR MaxQB; Q8NI37; -.
DR PaxDb; 9606-ENSP00000346255; -.
DR PeptideAtlas; Q8NI37; -.
DR ProteomicsDB; 73828; -.
DR Pumba; Q8NI37; -.
DR Antibodypedia; 50198; 133 antibodies from 17 providers.
DR DNASU; 160760; -.
DR Ensembl; ENST00000354300.5; ENSP00000346255.3; ENSG00000196850.6.
DR GeneID; 160760; -.
DR KEGG; hsa:160760; -.
DR MANE-Select; ENST00000354300.5; ENSP00000346255.3; NM_139283.2; NP_644812.1.
DR UCSC; uc001trh.2; human.
DR AGR; HGNC:30695; -.
DR CTD; 160760; -.
DR DisGeNET; 160760; -.
DR GeneCards; PPTC7; -.
DR HGNC; HGNC:30695; PPTC7.
DR HPA; ENSG00000196850; Tissue enhanced (tongue).
DR MIM; 609668; gene.
DR neXtProt; NX_Q8NI37; -.
DR OpenTargets; ENSG00000196850; -.
DR PharmGKB; PA143485580; -.
DR VEuPathDB; HostDB:ENSG00000196850; -.
DR eggNOG; KOG1379; Eukaryota.
DR GeneTree; ENSGT00390000011937; -.
DR HOGENOM; CLU_029404_3_0_1; -.
DR InParanoid; Q8NI37; -.
DR OMA; CGFPKDF; -.
DR OrthoDB; 240602at2759; -.
DR PhylomeDB; Q8NI37; -.
DR TreeFam; TF315105; -.
DR PathwayCommons; Q8NI37; -.
DR SignaLink; Q8NI37; -.
DR BioGRID-ORCS; 160760; 24 hits in 1161 CRISPR screens.
DR ChiTaRS; PPTC7; human.
DR GenomeRNAi; 160760; -.
DR Pharos; Q8NI37; Tbio.
DR PRO; PR:Q8NI37; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8NI37; Protein.
DR Bgee; ENSG00000196850; Expressed in left ventricle myocardium and 195 other cell types or tissues.
DR Genevisible; Q8NI37; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IMP:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IMP:UniProtKB.
DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PROTEIN PHOSPHATASE 2C; 1.
DR PANTHER; PTHR12320:SF1; PROTEIN PHOSPHATASE PTC7 HOMOLOG; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW Protein phosphatase; Reference proteome; Transit peptide.
FT TRANSIT 1..68
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 69..304
FT /note="Protein phosphatase PTC7 homolog"
FT /id="PRO_0000328745"
FT DOMAIN 69..299
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 223
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT CONFLICT 27
FT /note="Missing (in Ref. 2; AAQ57274)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="C -> R (in Ref. 2; AAQ57274)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="L -> S (in Ref. 6; CAH18073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 32646 MW; E27F2FAF8C44793B CRC64;
MFSVLSYGRL VARAVLGGLS QTDPRAGGGG GGDYGLVTAG CGFGKDFRKG LLKKGACYGD
DACFVARHRS ADVLGVADGV GGWRDYGVDP SQFSGTLMRT CERLVKEGRF VPSNPIGILT
TSYCELLQNK VPLLGSSTAC IVVLDRTSHR LHTANLGDSG FLVVRGGEVV HRSDEQQHYF
NTPFQLSIAP PEAEGVVLSD SPDAADSTSF DVQLGDIILT ATDGLFDNMP DYMILQELKK
LKNSNYESIQ QTARSIAEQA HELAYDPNYM SPFAQFACDN GLNVRGGKPD DITVLLSIVA
EYTD
//
