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PPTC7_HUMAN
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   03-AUG-2022, entry version 145.
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; 49.
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; Q8NI37; -.
DR   PeptideAtlas; Q8NI37; -.
DR   PRIDE; Q8NI37; -.
DR   ProteomicsDB; 73828; -.
DR   Antibodypedia; 50198; 120 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   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; MQSIYWT; -.
DR   OrthoDB; 826926at2759; -.
DR   PhylomeDB; Q8NI37; -.
DR   TreeFam; TF315105; -.
DR   PathwayCommons; Q8NI37; -.
DR   SignaLink; Q8NI37; -.
DR   BioGRID-ORCS; 160760; 18 hits in 1081 CRISPR screens.
DR   ChiTaRS; PPTC7; human.
DR   GenomeRNAi; 160760; -.
DR   Pharos; Q8NI37; Tdark.
DR   PRO; PR:Q8NI37; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q8NI37; protein.
DR   Bgee; ENSG00000196850; Expressed in left ventricle myocardium and 193 other 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; -; 1.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   InterPro; IPR039123; PPTC7.
DR   PANTHER; PTHR12320; PTHR12320; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 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
 
 
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