PPR17_MOUSE
ID PPR17_MOUSE Reviewed; 159 AA.
AC Q9Z2E4;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 17;
DE AltName: Full=G substrate;
GN Name=Ppp1r17; Synonyms=Gsbs;
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, PHOSPHORYLATION AT THR-72 AND
RP THR-123, MUTAGENESIS OF THR-72 AND THR-123, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9920894; DOI=10.1074/jbc.274.6.3485;
RA Hall K.U., Collins S.P., Gamm D.M., Massa E., Depaoli-Roach A.A.,
RA Uhler M.D.;
RT "Phosphorylation-dependent inhibition of protein phosphatase-1 by G-
RT substrate: a Purkinje cell substrate of the cyclic GMP-dependent protein
RT kinase.";
RL J. Biol. Chem. 274:3485-3495(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=12213562; DOI=10.1016/s0531-5565(02)00066-9;
RA Iida R., Yasuda T., Tsubota E., Takatsuka H., Masuyama M., Matsuki T.,
RA Kishi K.;
RT "Five age-dependently expressed genes in mouse brain revealed by the
RT fluorescence differential display-PCR technique.";
RL Exp. Gerontol. 37:1121-1126(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Inhibits phosphatase activities of protein phosphatase 1
CC (PP1) and protein phosphatase 2A (PP2A) complexes.
CC {ECO:0000269|PubMed:9920894}.
CC -!- TISSUE SPECIFICITY: Expressed in Purkinje cells of the cerebellum,
CC hippocampus, pons, medulla and eye. {ECO:0000269|PubMed:9920894}.
CC -!- PTM: Substrate for cGMP-dependent protein kinase (By similarity).
CC Phosphorylation of Thr-72 and Thr-123 is required for its phosphatase
CC activity. Phosphorylated by PRKG1 isoform alpha. {ECO:0000250,
CC ECO:0000269|PubMed:9920894}.
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DR EMBL; AF071562; AAD12589.1; -; mRNA.
DR EMBL; AF500906; AAM21706.1; -; mRNA.
DR EMBL; AK078335; BAC37224.1; -; mRNA.
DR EMBL; AC079365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466597; EDK98736.1; -; Genomic_DNA.
DR EMBL; BC026822; AAH26822.1; -; mRNA.
DR CCDS; CCDS20169.1; -.
DR RefSeq; NP_035283.1; NM_011153.3.
DR AlphaFoldDB; Q9Z2E4; -.
DR BioGRID; 202340; 1.
DR STRING; 10090.ENSMUSP00000059708; -.
DR iPTMnet; Q9Z2E4; -.
DR PhosphoSitePlus; Q9Z2E4; -.
DR MaxQB; Q9Z2E4; -.
DR PaxDb; Q9Z2E4; -.
DR PeptideAtlas; Q9Z2E4; -.
DR PRIDE; Q9Z2E4; -.
DR ProteomicsDB; 289383; -.
DR Antibodypedia; 26306; 148 antibodies from 15 providers.
DR DNASU; 19051; -.
DR Ensembl; ENSMUST00000052827; ENSMUSP00000059708; ENSMUSG00000002930.
DR GeneID; 19051; -.
DR KEGG; mmu:19051; -.
DR UCSC; uc009cay.1; mouse.
DR CTD; 10842; -.
DR MGI; MGI:1333876; Ppp1r17.
DR VEuPathDB; HostDB:ENSMUSG00000002930; -.
DR eggNOG; ENOG502S50G; Eukaryota.
DR GeneTree; ENSGT00390000005586; -.
DR HOGENOM; CLU_113768_0_0_1; -.
DR InParanoid; Q9Z2E4; -.
DR OMA; ISMMSTE; -.
DR OrthoDB; 1603863at2759; -.
DR PhylomeDB; Q9Z2E4; -.
DR TreeFam; TF335928; -.
DR BioGRID-ORCS; 19051; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ppp1r17; mouse.
DR PRO; PR:Q9Z2E4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9Z2E4; protein.
DR Bgee; ENSMUSG00000002930; Expressed in cerebellum lobe and 79 other tissues.
DR Genevisible; Q9Z2E4; MM.
DR GO; GO:0005829; C:cytosol; TAS:MGI.
DR GO; GO:0019212; F:phosphatase inhibitor activity; ISO:MGI.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:MGI.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:MGI.
DR GO; GO:0010921; P:regulation of phosphatase activity; IDA:UniProtKB.
DR InterPro; IPR033242; PPP1R17.
DR PANTHER; PTHR15387; PTHR15387; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Protein phosphatase inhibitor; Reference proteome.
FT CHAIN 1..159
FT /note="Protein phosphatase 1 regulatory subunit 17"
FT /id="PRO_0000414576"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphothreonine; by PKG/PRKG1"
FT /evidence="ECO:0000269|PubMed:9920894"
FT MOD_RES 123
FT /note="Phosphothreonine; by PKG/PRKG1"
FT /evidence="ECO:0000269|PubMed:9920894"
FT MUTAGEN 72
FT /note="T->A: Does not potentiate the phosphorylation of the
FT CREB transcription factor; when associated with A-123."
FT /evidence="ECO:0000269|PubMed:9920894"
FT MUTAGEN 123
FT /note="T->A: Does not potentiate the phosphorylation of the
FT CREB transcription factor; when associated with A-72."
FT /evidence="ECO:0000269|PubMed:9920894"
SQ SEQUENCE 159 AA; 17815 MW; 18B5ECA9E925856C CRC64;
MSTEMMTTEP VPPLELSDDI LGKLDPQCSP SDDLSDQFIK DCDLKKKPRK GKNVQATLNV
ESDQKKPRRK DTPAVHIPPF IPGVISEHLI KRYDVQERIP KAKSGPALHN SDMEQKRPRR
KDTPALHMPP FVAGLTLLRD ESAGVILEDE EMDGDKLAI
