PPR3F_MOUSE
ID PPR3F_MOUSE Reviewed; 799 AA.
AC Q9JIG4; B1AW09; B1AW10; Q3UGL4; Q6PCL6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3F;
DE Short=R3F;
GN Name=Ppp1r3f; Synonyms=DXImx48e;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-799 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 44-799 (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=10857745; DOI=10.1006/geno.2000.6173;
RA Means G.D., Toy D.Y., Baum P.R., Derry J.M.J.;
RT "A transcript map of a 2-Mb BAC contig in the proximal portion of the mouse
RT X chromosome and regional mapping of the scurfy mutation.";
RL Genomics 65:213-223(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-735 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Melanocyte;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545; SER-587 AND SER-592, AND
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP PHE-39.
RX PubMed=21668450; DOI=10.1111/j.1471-4159.2011.07345.x;
RA Kelsall I.R., Voss M., Munro S., Cuthbertson D.J., Cohen P.T.;
RT "R3F, a novel membrane-associated glycogen targeting subunit of protein
RT phosphatase 1 regulates glycogen synthase in astrocytoma cells in response
RT to glucose and extracellular signals.";
RL J. Neurochem. 118:596-610(2011).
CC -!- FUNCTION: Glycogen-targeting subunit for protein phosphatase 1 (PP1).
CC {ECO:0000269|PubMed:21668450}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:21668450}; Single-
CC pass membrane protein {ECO:0000269|PubMed:21668450}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JIG4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JIG4-2; Sequence=VSP_021363;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain (at protein level).
CC {ECO:0000269|PubMed:21668450}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF66954.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH59275.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM14759.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL731793; CAM14759.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL731793; CAM14760.1; -; Genomic_DNA.
DR EMBL; BC059275; AAH59275.1; ALT_INIT; mRNA.
DR EMBL; AF229644; AAF66954.2; ALT_INIT; mRNA.
DR EMBL; AK147873; BAE28194.1; -; mRNA.
DR CCDS; CCDS29964.2; -. [Q9JIG4-1]
DR CCDS; CCDS72328.1; -. [Q9JIG4-2]
DR RefSeq; NP_613071.3; NM_138605.3. [Q9JIG4-1]
DR AlphaFoldDB; Q9JIG4; -.
DR SMR; Q9JIG4; -.
DR BioGRID; 207708; 1.
DR IntAct; Q9JIG4; 1.
DR STRING; 10090.ENSMUSP00000122903; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR iPTMnet; Q9JIG4; -.
DR PhosphoSitePlus; Q9JIG4; -.
DR PaxDb; Q9JIG4; -.
DR PRIDE; Q9JIG4; -.
DR ProteomicsDB; 291843; -. [Q9JIG4-1]
DR ProteomicsDB; 291844; -. [Q9JIG4-2]
DR Antibodypedia; 338; 71 antibodies from 17 providers.
DR Ensembl; ENSMUST00000115742; ENSMUSP00000111407; ENSMUSG00000039556. [Q9JIG4-1]
DR Ensembl; ENSMUST00000150787; ENSMUSP00000122903; ENSMUSG00000039556. [Q9JIG4-2]
DR GeneID; 54646; -.
DR KEGG; mmu:54646; -.
DR UCSC; uc009slj.2; mouse. [Q9JIG4-1]
DR UCSC; uc057aqo.1; mouse. [Q9JIG4-2]
DR CTD; 89801; -.
DR MGI; MGI:1859617; Ppp1r3f.
DR VEuPathDB; HostDB:ENSMUSG00000039556; -.
DR eggNOG; KOG3986; Eukaryota.
DR GeneTree; ENSGT00390000013859; -.
DR HOGENOM; CLU_019259_1_0_1; -.
DR InParanoid; Q9JIG4; -.
DR OMA; NMDDNTP; -.
DR PhylomeDB; Q9JIG4; -.
DR TreeFam; TF352142; -.
DR BioGRID-ORCS; 54646; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ccdc22; mouse.
DR PRO; PR:Q9JIG4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9JIG4; protein.
DR Bgee; ENSMUSG00000039556; Expressed in dentate gyrus of hippocampal formation granule cell and 62 other tissues.
DR ExpressionAtlas; Q9JIG4; baseline and differential.
DR Genevisible; Q9JIG4; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR GO; GO:2001069; F:glycogen binding; ISO:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:2000465; P:regulation of glycogen (starch) synthase activity; ISO:MGI.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; ISO:MGI.
DR Gene3D; 2.60.40.2440; -; 1.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
DR Pfam; PF03370; CBM_21; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..799
FT /note="Protein phosphatase 1 regulatory subunit 3F"
FT /id="PRO_0000257497"
FT TOPO_DOM 1..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..799
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 127..283
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 36..39
FT /note="PP1-binding motif"
FT COMPBIAS 76..98
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSY5"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 377
FT /note="L -> LQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021363"
FT MUTAGEN 39
FT /note="F->A: Abrogates PP1-binding."
FT /evidence="ECO:0000269|PubMed:21668450"
FT CONFLICT 266
FT /note="T -> N (in Ref. 2; AAH59275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 84120 MW; DF6572A80FECB7BC CRC64;
MARTAPVEPP LRHPAPPSPA AGEPRASAEA AVAPRRVLFA DEALGLPLAQ LRRYRPWGGP
GAGKMAAATG QDGGGGGADE EDDGEDGDEG EEEEEAFPDP SPPCPVPAGG GFYLVPTFSL
PPALGRLERL GRVMVELEAL LPPPGAVPGG SGVWVPGGRP PVVRGLVRVL NRSFEKAVHV
RASHDGWATF CDHPARYVPR SPPGAGVGGT GAGDPLLDPG LGLGPGQMSA SSPDDGGCTD
RFAFQLPFAE GASDGARLDF VVRYETPEGT FWANNHGRNY TVLLRIAPAP TPTDAEGLPQ
QQQLQQLEPQ PECQGPVEAE ARQLKSCMKP VRRRPFEEEP RMRSADDNTL AEHPDVRESL
GPLLAPTPLR PWPQMTLQVP EVMLTSNPQE EGDIPRSNPP VAFTEVRQAP AIRILPATCG
LGGPPRDQAS GPDASDRAAG SFLEPTQQQV EAAWESGGGR KAPMVGALTD EPARGLEIVS
GLDELLGEDT IDQELEQLYL SHLSRLRAVA AAGGGEGTSP THALGILTDR DLILKWPGPE
RALNSALAEE ITLHYARLGC GVELIKDTED PDDEGEGEDG LSITPSSPEG GSPKESPPEI
LSGARSVIAT MGDVWVPWAE RSSSRCDSPV VLGTQGQFTE NPEKGMGKDT KSLHLNRVIV
GMSKSPGEAG TESQMEELPT ERESSWVPSS EKELPLPVQQ EQSPALLGPT GTEVCLSSVA
KPHVNSQEEE GGSLNLESPK RSPMPAAPAE CACGLAPQLW GPLTQTLGVL AGLVMVPVAL
NSGVSLLVLV LCLSLAWFS
