PP6R3_MOUSE
ID PP6R3_MOUSE Reviewed; 844 AA.
AC Q922D4; Q6ZPM9; Q8BTW6; Q9D2X9;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 3;
DE AltName: Full=SAPS domain family member 3;
GN Name=Ppp6r3; Synonyms=D19Ertd703e, Kiaa1558, Pp6r3, Saps3;
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 MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, Thymus, and Urinary bladder;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16769727; DOI=10.1074/jbc.m601772200;
RA Stefansson B., Brautigan D.L.;
RT "Protein phosphatase 6 subunit with conserved Sit4-associated protein
RT domain targets IkappaBepsilon.";
RL J. Biol. Chem. 281:22624-22634(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; THR-820 AND SER-824, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-550; SER-588;
RP THR-820 AND SER-824, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525
RP (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Regulatory subunit of protein phosphatase 6 (PP6). May
CC function as a scaffolding PP6 subunit. May have an important role in
CC maintaining immune self-tolerance (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a
CC heterotrimeric complex formed by the catalytic subunit, a SAPS domain-
CC containing subunit (PP6R) and an ankyrin repeat-domain containing
CC regulatory subunit (ARS). Interacts with PPP6C and ANKRD28 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q922D4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q922D4-2; Sequence=VSP_017145;
CC Name=3;
CC IsoId=Q922D4-3; Sequence=VSP_017146, VSP_017147;
CC Name=4;
CC IsoId=Q922D4-4; Sequence=VSP_017148, VSP_017149;
CC -!- TISSUE SPECIFICITY: Strongest expression observed in lung, spleen,
CC bladder and liver and weaker levels present in brain, heart, kidney,
CC skeletal muscle and pancreas. {ECO:0000269|PubMed:16769727}.
CC -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98202.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129392; BAC98202.1; ALT_INIT; mRNA.
DR EMBL; AK018652; BAB31326.1; -; mRNA.
DR EMBL; AK035236; BAC28993.1; -; mRNA.
DR EMBL; AK088526; BAC40403.1; -; mRNA.
DR EMBL; BC008529; AAH08529.1; -; mRNA.
DR CCDS; CCDS29397.1; -. [Q922D4-1]
DR CCDS; CCDS50340.1; -. [Q922D4-2]
DR RefSeq; NP_001157631.1; NM_001164159.1. [Q922D4-2]
DR RefSeq; NP_083275.1; NM_028999.1.
DR RefSeq; NP_083732.1; NM_029456.2. [Q922D4-1]
DR RefSeq; XP_006531859.1; XM_006531796.1.
DR AlphaFoldDB; Q922D4; -.
DR SMR; Q922D4; -.
DR BioGRID; 206340; 15.
DR IntAct; Q922D4; 19.
DR MINT; Q922D4; -.
DR STRING; 10090.ENSMUSP00000109630; -.
DR iPTMnet; Q922D4; -.
DR PhosphoSitePlus; Q922D4; -.
DR EPD; Q922D4; -.
DR jPOST; Q922D4; -.
DR MaxQB; Q922D4; -.
DR PaxDb; Q922D4; -.
DR PeptideAtlas; Q922D4; -.
DR PRIDE; Q922D4; -.
DR ProteomicsDB; 289723; -. [Q922D4-1]
DR ProteomicsDB; 289724; -. [Q922D4-2]
DR ProteomicsDB; 289725; -. [Q922D4-3]
DR ProteomicsDB; 289726; -. [Q922D4-4]
DR Antibodypedia; 30575; 78 antibodies from 19 providers.
DR Ensembl; ENSMUST00000025846; ENSMUSP00000025846; ENSMUSG00000024908. [Q922D4-1]
DR Ensembl; ENSMUST00000172362; ENSMUSP00000131084; ENSMUSG00000024908. [Q922D4-2]
DR GeneID; 52036; -.
DR KEGG; mmu:52036; -.
DR UCSC; uc008fwk.3; mouse. [Q922D4-1]
DR UCSC; uc008fwl.3; mouse. [Q922D4-2]
DR UCSC; uc008fwm.2; mouse. [Q922D4-3]
DR UCSC; uc008fwo.2; mouse. [Q922D4-4]
DR CTD; 55291; -.
DR MGI; MGI:1921807; Ppp6r3.
DR VEuPathDB; HostDB:ENSMUSG00000024908; -.
DR eggNOG; KOG2073; Eukaryota.
DR GeneTree; ENSGT00390000009899; -.
DR InParanoid; Q922D4; -.
DR OrthoDB; 329232at2759; -.
DR PhylomeDB; Q922D4; -.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR BioGRID-ORCS; 52036; 16 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp6r3; mouse.
DR PRO; PR:Q922D4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q922D4; protein.
DR Bgee; ENSMUSG00000024908; Expressed in rostral migratory stream and 253 other tissues.
DR ExpressionAtlas; Q922D4; baseline and differential.
DR Genevisible; Q922D4; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..844
FT /note="Serine/threonine-protein phosphatase 6 regulatory
FT subunit 3"
FT /id="PRO_0000046101"
FT REGION 599..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 602
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5H9R7"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5H9R7"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5H9R7"
FT MOD_RES 820
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 487..497
FT /note="DLPDEVRERWE -> GKLVNNLITCV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_017148"
FT VAR_SEQ 498..844
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_017149"
FT VAR_SEQ 516..548
FT /note="AFSDYQMQQMTSNFIDQFGFNDEKFADQDDIGN -> VTTCHIHSSSDDEID
FT FKDTGFSQDSSLQQVSHT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017146"
FT VAR_SEQ 516..532
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017145"
FT VAR_SEQ 549..844
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017147"
FT MOD_RES Q922D4-3:525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 844 AA; 94653 MW; 1C70ED57ECEF1D45 CRC64;
MFWKFDLHSS SHIDTLLERE DVTLKELMDE EDVLQECKAQ NRKLIEFLLK AECLEDLVSF
IIEEPPQDMD EKIRYKYPNI SCELLTSDVS QMNDRLGEDE SLLMKLYSFL LNESPLNPLL
ASFFSKVLSI LISRKPEQIV DFLKKKRDFV DLIIKHIGTS AIMDLLLRLL TCIEPPQPRQ
DVLNWLNEER IIQRLVEIVH PSQEEDRHSN ASQSLCEIVR LSRDQMLQVQ NSTEPDPLLA
TLEKQEIIEQ LLSNIFHKEK NESAIVSAIQ ILLTLLETRR PTFEGHIEIC PPGMSHSACS
VNKSVLEAIR GRLGSFHELL LEPPKKSVMK TTWGILDPPV GNTRLNVIRL ISSLLQTNTS
SINGDLMELN SIGVILDMFF KYTWNNFLHT QVEICIALIL ASPFENAENG TITDQDSTGD
NLLLKHLFQK CQLIERILEA WDTNEKKQAE GGRRHGYMGH LTRIANCIVH STDKGPNSAL
VQQLIKDLPD EVRERWETFC TNSLGETNKR NTVDLAFSDY QMQQMTSNFI DQFGFNDEKF
ADQDDIGNVS FDRVSDINFT LNTNESGNIA LFEACCKERI QQFDDGGSDE EDIWEEKHIA
FTPESQRRSS SGSTDSEEST DSEEEDGAKQ DLFESSSANT EDKMEVDLNE PPTWSANFDV
PMETTHGAPL DSVGSDVWST EEPMPTKETG WASFSEFTSS LSTKESLRSN SPVEMETSTE
SVDPLTPGAA ALATQPEAPG SMAMEASSDG EEDAESTDKV TETVMNGGMK ETLSLTVDAK
TETAVFKSEE EKLSTSQDAA CKDAEETPEP AEAKCTAPLT PSSSPEQRTD QPSMPSDPSV
NGPV
