P4R3A_MOUSE
ID P4R3A_MOUSE Reviewed; 820 AA.
AC Q6P2K6; Q3UF79; Q69Z35; Q80VS2; Q8BKP7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 3A {ECO:0000250|UniProtKB:Q6IN85};
DE AltName: Full=SMEK homolog 1;
GN Name=Ppp4r3a {ECO:0000250|UniProtKB:Q6IN85};
GN Synonyms=Kiaa2010, Pp4r3a, Smek1;
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 1).
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Spinal ganglion, Spleen, and Sympathetic ganglion;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and 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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-755; SER-758;
RP SER-761; SER-764 AND SER-767, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-642, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4.
CC May regulate the activity of PPP4C at centrosomal microtubule
CC organizing centers. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically
CC dephosphorylates H2AX phosphorylated on 'Ser-140' (gamma-H2AX)
CC generated during DNA replication and required for DNA DSB repair (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits. Component of the PP4 complex PPP4C-PPP4R2-PPP4R3A. Interacts
CC with PPP4C; the interaction requires PPP4R2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=In interphase localized in the cytoplasm and in the
CC nucleus (with higher levels). During metaphase located in
CC pericentriolar regions (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P2K6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P2K6-2; Sequence=VSP_021257;
CC -!- SIMILARITY: Belongs to the SMEK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32609.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173331; BAD32609.1; ALT_INIT; Transcribed_RNA.
DR EMBL; AK051239; BAC34569.2; -; mRNA.
DR EMBL; AK148868; BAE28682.1; -; mRNA.
DR EMBL; AK156272; BAE33651.1; -; mRNA.
DR EMBL; BC044817; AAH44817.1; -; mRNA.
DR EMBL; BC064465; AAH64465.1; -; mRNA.
DR CCDS; CCDS26111.1; -. [Q6P2K6-1]
DR RefSeq; NP_001153686.1; NM_001160214.1.
DR RefSeq; NP_997594.1; NM_211355.2. [Q6P2K6-1]
DR AlphaFoldDB; Q6P2K6; -.
DR BioGRID; 213022; 27.
DR ComplexPortal; CPX-158; PPP4C-PPP4R2-PPP4R3A protein phosphatase 4 complex.
DR IntAct; Q6P2K6; 18.
DR MINT; Q6P2K6; -.
DR STRING; 10090.ENSMUSP00000129654; -.
DR iPTMnet; Q6P2K6; -.
DR PhosphoSitePlus; Q6P2K6; -.
DR EPD; Q6P2K6; -.
DR jPOST; Q6P2K6; -.
DR MaxQB; Q6P2K6; -.
DR PaxDb; Q6P2K6; -.
DR PeptideAtlas; Q6P2K6; -.
DR PRIDE; Q6P2K6; -.
DR ProteomicsDB; 294421; -. [Q6P2K6-1]
DR ProteomicsDB; 294422; -. [Q6P2K6-2]
DR Antibodypedia; 119; 120 antibodies from 23 providers.
DR Ensembl; ENSMUST00000048305; ENSMUSP00000041667; ENSMUSG00000041846. [Q6P2K6-1]
DR GeneID; 68734; -.
DR KEGG; mmu:68734; -.
DR UCSC; uc007oti.2; mouse. [Q6P2K6-1]
DR CTD; 55671; -.
DR MGI; MGI:1915984; Ppp4r3a.
DR VEuPathDB; HostDB:ENSMUSG00000041846; -.
DR eggNOG; KOG2175; Eukaryota.
DR GeneTree; ENSGT00390000018199; -.
DR HOGENOM; CLU_004909_3_0_1; -.
DR InParanoid; Q6P2K6; -.
DR OrthoDB; 388216at2759; -.
DR PhylomeDB; Q6P2K6; -.
DR BioGRID-ORCS; 68734; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Smek1; mouse.
DR PRO; PR:Q6P2K6; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q6P2K6; protein.
DR Bgee; ENSMUSG00000041846; Expressed in embryonic post-anal tail and 242 other tissues.
DR ExpressionAtlas; Q6P2K6; baseline and differential.
DR Genevisible; Q6P2K6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IDA:MGI.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IDA:MGI.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IDA:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006887; DUF625.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF04802; SMK-1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..820
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 3A"
FT /id="PRO_0000254599"
FT DOMAIN 1..100
FT /note="WH1"
FT REGION 670..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..807
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IN85"
FT MOD_RES 642
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IN85"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..561
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021257"
SQ SEQUENCE 820 AA; 93842 MW; 20D6E184C89E6015 CRC64;
MTDTRRRVKV YTLNEDRQWD DRGTGHVSSG YVERLKGMSL LVRAESDGSL LLESKINPNT
AYQKQQDTLI VWSEAENYDL ALSFQEKAGC DEIWEKICQV QGKDPSVDIT QDLVDESEEE
RFDDMSSPGL ELPSCELSRL EEIAELVASS LPSPLRREKL ALALENEGYI KKLLELFHVC
EDLENIEGLH HLYEIIKGIF LLNRTALFEV MFSEECIMDV IGCLEYDPTL SQPRKHREFL
TKTAKFKEVI PISDPELKQK IHQTYRVQYI QDMVLPTPSV FEENMLSTLH SFIFFNKVEI
VGMLQEDEKF LTDLFAQLTD EATDEEKRQE LVNFLKEFCA FSQTLQPQNR DAFFKTLSNM
GILPALEVIL GMDDTQVRSA ATDIFSYLVE YNPSMVREFV MQEAQQNDDD ILLINLIIEH
MICDTDPELG GAVQLMGLLR TLVDPENMLA TANKTEKTEF LGFFYKHCMH VLTAPLLANT
TEDKPSKDDF QTAQLLALVL ELLTFCVEHH TYHIKNYIIN KDILRRVLVL MASKHAFLAL
CALRFKRKII GLKDEFYNRY IMKSFLFEPV VKAFLNNGSR YNLMNSAIIE MFEFIRVEDI
KSLTAHVIEN YWKALEDVDY VQTFKGLKLR FEQQRERQDN PKLDSMRSIL RNHRYRRDAR
TLEDEEEMWF NTDEDDMEDG EAVVSPSDKT KNDDDIMDPI SKFMERKKLK ESEEKEVLLK
TNLSGRQSPS FKLSLSSGTK TNLTSQSSAT SLPGSPGSPG SPGSPGSPGS VPKSTSQTAA
ITTKGGLVGL VDYPDDDEDD DEDEDKEDTL PVSKKAKFES
