PP4R4_MOUSE
ID PP4R4_MOUSE Reviewed; 875 AA.
AC Q8C0Y0; E9QKU6; Q14CI7; Q14DT1; Q69ZE5; Q9CRR0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 4;
GN Name=Ppp4r4; Synonyms=Kiaa1622, Pp4r4;
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 3).
RC TISSUE=Pancreatic islet;
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), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-698 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Testis;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777 AND THR-799, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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: Putative regulatory subunit of serine/threonine-protein
CC phosphatase 4. {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-PPP4R4 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C0Y0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0Y0-2; Sequence=VSP_029619, VSP_029620;
CC Name=3;
CC IsoId=Q8C0Y0-3; Sequence=VSP_029618;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32499.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK173221; BAD32499.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; AK018414; BAB31199.1; -; mRNA.
DR EMBL; AK029499; BAC26478.1; -; mRNA.
DR EMBL; AC125360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC111887; AAI11888.1; -; mRNA.
DR EMBL; BC113754; AAI13755.1; -; mRNA.
DR CCDS; CCDS36532.1; -. [Q8C0Y0-1]
DR RefSeq; NP_083256.2; NM_028980.3. [Q8C0Y0-1]
DR RefSeq; XP_006516375.1; XM_006516312.2.
DR RefSeq; XP_011242496.1; XM_011244194.2. [Q8C0Y0-2]
DR AlphaFoldDB; Q8C0Y0; -.
DR BioGRID; 216818; 5.
DR ComplexPortal; CPX-165; PPP4C-PPP4R4 protein phosphatase 4 complex.
DR IntAct; Q8C0Y0; 1.
DR STRING; 10090.ENSMUSP00000021631; -.
DR iPTMnet; Q8C0Y0; -.
DR PhosphoSitePlus; Q8C0Y0; -.
DR MaxQB; Q8C0Y0; -.
DR PaxDb; Q8C0Y0; -.
DR PeptideAtlas; Q8C0Y0; -.
DR PRIDE; Q8C0Y0; -.
DR ProteomicsDB; 289795; -. [Q8C0Y0-1]
DR ProteomicsDB; 289796; -. [Q8C0Y0-2]
DR ProteomicsDB; 289797; -. [Q8C0Y0-3]
DR Antibodypedia; 49053; 48 antibodies from 18 providers.
DR Ensembl; ENSMUST00000021631; ENSMUSP00000021631; ENSMUSG00000021209. [Q8C0Y0-1]
DR Ensembl; ENSMUST00000187155; ENSMUSP00000140874; ENSMUSG00000021209. [Q8C0Y0-3]
DR Ensembl; ENSMUST00000189871; ENSMUSP00000139786; ENSMUSG00000021209. [Q8C0Y0-2]
DR GeneID; 74521; -.
DR KEGG; mmu:74521; -.
DR UCSC; uc007ovw.2; mouse. [Q8C0Y0-1]
DR CTD; 57718; -.
DR MGI; MGI:1921771; Ppp4r4.
DR VEuPathDB; HostDB:ENSMUSG00000021209; -.
DR eggNOG; KOG0211; Eukaryota.
DR GeneTree; ENSGT00510000047895; -.
DR HOGENOM; CLU_010601_0_0_1; -.
DR InParanoid; Q8C0Y0; -.
DR OMA; NEREAEC; -.
DR OrthoDB; 447572at2759; -.
DR PhylomeDB; Q8C0Y0; -.
DR TreeFam; TF313717; -.
DR BioGRID-ORCS; 74521; 2 hits in 70 CRISPR screens.
DR PRO; PR:Q8C0Y0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8C0Y0; protein.
DR Bgee; ENSMUSG00000021209; Expressed in spermatid and 108 other tissues.
DR ExpressionAtlas; Q8C0Y0; baseline and differential.
DR Genevisible; Q8C0Y0; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; ISS:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISO:MGI.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR039918; PPP4R4.
DR PANTHER; PTHR21467; PTHR21467; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..875
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 4"
FT /id="PRO_0000311851"
FT REPEAT 215..253
FT /note="HEAT 1"
FT REPEAT 254..292
FT /note="HEAT 2"
FT REGION 718..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 686..730
FT /evidence="ECO:0000255"
FT COMPBIAS 718..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 799
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..109
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029618"
FT VAR_SEQ 764..790
FT /note="SKEIKKSKLTRSQSFNNQAFHAKYGTL -> REKSPSASQNSGSLFSLHEIP
FT ESVLVP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029619"
FT VAR_SEQ 791..875
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029620"
FT CONFLICT 624..631
FT /note="RMKLCYLL -> SCLLM (in Ref. 1; BAD32499)"
FT /evidence="ECO:0000305"
FT CONFLICT 792
FT /note="K -> Q (in Ref. 2; BAC26478)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="R -> G (in Ref. 4; AAI11888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 875 AA; 99481 MW; E9F94A9064291BD1 CRC64;
MHPPPPDAGV AMDFGQNSLF GYMEDLQELT IIERPVRRSL KTPEEIERLT VDEDLSDIDR
AVYLLSAGQD VQGASVIANL PFLMRQNPTE TLRRVLPKVR EVLHVASVEM QLTAAVSFLT
ILQEESMSVH TCAHSFLQVI LLHLEHRDTG VSNAWLETLL SAVELLPKET LRHEILNPLV
SKAQLSQTVQ SRLVSCKILG KITNKFDAHS IKREILPLVK SLCQDVEYEV RSCMCRQLEN
IAQGIGAELT KNVVLPELIE LSRDESGSVR LAAFETLVNM LDMFDTDDRS QTILPLVKSF
CEKSFKADES ILISLSFHLG KLCHGLYGIF TPDQHLRFLE FYKKLCTLGL QQENGHNESQ
IPSQIVEQEK KYTSVRKNCA YNFPAMIVFV DPKNFHMELY STFFCLCHDP EVPVRHTIAI
CFYEVSKLLN SGVHLIHKEL ITLLQDESLE VLDALINHLP EILELMSTGG ENSVQENKFS
SVPDLIPALT AAEQRAAASL KWRTHEKLLQ KYTCLPHIIS SDQIYYRFLQ RMFTIMMTNN
VLPVQRAAAR TLCIFLRYNR KQEQRHEVIQ KLIEQLGQGK SYWNRLRFLD TCEFIIEIFS
RSFFCKYFFL PVIELTHDPV ANVRMKLCYL LPKVKSALKI PADMHLLQQL EMCVRKLLCQ
EKDKDVLAIV KKTVLELDRM EMSMDMFQKK NYEKDLLDQE KEREELLFLE MEQLEKEKHQ
SDGRLASDKS FEKKRRDSRT STQSLSKNLP ISVPGPSSST ASTSKEIKKS KLTRSQSFNN
QAFHAKYGTL DKCASKSSTL AHTSSVSGLV RTAMLSLTDD SFRTRNASSV PASFSPNPVM
PSTSRGPGNT ADPKSSGSKD AQPRKATLKS RKSNP
