MRT4_MOUSE
ID MRT4_MOUSE Reviewed; 239 AA.
AC Q9D0I8; Q99JR7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=mRNA turnover protein 4 homolog {ECO:0000250|UniProtKB:P33201};
DE AltName: Full=Ribosome assembly factor Mrto4 {ECO:0000250|UniProtKB:P33201, ECO:0000305};
GN Name=Mrto4; Synonyms=Mrt4;
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].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-229 AND SER-233, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, 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: Component of the ribosome assembly machinery. Nuclear paralog
CC of the ribosomal protein P0, it binds pre-60S subunits at an early
CC stage of assembly in the nucleolus, and is replaced by P0 in
CC cytoplasmic pre-60S subunits and mature 80S ribosomes.
CC {ECO:0000250|UniProtKB:P33201}.
CC -!- SUBUNIT: Associates with the pre-60S ribosomal particle. Interacts with
CC MINAS-60 (product of an alternative open reading frame of RBM10).
CC {ECO:0000250|UniProtKB:Q9UKD2}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P33201}. Cytoplasm
CC {ECO:0000250|UniProtKB:P33201}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:P33201}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
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DR EMBL; AK011387; BAB27585.1; -; mRNA.
DR EMBL; BC005734; AAH05734.1; -; mRNA.
DR CCDS; CCDS71505.1; -.
DR RefSeq; NP_001277739.1; NM_001290810.1.
DR RefSeq; NP_076025.1; NM_023536.3.
DR AlphaFoldDB; Q9D0I8; -.
DR SMR; Q9D0I8; -.
DR BioGRID; 213745; 29.
DR CORUM; Q9D0I8; -.
DR IntAct; Q9D0I8; 1.
DR STRING; 10090.ENSMUSP00000099561; -.
DR iPTMnet; Q9D0I8; -.
DR PhosphoSitePlus; Q9D0I8; -.
DR EPD; Q9D0I8; -.
DR MaxQB; Q9D0I8; -.
DR PaxDb; Q9D0I8; -.
DR PRIDE; Q9D0I8; -.
DR ProteomicsDB; 290060; -.
DR Antibodypedia; 29590; 213 antibodies from 25 providers.
DR DNASU; 69902; -.
DR Ensembl; ENSMUST00000102503; ENSMUSP00000099561; ENSMUSG00000028741.
DR GeneID; 69902; -.
DR KEGG; mmu:69902; -.
DR UCSC; uc008vme.2; mouse.
DR CTD; 51154; -.
DR MGI; MGI:1917152; Mrto4.
DR VEuPathDB; HostDB:ENSMUSG00000028741; -.
DR eggNOG; KOG0816; Eukaryota.
DR GeneTree; ENSGT00390000006238; -.
DR HOGENOM; CLU_071690_3_0_1; -.
DR InParanoid; Q9D0I8; -.
DR OMA; LEWAENY; -.
DR OrthoDB; 1181992at2759; -.
DR PhylomeDB; Q9D0I8; -.
DR TreeFam; TF300111; -.
DR BioGRID-ORCS; 69902; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Mrto4; mouse.
DR PRO; PR:Q9D0I8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D0I8; protein.
DR Bgee; ENSMUSG00000028741; Expressed in epiblast (generic) and 67 other tissues.
DR ExpressionAtlas; Q9D0I8; baseline and differential.
DR Genevisible; Q9D0I8; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:InterPro.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR CDD; cd05796; Ribosomal_P0_like; 1.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR InterPro; IPR033867; Mrt4.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR InterPro; IPR043164; RL10_insert_sf.
DR InterPro; IPR040637; RL10P_insert.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..239
FT /note="mRNA turnover protein 4 homolog"
FT /id="PRO_0000154817"
FT REGION 216..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..239
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 191
FT /note="Missing (in Ref. 2; AAH05734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 27546 MW; 9692756DDBFB95BF CRC64;
MPKSKRDKKV SLTKTAKKGL ELKQNLIEEL RKCVDTYKYL FIFSVANMRN SKLKDIRNAW
KHSRMFFGKN KVMMVALGRS PSDEYKDNLH QVSKKLRGEV GLLFTNRTKE EVNEWFTKYT
EMDFARAGNK ATLTVSLDPG PLKQFPHSME PQLRQLGLPT ALKKGVVTLL SDYEVCKEGD
VLTPEQARIL KLFGYEMAEF KVIIKYMWDA QSGRFQQMDD DLPESAPESE GESEEEDDS
