RPF2_MOUSE
ID RPF2_MOUSE Reviewed; 306 AA.
AC Q9JJ80; Q8R3K6; Q9CQ34; Q9CSY9; Q9CYR9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ribosome production factor 2 homolog;
DE AltName: Full=Brix domain-containing protein 1;
DE AltName: Full=Ribosome biogenesis protein RPF2 homolog;
GN Name=Rpf2; Synonyms=Bxdc1; ORFNames=MNCb-4285;
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; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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).
CC -!- FUNCTION: Involved in ribosomal large subunit assembly. May regulate
CC the localization of the 5S RNP/5S ribonucleoprotein particle to the
CC nucleolus. {ECO:0000250|UniProtKB:Q9H7B2}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9H7B2}. Note=Associated with the nucleolus in
CC an RNA-dependent manner. {ECO:0000250|UniProtKB:Q9H7B2}.
CC -!- SIMILARITY: Belongs to the RPF2 family. {ECO:0000305}.
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DR EMBL; AB041810; BAA95117.1; -; mRNA.
DR EMBL; AK010776; BAB27175.1; -; mRNA.
DR EMBL; AK011644; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK012188; BAB28087.1; -; mRNA.
DR EMBL; AK012641; BAB28375.1; -; mRNA.
DR EMBL; AK013395; BAB28829.1; -; mRNA.
DR EMBL; AK017678; BAB30868.1; -; mRNA.
DR EMBL; AK020030; BAB31973.1; -; mRNA.
DR CCDS; CCDS59543.1; -.
DR RefSeq; NP_001036021.1; NM_001042556.1.
DR RefSeq; NP_075812.3; NM_023323.3.
DR AlphaFoldDB; Q9JJ80; -.
DR SMR; Q9JJ80; -.
DR BioGRID; 212039; 8.
DR CORUM; Q9JJ80; -.
DR IntAct; Q9JJ80; 2.
DR MINT; Q9JJ80; -.
DR STRING; 10090.ENSMUSP00000035456; -.
DR PhosphoSitePlus; Q9JJ80; -.
DR EPD; Q9JJ80; -.
DR MaxQB; Q9JJ80; -.
DR PaxDb; Q9JJ80; -.
DR PeptideAtlas; Q9JJ80; -.
DR PRIDE; Q9JJ80; -.
DR ProteomicsDB; 260926; -.
DR Antibodypedia; 19293; 165 antibodies from 25 providers.
DR DNASU; 67239; -.
DR Ensembl; ENSMUST00000183309; ENSMUSP00000138581; ENSMUSG00000038510.
DR GeneID; 67239; -.
DR KEGG; mmu:67239; -.
DR UCSC; uc007ewo.1; mouse.
DR CTD; 84154; -.
DR MGI; MGI:1914489; Rpf2.
DR VEuPathDB; HostDB:ENSMUSG00000038510; -.
DR eggNOG; KOG3031; Eukaryota.
DR GeneTree; ENSGT00390000007279; -.
DR InParanoid; Q9JJ80; -.
DR OMA; GCKIPRI; -.
DR OrthoDB; 974865at2759; -.
DR PhylomeDB; Q9JJ80; -.
DR BioGRID-ORCS; 67239; 29 hits in 71 CRISPR screens.
DR ChiTaRS; Rpf2; mouse.
DR PRO; PR:Q9JJ80; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9JJ80; protein.
DR Bgee; ENSMUSG00000038510; Expressed in primitive streak and 252 other tissues.
DR ExpressionAtlas; Q9JJ80; baseline and differential.
DR Genevisible; Q9JJ80; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0008097; F:5S rRNA binding; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:1902570; P:protein localization to nucleolus; ISS:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISS:UniProtKB.
DR InterPro; IPR007109; Brix.
DR InterPro; IPR039770; Rpf2.
DR PANTHER; PTHR12728; PTHR12728; 1.
DR Pfam; PF04427; Brix; 1.
DR SMART; SM00879; Brix; 1.
DR PROSITE; PS50833; BRIX; 1.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..306
FT /note="Ribosome production factor 2 homolog"
FT /id="PRO_0000120224"
FT DOMAIN 31..234
FT /note="Brix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00034"
FT REGION 270..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 8
FT /note="L -> R (in Ref. 1; BAA95117)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="E -> G (in Ref. 2; BAB28829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 35364 MW; CF732DBD515794AB CRC64;
MDALDKVLKP KTKRAKRFLE KREPKLTENI KNAMLIKGGN ANATVTQVLR DMYALKKPYG
VLYKKKNITR PFEDQTSLEF FSKKSDCSLF MFGSHNKKRP NNLVIGRMYD YHVLDMIELG
IEKFVSLKDI KTSKCPEGTK PMLIFAGDDF DVTEDFRRLK NLLIDFFRGP TVSNVRLAGL
EYVLHFTALN GKVYFRSYKL LLKKSGCRTP RIELEEMGPS LDLVMRRTHL ASDDLYKLSM
KVPKALKPKK RKNISQDTFG TTFGRIHMQK QDLSKLQTRK MKGLKKRPAE NGVDDQGKKS
KRIKKN
