DENR_MOUSE
ID DENR_MOUSE Reviewed; 198 AA.
AC Q9CQJ6; Q3UXY1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Density-regulated protein;
DE Short=DRP;
GN Name=Denr;
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=Cerebellum, and 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; 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-189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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).
CC -!- FUNCTION: May be involved in the translation of target mRNAs by
CC scanning and recognition of the initiation codon. Involved in
CC translation initiation; promotes recruitment of aminoacetyled initiator
CC tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA
CC and mRNA from recycled 40S subunits following ABCE1-mediated
CC dissociation of post-termination ribosomal complexes into subunits (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MCTS1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DENR family. {ECO:0000305}.
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DR EMBL; AK017647; BAB30854.1; -; mRNA.
DR EMBL; AK018762; BAB31392.1; -; mRNA.
DR EMBL; AK135127; BAE22432.1; -; mRNA.
DR EMBL; BC043922; AAH43922.1; -; mRNA.
DR CCDS; CCDS39275.1; -.
DR RefSeq; NP_080879.1; NM_026603.4.
DR AlphaFoldDB; Q9CQJ6; -.
DR SMR; Q9CQJ6; -.
DR BioGRID; 212709; 15.
DR IntAct; Q9CQJ6; 1.
DR MINT; Q9CQJ6; -.
DR STRING; 10090.ENSMUSP00000023869; -.
DR iPTMnet; Q9CQJ6; -.
DR PhosphoSitePlus; Q9CQJ6; -.
DR SwissPalm; Q9CQJ6; -.
DR EPD; Q9CQJ6; -.
DR jPOST; Q9CQJ6; -.
DR MaxQB; Q9CQJ6; -.
DR PaxDb; Q9CQJ6; -.
DR PeptideAtlas; Q9CQJ6; -.
DR PRIDE; Q9CQJ6; -.
DR ProteomicsDB; 279340; -.
DR Antibodypedia; 31699; 205 antibodies from 30 providers.
DR DNASU; 68184; -.
DR Ensembl; ENSMUST00000023869; ENSMUSP00000023869; ENSMUSG00000023106.
DR GeneID; 68184; -.
DR KEGG; mmu:68184; -.
DR UCSC; uc008zor.1; mouse.
DR CTD; 8562; -.
DR MGI; MGI:1915434; Denr.
DR VEuPathDB; HostDB:ENSMUSG00000023106; -.
DR eggNOG; KOG3239; Eukaryota.
DR GeneTree; ENSGT00390000014349; -.
DR HOGENOM; CLU_073511_1_0_1; -.
DR InParanoid; Q9CQJ6; -.
DR OMA; VIYCGVC; -.
DR OrthoDB; 1490022at2759; -.
DR PhylomeDB; Q9CQJ6; -.
DR TreeFam; TF105912; -.
DR BioGRID-ORCS; 68184; 20 hits in 72 CRISPR screens.
DR ChiTaRS; Denr; mouse.
DR PRO; PR:Q9CQJ6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CQJ6; protein.
DR Bgee; ENSMUSG00000023106; Expressed in primitive streak and 249 other tissues.
DR ExpressionAtlas; Q9CQJ6; baseline and differential.
DR Genevisible; Q9CQJ6; MM.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001731; P:formation of translation preinitiation complex; ISO:MGI.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR GO; GO:0032790; P:ribosome disassembly; ISO:MGI.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR InterPro; IPR005873; DENR_eukaryotes.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR Pfam; PF01253; SUI1; 1.
DR SUPFAM; SSF55159; SSF55159; 1.
DR TIGRFAMs; TIGR01159; DRP1; 1.
DR PROSITE; PS50296; SUI1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43583"
FT CHAIN 2..198
FT /note="Density-regulated protein"
FT /id="PRO_0000130601"
FT DOMAIN 115..182
FT /note="SUI1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
FT REGION 72..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43583"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43583"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43583"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 198 AA; 22166 MW; 8482AA9E13E27A10 CRC64;
MATDISESSG ADCKGDTKNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN
FPNEFAKLTV ENSPKQETGI TEGQGPVGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI
PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE
KWPEVDDDSI EDLGEVKK
