ID   RS5_MOUSE               Reviewed;         204 AA.
AC   P97461; O08607; Q91V55;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2023, sequence version 4.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Small ribosomal subunit protein uS7 {ECO:0000305};
DE   AltName: Full=40S ribosomal protein S5;
DE   Contains:
DE     RecName: Full=Small ribosomal subunit protein uS7, N-terminally processed;
GN   Name=Rps5;
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 [MRNA].
RX   PubMed=9202169; DOI=10.1016/s0167-4889(97)00054-2;
RA   Vanegas N., Castaneda V., Santamaria D., Hernandez P., Schvartzman J.B.,
RA   Krimer D.B.;
RT   "Cloning, sequencing and expression in MEL cells of a cDNA encoding the
RT   mouse ribosomal protein S5.";
RL   Biochim. Biophys. Acta 1357:1-4(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DAB/2J;
RA   Vizirianakis I.S., Pappas I.S., Tsiftsoglou A.S.;
RT   "Cloning, sequencing and expression of a cDNA coding for the mouse S5
RT   ribosomal protein in differentiating murine erythroleukemia (MEL) cells.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD;
RC   TISSUE=Bone marrow, Kidney, Liver, Spinal cord, Spleen, Thymus, and
RC   Tongue;
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   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).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47, 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).
RN   [8] {ECO:0007744|PDB:7CPU, ECO:0007744|PDB:7CPV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=36517592; DOI=10.1038/s41586-022-05508-0;
RA   Li H., Huo Y., He X., Yao L., Zhang H., Cui Y., Xiao H., Xie W., Zhang D.,
RA   Wang Y., Zhang S., Tu H., Cheng Y., Guo Y., Cao X., Zhu Y., Jiang T.,
RA   Guo X., Qin Y., Sha J.;
RT   "A male germ-cell-specific ribosome controls male fertility.";
RL   Nature 0:0-0(2022).
CC   -!- FUNCTION: Component of the small ribosomal subunit (PubMed:36517592).
CC       The ribosome is a large ribonucleoprotein complex responsible for the
CC       synthesis of proteins in the cell (PubMed:36517592). Part of the small
CC       subunit (SSU) processome, first precursor of the small eukaryotic
CC       ribosomal subunit. During the assembly of the SSU processome in the
CC       nucleolus, many ribosome biogenesis factors, an RNA chaperone and
CC       ribosomal proteins associate with the nascent pre-rRNA and work in
CC       concert to generate RNA folding, modifications, rearrangements and
CC       cleavage as well as targeted degradation of pre-ribosomal RNA by the
CC       RNA exosome (By similarity). {ECO:0000250|UniProtKB:P46782,
CC       ECO:0000269|PubMed:36517592}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:36517592).
CC       Part of the small subunit (SSU) processome, composed of more than 70
CC       proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3 (By
CC       similarity). {ECO:0000250|UniProtKB:P46782,
CC       ECO:0000269|PubMed:36517592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:P46782}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC       {ECO:0000305}.
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DR   EMBL; U78085; AAB63526.1; -; mRNA.
DR   EMBL; Y12431; CAA73041.1; -; mRNA.
DR   EMBL; AK009663; BAB26424.1; -; mRNA.
DR   EMBL; AK002235; BAB21953.1; -; mRNA.
DR   EMBL; AK010681; BAB27113.1; -; mRNA.
DR   EMBL; AK012424; BAB28229.1; -; mRNA.
DR   EMBL; AK012481; BAB28270.1; -; mRNA.
DR   EMBL; AK020477; BAB32115.1; -; mRNA.
DR   EMBL; AK020754; BAB32203.1; -; mRNA.
DR   EMBL; AK050611; BAC34342.1; -; mRNA.
DR   EMBL; AK050622; BAC34347.1; -; mRNA.
DR   EMBL; AK152449; BAE31228.1; -; mRNA.
DR   EMBL; AK160552; BAE35868.1; -; mRNA.
DR   EMBL; AK164079; BAE37616.1; -; mRNA.
DR   EMBL; AK167533; BAE39602.1; -; mRNA.
DR   EMBL; AK168106; BAE40077.1; -; mRNA.
DR   EMBL; AK168044; BAE40026.1; -; mRNA.
DR   EMBL; AK169016; BAE40813.1; -; mRNA.
DR   EMBL; AK172446; BAE43008.1; -; mRNA.
DR   EMBL; BC058690; AAH58690.1; -; mRNA.
DR   CCDS; CCDS20817.1; -.
DR   RefSeq; NP_033121.2; NM_009095.2.
DR   PDB; 7CPU; EM; 2.82 A; SF=1-204.
DR   PDB; 7CPV; EM; 3.03 A; SF=1-204.
DR   PDB; 7LS1; EM; 3.30 A; s2=1-204.
DR   PDB; 7LS2; EM; 3.10 A; s2=1-204.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; P97461; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; P97461; -.
DR   BioGRID; 203012; 98.
DR   ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR   IntAct; P97461; 2.
DR   STRING; 10090.ENSMUSP00000104179; -.
DR   GlyGen; P97461; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P97461; -.
DR   PhosphoSitePlus; P97461; -.
DR   SwissPalm; P97461; -.
DR   EPD; P97461; -.
DR   jPOST; P97461; -.
DR   MaxQB; P97461; -.
DR   PaxDb; 10090-ENSMUSP00000004554; -.
DR   PeptideAtlas; P97461; -.
DR   ProteomicsDB; 256936; -.
DR   ProteomicsDB; 329197; -.
DR   Pumba; P97461; -.
DR   TopDownProteomics; P97461; -.
DR   TopDownProteomics; Q91V55; -.
DR   Antibodypedia; 33338; 279 antibodies from 28 providers.
DR   DNASU; 20103; -.
DR   Ensembl; ENSMUST00000004554.14; ENSMUSP00000004554.8; ENSMUSG00000012848.16.
DR   Ensembl; ENSMUST00000108539.8; ENSMUSP00000104179.2; ENSMUSG00000012848.16.
DR   GeneID; 20103; -.
DR   KEGG; mmu:20103; -.
DR   AGR; MGI:1097682; -.
DR   CTD; 6193; -.
DR   MGI; MGI:1097682; Rps5.
DR   VEuPathDB; HostDB:ENSMUSG00000012848; -.
DR   eggNOG; KOG3291; Eukaryota.
DR   GeneTree; ENSGT00390000010806; -.
DR   HOGENOM; CLU_063975_0_0_1; -.
DR   InParanoid; P97461; -.
DR   OMA; ASTMMMH; -.
DR   OrthoDB; 5473800at2759; -.
DR   PhylomeDB; P97461; -.
DR   TreeFam; TF300872; -.
DR   Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-MMU-72649; Translation initiation complex formation.
DR   Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 20103; 25 hits in 75 CRISPR screens.
DR   ChiTaRS; Rps5; mouse.
DR   PRO; PR:P97461; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P97461; Protein.
DR   Bgee; ENSMUSG00000012848; Expressed in gonadal ridge and 264 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0098794; C:postsynapse; NAS:SynGO.
DR   GO; GO:0098793; C:presynapse; NAS:SynGO.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR   GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR   GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR   GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal.
DR   GO; GO:0006450; P:regulation of translational fidelity; ISO:MGI.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:UniProtKB.
DR   GO; GO:0006412; P:translation; ISO:MGI.
DR   GO; GO:0140242; P:translation at postsynapse; NAS:SynGO.
DR   GO; GO:0140236; P:translation at presynapse; NAS:SynGO.
DR   CDD; cd14867; uS7_Eukaryote; 1.
DR   Gene3D; 1.10.455.10; Ribosomal protein S7 domain; 1.
DR   InterPro; IPR000235; Ribosomal_uS7.
DR   InterPro; IPR020606; Ribosomal_uS7_CS.
DR   InterPro; IPR023798; Ribosomal_uS7_dom.
DR   InterPro; IPR036823; Ribosomal_uS7_dom_sf.
DR   InterPro; IPR005716; Ribosomal_uS7_euk/arc.
DR   NCBIfam; TIGR01028; uS7_euk_arch; 1.
DR   PANTHER; PTHR11205:SF18; 40S RIBOSOMAL PROTEIN S5; 1.
DR   PANTHER; PTHR11205; RIBOSOMAL PROTEIN S7; 1.
DR   Pfam; PF00177; Ribosomal_S7; 1.
DR   PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1.
DR   SUPFAM; SSF47973; Ribosomal protein S7; 1.
DR   PROSITE; PS00052; RIBOSOMAL_S7; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   Ubl conjugation.
FT   CHAIN           1..204
FT                   /note="Small ribosomal subunit protein uS7"
FT                   /id="PRO_0000124527"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P46782"
FT   CHAIN           2..204
FT                   /note="Small ribosomal subunit protein uS7, N-terminally
FT                   processed"
FT                   /id="PRO_0000370370"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P46782"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine; in 40S ribosomal protein S5, N-
FT                   terminally processed"
FT                   /evidence="ECO:0000250|UniProtKB:P46782"
FT   MOD_RES         14
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P46782"
FT   MOD_RES         47
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46782"
FT   CROSSLNK        47
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P46782"
FT   CONFLICT        168
FT                   /note="T -> N (in Ref. 1; AAB63526 and 2; CAA73041)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   204 AA;  22876 MW;  9F59F6EA13B2A998 CRC64;
     MTEWEAATPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP HSAGRYAAKR
     FRKAQCPIVE RLTNSMMMHG RNNGKKLMTV RIVKHAFEII HLLTGENPLQ VLVNAIINSG
     PREDSTRIGR AGTVRRQAVD VSPLRRVNQA IWLLCTGARE AAFRNIKTIA ECLADELINA
     AKGSSNSYAI KKKDELERVA KSNR
//