ID RS5_RABIT Reviewed; 204 AA. AC G1TFM5; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Small ribosomal subunit protein uS7 {ECO:0000305}; DE AltName: Full=40S ribosomal protein S5; GN Name=RPS5; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S., RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B., RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J., RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M., RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M., RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D., RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J., RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S., RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A., RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R., RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R., RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C., RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E., RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N., RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0007744|PDB:4KZX, ECO:0007744|PDB:4KZY} RP X-RAY CRYSTALLOGRAPHY (7.01 ANGSTROMS) OF 40S RIBOSOME, FUNCTION, SUBUNIT, RP AND SUBCELLULAR LOCATION. RX PubMed=23873042; DOI=10.1038/nature12355; RA Lomakin I.B., Steitz T.A.; RT "The initiation of mammalian protein synthesis and mRNA scanning RT mechanism."; RL Nature 500:307-311(2013). RN [3] {ECO:0007744|PDB:4D5L, ECO:0007744|PDB:4D61} RP STRUCTURE BY ELECTRON MICROSCOPY (9.00 ANGSTROMS) OF RIBOSOME, FUNCTION, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=25601755; DOI=10.1016/j.molcel.2014.12.016; RA Muhs M., Hilal T., Mielke T., Skabkin M.A., Sanbonmatsu K.Y., Pestova T.V., RA Spahn C.M.; RT "Cryo-EM of ribosomal 80S complexes with termination factors reveals the RT translocated cricket paralysis virus IRES."; RL Mol. Cell 57:422-432(2015). RN [4] {ECO:0007744|PDB:3JAG, ECO:0007744|PDB:3JAH} RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS) OF 14-204 OF RIBOSOME, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=26245381; DOI=10.1038/nature14896; RA Brown A., Shao S., Murray J., Hegde R.S., Ramakrishnan V.; RT "Structural basis for stop codon recognition in eukaryotes."; RL Nature 524:493-496(2015). RN [5] {ECO:0007744|PDB:5LZS, ECO:0007744|PDB:5LZT} RP STRUCTURE BY ELECTRON MICROSCOPY (3.31 ANGSTROMS) OF RIBOSOME, FUNCTION, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=27863242; DOI=10.1016/j.cell.2016.10.046; RA Shao S., Murray J., Brown A., Taunton J., Ramakrishnan V., Hegde R.S.; RT "Decoding mammalian ribosome-mRNA states by translational GTPase RT complexes."; RL Cell 167:1229-1240(2016). RN [6] {ECO:0007744|PDB:6GZ3} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 15-204 OF RIBOSOME, RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=30517857; DOI=10.1016/j.celrep.2018.11.040; RA Flis J., Holm M., Rundlet E.J., Loerke J., Hilal T., Dabrowski M., RA Burger J., Mielke T., Blanchard S.C., Spahn C.M.T., Budkevich T.V.; RT "tRNA translocation by the eukaryotic 80S ribosome and the impact of GTP RT hydrolysis."; RL Cell Rep. 25:2676-2688(2018). RN [7] {ECO:0007744|PDB:6D90, ECO:0007744|PDB:6D9J} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=29856316; DOI=10.7554/elife.34062; RA Pisareva V.P., Pisarev A.V., Fernandez I.S.; RT "Dual tRNA mimicry in the Cricket paralysis virus IRES uncovers an RT unexpected similarity with the Hepatitis C Virus IRES."; RL Elife 7:0-0(2018). RN [8] {ECO:0007744|PDB:6MTB, ECO:0007744|PDB:6MTC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=30355441; DOI=10.7554/elife.40486; RA Brown A., Baird M.R., Yip M.C., Murray J., Shao S.; RT "Structures of translationally inactive mammalian ribosomes."; RL Elife 7:e40486-e40486(2018). RN [9] {ECO:0007744|PDB:6HCF, ECO:0007744|PDB:6HCJ} RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=30293783; DOI=10.1016/j.molcel.2018.08.037; RA Juszkiewicz S., Chandrasekaran V., Lin Z., Kraatz S., Ramakrishnan V., RA Hegde R.S.; RT "ZNF598 is a quality control sensor of collided ribosomes."; RL Mol. Cell 72:469-481(2018). RN [10] {ECO:0007744|PDB:6R5Q, ECO:0007744|PDB:6R6G} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 14-204 OF RIBOSOME, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=31246176; DOI=10.7554/elife.46267; RA Shanmuganathan V., Schiller N., Magoulopoulou A., Cheng J., Braunger K., RA Cymer F., Berninghausen O., Beatrix B., Kohno K., von Heijne G., RA Beckmann R.; RT "Structural and mutational analysis of the ribosome-arresting human RT XBP1u."; RL Elife 8:0-0(2019). RN [11] {ECO:0007744|PDB:6P4G, ECO:0007744|PDB:6P4H} RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=31609474; DOI=10.15252/embj.2019102226; RA Acosta-Reyes F., Neupane R., Frank J., Fernandez I.S.; RT "The Israeli acute paralysis virus IRES captures host ribosomes by RT mimicking a ribosomal state with hybrid tRNAs."; RL EMBO J. 38:e102226-e102226(2019). RN [12] {ECO:0007744|PDB:6SGC} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=31768042; DOI=10.1038/s41594-019-0331-x; RA Chandrasekaran V., Juszkiewicz S., Choi J., Puglisi J.D., Brown A., RA Shao S., Ramakrishnan V., Hegde R.S.; RT "Mechanism of ribosome stalling during translation of a poly(A) tail."; RL Nat. Struct. Mol. Biol. 26:1132-1140(2019). RN [13] {ECO:0007744|PDB:6W2S, ECO:0007744|PDB:6W2T} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=32286223; DOI=10.7554/elife.54575; RA Neupane R., Pisareva V.P., Rodriguez C.F., Pisarev A.V., Fernandez I.S.; RT "A complex IRES at the 5'-UTR of a viral mRNA assembles a functional 48S RT complex via an uAUG intermediate."; RL Elife 9:0-0(2020). RN [14] {ECO:0007744|PDB:7OYD} RP STRUCTURE BY ELECTRON MICROSCOPY (2.30 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=36653451; DOI=10.1038/s41586-022-05623-y; RA Leesch F., Lorenzo-Orts L., Pribitzer C., Grishkovskaya I., Roehsner J., RA Chugunova A., Matzinger M., Roitinger E., Belacic K., Kandolf S., Lin T.Y., RA Mechtler K., Meinhart A., Haselbach D., Pauli A.; RT "A molecular network of conserved factors keeps ribosomes dormant in the RT egg."; RL Nature 613:712-720(2023). CC -!- FUNCTION: Component of the small ribosomal subunit (PubMed:23873042, CC PubMed:25601755, PubMed:27863242, PubMed:30517857). The ribosome is a CC large ribonucleoprotein complex responsible for the synthesis of CC proteins in the cell (PubMed:23873042, PubMed:25601755, CC PubMed:27863242, PubMed:30517857). Part of the small subunit (SSU) CC processome, first precursor of the small eukaryotic ribosomal subunit CC (PubMed:23873042, PubMed:25601755, PubMed:27863242, PubMed:30517857). CC During the assembly of the SSU processome in the nucleolus, many CC ribosome biogenesis factors, an RNA chaperone and ribosomal proteins CC associate with the nascent pre-rRNA and work in concert to generate RNA CC folding, modifications, rearrangements and cleavage as well as targeted CC degradation of pre-ribosomal RNA by the RNA exosome (By similarity). CC {ECO:0000250|UniProtKB:P46782, ECO:0000269|PubMed:23873042, CC ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:27863242, CC ECO:0000269|PubMed:30517857}. CC -!- SUBUNIT: Component of the small ribosomal subunit. Part of the small CC subunit (SSU) processome, composed of more than 70 proteins and the RNA CC chaperone small nucleolar RNA (snoRNA) U3. CC {ECO:0000269|PubMed:23873042, ECO:0000269|PubMed:25601755, CC ECO:0000269|PubMed:26245381, ECO:0000269|PubMed:27863242, CC ECO:0000269|PubMed:29856316, ECO:0000269|PubMed:30293783, CC ECO:0000269|PubMed:30355441, ECO:0000269|PubMed:30517857, CC ECO:0000269|PubMed:31246176, ECO:0000269|PubMed:31609474, CC ECO:0000269|PubMed:31768042, ECO:0000269|PubMed:32286223, CC ECO:0000269|PubMed:36653451}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23873042, CC ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, CC ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, CC ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, CC ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, CC ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, CC ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:36653451}. Nucleus, CC nucleolus {ECO:0000250|UniProtKB:P46782}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_002721942.1; XM_002721896.3. DR PDB; 3JAG; EM; 3.65 A; FF=14-204. DR PDB; 3JAH; EM; 3.45 A; FF=14-204. DR PDB; 3JAI; EM; 3.65 A; FF=14-204. DR PDB; 4D5L; EM; 9.00 A; F=1-204. DR PDB; 4D61; EM; 9.00 A; F=1-204. DR PDB; 4KZX; X-ray; 7.81 A; F=1-204. DR PDB; 4KZY; X-ray; 7.01 A; F=1-204. DR PDB; 4KZZ; X-ray; 7.03 A; F=1-204. DR PDB; 5LZS; EM; 3.31 A; FF=1-204. DR PDB; 5LZT; EM; 3.65 A; FF=1-204. DR PDB; 5LZU; EM; 3.75 A; FF=1-204. DR PDB; 5LZV; EM; 3.35 A; FF=1-204. DR PDB; 5LZW; EM; 3.53 A; FF=1-204. DR PDB; 5LZX; EM; 3.67 A; FF=1-204. DR PDB; 5LZY; EM; 3.99 A; FF=1-204. DR PDB; 5LZZ; EM; 3.47 A; FF=1-204. DR PDB; 6D90; EM; 3.20 A; GG=1-204. DR PDB; 6D9J; EM; 3.20 A; GG=1-204. DR PDB; 6GZ3; EM; 3.60 A; BF=15-204. DR PDB; 6HCF; EM; 3.90 A; G1=1-204. DR PDB; 6HCJ; EM; 3.80 A; G2=1-204. DR PDB; 6HCM; EM; 6.80 A; G1=1-204. DR PDB; 6HCQ; EM; 6.50 A; G2=1-204. DR PDB; 6MTB; EM; 3.60 A; FF=1-204. DR PDB; 6MTC; EM; 3.40 A; FF=1-204. DR PDB; 6MTD; EM; 3.30 A; FF=1-204. DR PDB; 6MTE; EM; 3.40 A; FF=1-204. DR PDB; 6P4G; EM; 3.10 A; G=1-204. DR PDB; 6P4H; EM; 3.20 A; G=1-204. DR PDB; 6P5I; EM; 3.10 A; G=1-204. DR PDB; 6P5J; EM; 3.10 A; G=1-204. DR PDB; 6P5K; EM; 3.10 A; G=1-204. DR PDB; 6P5N; EM; 3.20 A; G=1-204. DR PDB; 6R5Q; EM; 3.00 A; y=14-204. DR PDB; 6R6G; EM; 3.70 A; y=14-204. DR PDB; 6R6P; EM; 3.10 A; BB=14-204. DR PDB; 6R7Q; EM; 3.90 A; y=14-204. DR PDB; 6SGC; EM; 2.80 A; G1=1-204. DR PDB; 6W2S; EM; 3.00 A; G=1-204. DR PDB; 6W2T; EM; 3.36 A; G=1-204. DR PDB; 6YAN; EM; 3.48 A; H=14-204. DR PDB; 7JQB; EM; 2.70 A; G=1-204. DR PDB; 7JQC; EM; 3.30 A; G=1-204. DR PDB; 7MDZ; EM; 3.20 A; FF=1-204. DR PDB; 7NWG; EM; 3.80 A; G2=1-204. DR PDB; 7NWH; EM; 4.10 A; FF=1-204. DR PDB; 7NWI; EM; 3.13 A; FF=1-204. DR PDB; 7O7Y; EM; 2.20 A; Ae=1-204. DR PDB; 7O7Z; EM; 2.40 A; Ae=1-204. DR PDB; 7O80; EM; 2.90 A; Ae=1-204. DR PDB; 7O81; EM; 3.10 A; Ae=1-204. DR PDB; 7OYD; EM; 2.30 A; FF=1-204. DR PDB; 7SYG; EM; 4.30 A; G=1-204. DR PDB; 7SYH; EM; 4.60 A; G=1-204. DR PDB; 7SYI; EM; 4.50 A; G=1-204. DR PDB; 7SYJ; EM; 4.80 A; G=1-204. DR PDB; 7SYK; EM; 4.20 A; G=1-204. DR PDB; 7SYL; EM; 4.50 A; G=1-204. DR PDB; 7SYM; EM; 4.80 A; G=1-204. DR PDB; 7SYN; EM; 4.00 A; G=1-204. DR PDB; 7SYO; EM; 4.60 A; G=1-204. DR PDB; 7SYP; EM; 4.00 A; G=1-204. DR PDB; 7SYQ; EM; 3.80 A; G=1-204. DR PDB; 7SYR; EM; 3.60 A; G=1-204. DR PDB; 7SYS; EM; 3.50 A; G=1-204. DR PDB; 7SYT; EM; 4.40 A; G=1-204. DR PDB; 7SYU; EM; 4.60 A; G=1-204. DR PDB; 7SYV; EM; 3.90 A; G=1-204. DR PDB; 7SYW; EM; 3.70 A; G=1-204. DR PDB; 7SYX; EM; 3.70 A; G=1-204. DR PDB; 7TOQ; EM; 3.10 A; AS05=14-204. DR PDB; 7TOR; EM; 2.90 A; AS05=14-204. DR PDB; 7UCJ; EM; 3.10 A; FF=14-204. DR PDB; 7UCK; EM; 2.80 A; FF=14-204. DR PDB; 8BHF; EM; 3.10 A; G3=14-204. DR PDB; 8BTK; EM; 3.50 A; Ae=1-204. DR PDB; 8P2K; EM; 2.90 A; Ae=1-204. DR PDBsum; 3JAG; -. DR PDBsum; 3JAH; -. DR PDBsum; 3JAI; -. DR PDBsum; 4D5L; -. DR PDBsum; 4D61; -. DR PDBsum; 4KZX; -. DR PDBsum; 4KZY; -. DR PDBsum; 4KZZ; -. DR PDBsum; 5LZS; -. DR PDBsum; 5LZT; -. DR PDBsum; 5LZU; -. DR PDBsum; 5LZV; -. DR PDBsum; 5LZW; -. DR PDBsum; 5LZX; -. DR PDBsum; 5LZY; -. DR PDBsum; 5LZZ; -. DR PDBsum; 6D90; -. DR PDBsum; 6D9J; -. DR PDBsum; 6GZ3; -. DR PDBsum; 6HCF; -. DR PDBsum; 6HCJ; -. DR PDBsum; 6HCM; -. DR PDBsum; 6HCQ; -. DR PDBsum; 6MTB; -. DR PDBsum; 6MTC; -. DR PDBsum; 6MTD; -. DR PDBsum; 6MTE; -. DR PDBsum; 6P4G; -. DR PDBsum; 6P4H; -. DR PDBsum; 6P5I; -. DR PDBsum; 6P5J; -. DR PDBsum; 6P5K; -. DR PDBsum; 6P5N; -. DR PDBsum; 6R5Q; -. DR PDBsum; 6R6G; -. DR PDBsum; 6R6P; -. DR PDBsum; 6R7Q; -. DR PDBsum; 6SGC; -. DR PDBsum; 6W2S; -. DR PDBsum; 6W2T; -. DR PDBsum; 6YAN; -. DR PDBsum; 7JQB; -. DR PDBsum; 7JQC; -. DR PDBsum; 7MDZ; -. DR PDBsum; 7NWG; -. DR PDBsum; 7NWH; -. DR PDBsum; 7NWI; -. DR PDBsum; 7O7Y; -. DR PDBsum; 7O7Z; -. DR PDBsum; 7O80; -. DR PDBsum; 7O81; -. DR PDBsum; 7OYD; -. DR PDBsum; 7SYG; -. DR PDBsum; 7SYH; -. DR PDBsum; 7SYI; -. DR PDBsum; 7SYJ; -. DR PDBsum; 7SYK; -. DR PDBsum; 7SYL; -. DR PDBsum; 7SYM; -. DR PDBsum; 7SYN; -. DR PDBsum; 7SYO; -. DR PDBsum; 7SYP; -. DR PDBsum; 7SYQ; -. DR PDBsum; 7SYR; -. DR PDBsum; 7SYS; -. DR PDBsum; 7SYT; -. DR PDBsum; 7SYU; -. DR PDBsum; 7SYV; -. DR PDBsum; 7SYW; -. DR PDBsum; 7SYX; -. DR PDBsum; 7TOQ; -. DR PDBsum; 7TOR; -. DR PDBsum; 7UCJ; -. DR PDBsum; 7UCK; -. DR PDBsum; 8BHF; -. DR PDBsum; 8BTK; -. DR PDBsum; 8P2K; -. DR AlphaFoldDB; G1TFM5; -. DR IntAct; G1TFM5; 1. DR Ensembl; ENSOCUT00000023676.1; ENSOCUP00000015718.1; ENSOCUG00000024505.3. DR GeneID; 100340028; -. DR HOGENOM; CLU_063975_0_0_1; -. DR OrthoDB; 5473800at2759; -. DR TreeFam; TF300872; -. DR Proteomes; UP000001811; Unplaced. DR Bgee; ENSOCUG00000024505; Expressed in upper lobe of left lung and 14 other cell types or tissues. 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_0000460055" FT MOD_RES 1 FT /note="N-acetylmethionine; in 40S ribosomal protein S5; FT alternate" 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:0000250|UniProtKB:P46782" 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" SQ SEQUENCE 204 AA; 22876 MW; DFE2FD5AAFCFD894 CRC64; MTEWETAAPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP HSAGRYAAKR FRKAQCPIVE RLTNSMMMHG RNNGKKLMTV RIVKHAFEII HLLTGENPLQ VLVNAIINSG PREDSTRIGR AGTVRRQAVD VSPLRRVNQA IWLLCTGARE AAFRNIKTIA ECLADELINA AKGSSNSYAI KKKDELERVA KSNR //