ID   RT07_HUMAN              Reviewed;         242 AA.
AC   Q9Y2R9; B2R9N5; Q53GD6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   24-JAN-2024, entry version 174.
DE   RecName: Full=Small ribosomal subunit protein uS7m {ECO:0000303|PubMed:25838379};
DE   AltName: Full=28S ribosomal protein S7, mitochondrial;
DE            Short=MRP-S7;
DE            Short=S7mt;
DE   AltName: Full=bMRP-27a;
DE            Short=bMRP27a;
DE   Flags: Precursor;
GN   Name=MRPS7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-2.
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-2.
RC   TISSUE=Skeletal muscle;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-2.
RC   TISSUE=Small intestine;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-2.
RC   TISSUE=Eye;
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.
RX   PubMed=10581179; DOI=10.1006/bbrc.1999.1785;
RA   Koc E.C., Blackburn K., Burkhart W., Spremulli L.L.;
RT   "Identification of a mammalian mitochondrial homolog of ribosomal protein
RT   S7.";
RL   Biochem. Biophys. Res. Commun. 266:141-146(1999).
RN   [7]
RP   IDENTIFICATION.
RX   PubMed=11279123; DOI=10.1074/jbc.m100727200;
RA   Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.;
RT   "The small subunit of the mammalian mitochondrial ribosome: identification
RT   of the full complement of ribosomal proteins present.";
RL   J. Biol. Chem. 276:19363-19374(2001).
RN   [8]
RP   IDENTIFICATION.
RX   PubMed=11402041; DOI=10.1074/jbc.m103236200;
RA   Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA   Watanabe K.;
RT   "Proteomic analysis of the mammalian mitochondrial ribosome. Identification
RT   of protein components in the 28S small subunit.";
RL   J. Biol. Chem. 276:33181-33195(2001).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-208 AND LYS-228, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   FUNCTION, INVOLVEMENT IN COXPD34, VARIANT COXPD34 VAL-184, AND
RP   CHARACTERIZATION OF VARIANT COXPD34 VAL-184.
RX   PubMed=25556185; DOI=10.1093/hmg/ddu747;
RA   Menezes M.J., Guo Y., Zhang J., Riley L.G., Cooper S.T., Thorburn D.R.,
RA   Li J., Dong D., Li Z., Glessner J., Davis R.L., Sue C.M., Alexander S.I.,
RA   Arbuckle S., Kirwan P., Keating B.J., Xu X., Hakonarson H.,
RA   Christodoulou J.;
RT   "Mutation in mitochondrial ribosomal protein S7 (MRPS7) causes congenital
RT   sensorineural deafness, progressive hepatic and renal failure and lactic
RT   acidemia.";
RL   Hum. Mol. Genet. 24:2297-2307(2015).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [13] {ECO:0007744|PDB:3J9M}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP   AND SUBUNIT.
RX   PubMed=25838379; DOI=10.1126/science.aaa1193;
RA   Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT   "Ribosome. The structure of the human mitochondrial ribosome.";
RL   Science 348:95-98(2015).
CC   -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC       SSU), essential for mitochondrial protein synthesis (PubMed:25556185,
CC       PubMed:25838379). Mature mammalian 55S mitochondrial ribosomes consist
CC       of a small (28S) and a large (39S) subunit. The 28S small subunit
CC       contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins.
CC       The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of
CC       mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an
CC       integral structural role, and 52 different proteins (PubMed:25838379).
CC       {ECO:0000269|PubMed:25556185, ECO:0000269|PubMed:25838379}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}.
CC   -!- DISEASE: Combined oxidative phosphorylation deficiency 34 (COXPD34)
CC       [MIM:617872]: An autosomal recessive disorder caused by mitochondrial
CC       dysfunction and combined respiratory chain deficiencies of complexes I,
CC       III and IV. Clinical manifestations are variable and include congenital
CC       sensorineural deafness, lactic acidemia, and progressive hepatic and
CC       renal failure. {ECO:0000269|PubMed:25556185}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS7 family.
CC       {ECO:0000305}.
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DR   EMBL; AF077042; AAD27775.1; -; mRNA.
DR   EMBL; AK222995; BAD96715.1; -; mRNA.
DR   EMBL; AK313854; BAG36582.1; -; mRNA.
DR   EMBL; AC022211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000241; AAH00241.1; -; mRNA.
DR   CCDS; CCDS11718.1; -.
DR   PIR; JC7165; JC7165.
DR   RefSeq; NP_057055.2; NM_015971.3.
DR   PDB; 3J9M; EM; 3.50 A; AF=1-242.
DR   PDB; 6NU2; EM; 3.90 A; AF=35-242.
DR   PDB; 6NU3; EM; 4.40 A; AF=1-242.
DR   PDB; 6RW4; EM; 2.97 A; F=1-242.
DR   PDB; 6RW5; EM; 3.14 A; F=1-242.
DR   PDB; 6VLZ; EM; 2.97 A; AF=1-242.
DR   PDB; 6VMI; EM; 2.96 A; AF=1-242.
DR   PDB; 6ZM5; EM; 2.89 A; AF=1-242.
DR   PDB; 6ZM6; EM; 2.59 A; AF=1-242.
DR   PDB; 6ZS9; EM; 4.00 A; AF=1-242.
DR   PDB; 6ZSA; EM; 4.00 A; AF=1-242.
DR   PDB; 6ZSB; EM; 4.50 A; AF=1-242.
DR   PDB; 6ZSC; EM; 3.50 A; AF=1-242.
DR   PDB; 6ZSD; EM; 3.70 A; AF=1-242.
DR   PDB; 6ZSE; EM; 5.00 A; AF=1-242.
DR   PDB; 6ZSG; EM; 4.00 A; AF=1-242.
DR   PDB; 7A5F; EM; 4.40 A; F6=1-242.
DR   PDB; 7A5G; EM; 4.33 A; F6=1-242.
DR   PDB; 7A5I; EM; 3.70 A; F6=1-242.
DR   PDB; 7A5K; EM; 3.70 A; F6=1-242.
DR   PDB; 7L08; EM; 3.49 A; AF=1-242.
DR   PDB; 7OG4; EM; 3.80 A; AF=1-242.
DR   PDB; 7P2E; EM; 2.40 A; F=1-242.
DR   PDB; 7PNX; EM; 2.76 A; F=1-242.
DR   PDB; 7PNY; EM; 3.06 A; F=1-242.
DR   PDB; 7PNZ; EM; 3.09 A; F=1-242.
DR   PDB; 7PO0; EM; 2.90 A; F=1-242.
DR   PDB; 7PO1; EM; 2.92 A; F=1-242.
DR   PDB; 7PO2; EM; 3.09 A; F=1-242.
DR   PDB; 7PO3; EM; 2.92 A; F=1-242.
DR   PDB; 7QI4; EM; 2.21 A; AF=1-242.
DR   PDB; 7QI5; EM; 2.63 A; AF=1-242.
DR   PDB; 7QI6; EM; 2.98 A; AF=1-242.
DR   PDB; 8ANY; EM; 2.85 A; AF=1-242.
DR   PDB; 8CSP; EM; 2.66 A; F=1-242.
DR   PDB; 8CSQ; EM; 2.54 A; F=1-242.
DR   PDB; 8CSR; EM; 2.54 A; F=1-242.
DR   PDB; 8CSS; EM; 2.36 A; F=1-242.
DR   PDB; 8CST; EM; 2.85 A; F=1-242.
DR   PDB; 8CSU; EM; 3.03 A; F=1-242.
DR   PDB; 8OIR; EM; 3.10 A; AF=1-242.
DR   PDB; 8OIS; EM; 3.00 A; AF=1-242.
DR   PDBsum; 3J9M; -.
DR   PDBsum; 6NU2; -.
DR   PDBsum; 6NU3; -.
DR   PDBsum; 6RW4; -.
DR   PDBsum; 6RW5; -.
DR   PDBsum; 6VLZ; -.
DR   PDBsum; 6VMI; -.
DR   PDBsum; 6ZM5; -.
DR   PDBsum; 6ZM6; -.
DR   PDBsum; 6ZS9; -.
DR   PDBsum; 6ZSA; -.
DR   PDBsum; 6ZSB; -.
DR   PDBsum; 6ZSC; -.
DR   PDBsum; 6ZSD; -.
DR   PDBsum; 6ZSE; -.
DR   PDBsum; 6ZSG; -.
DR   PDBsum; 7A5F; -.
DR   PDBsum; 7A5G; -.
DR   PDBsum; 7A5I; -.
DR   PDBsum; 7A5K; -.
DR   PDBsum; 7L08; -.
DR   PDBsum; 7OG4; -.
DR   PDBsum; 7P2E; -.
DR   PDBsum; 7PNX; -.
DR   PDBsum; 7PNY; -.
DR   PDBsum; 7PNZ; -.
DR   PDBsum; 7PO0; -.
DR   PDBsum; 7PO1; -.
DR   PDBsum; 7PO2; -.
DR   PDBsum; 7PO3; -.
DR   PDBsum; 7QI4; -.
DR   PDBsum; 7QI5; -.
DR   PDBsum; 7QI6; -.
DR   PDBsum; 8ANY; -.
DR   PDBsum; 8CSP; -.
DR   PDBsum; 8CSQ; -.
DR   PDBsum; 8CSR; -.
DR   PDBsum; 8CSS; -.
DR   PDBsum; 8CST; -.
DR   PDBsum; 8CSU; -.
DR   PDBsum; 8OIR; -.
DR   PDBsum; 8OIS; -.
DR   AlphaFoldDB; Q9Y2R9; -.
DR   EMDB; EMD-0514; -.
DR   EMDB; EMD-0515; -.
DR   EMDB; EMD-10021; -.
DR   EMDB; EMD-10022; -.
DR   EMDB; EMD-11278; -.
DR   EMDB; EMD-11279; -.
DR   EMDB; EMD-11390; -.
DR   EMDB; EMD-11391; -.
DR   EMDB; EMD-11392; -.
DR   EMDB; EMD-11393; -.
DR   EMDB; EMD-11394; -.
DR   EMDB; EMD-11395; -.
DR   EMDB; EMD-11397; -.
DR   EMDB; EMD-11641; -.
DR   EMDB; EMD-11642; -.
DR   EMDB; EMD-11644; -.
DR   EMDB; EMD-11646; -.
DR   EMDB; EMD-12877; -.
DR   EMDB; EMD-13170; -.
DR   EMDB; EMD-13555; -.
DR   EMDB; EMD-13556; -.
DR   EMDB; EMD-13557; -.
DR   EMDB; EMD-13558; -.
DR   EMDB; EMD-13559; -.
DR   EMDB; EMD-13560; -.
DR   EMDB; EMD-13561; -.
DR   EMDB; EMD-13980; -.
DR   EMDB; EMD-13981; -.
DR   EMDB; EMD-13982; -.
DR   EMDB; EMD-15544; -.
DR   EMDB; EMD-16897; -.
DR   EMDB; EMD-16898; -.
DR   EMDB; EMD-21233; -.
DR   EMDB; EMD-21242; -.
DR   EMDB; EMD-23096; -.
DR   EMDB; EMD-26966; -.
DR   EMDB; EMD-26967; -.
DR   EMDB; EMD-26968; -.
DR   EMDB; EMD-26969; -.
DR   EMDB; EMD-26970; -.
DR   EMDB; EMD-26971; -.
DR   SMR; Q9Y2R9; -.
DR   BioGRID; 119271; 363.
DR   ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR   CORUM; Q9Y2R9; -.
DR   IntAct; Q9Y2R9; 91.
DR   MINT; Q9Y2R9; -.
DR   STRING; 9606.ENSP00000245539; -.
DR   ChEMBL; CHEMBL4295986; -.
DR   GlyGen; Q9Y2R9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y2R9; -.
DR   MetOSite; Q9Y2R9; -.
DR   PhosphoSitePlus; Q9Y2R9; -.
DR   SwissPalm; Q9Y2R9; -.
DR   BioMuta; MRPS7; -.
DR   DMDM; 296452884; -.
DR   EPD; Q9Y2R9; -.
DR   jPOST; Q9Y2R9; -.
DR   MassIVE; Q9Y2R9; -.
DR   MaxQB; Q9Y2R9; -.
DR   PaxDb; 9606-ENSP00000245539; -.
DR   PeptideAtlas; Q9Y2R9; -.
DR   ProteomicsDB; 85881; -.
DR   Pumba; Q9Y2R9; -.
DR   TopDownProteomics; Q9Y2R9; -.
DR   Antibodypedia; 19534; 160 antibodies from 20 providers.
DR   DNASU; 51081; -.
DR   Ensembl; ENST00000245539.11; ENSP00000245539.6; ENSG00000125445.11.
DR   GeneID; 51081; -.
DR   KEGG; hsa:51081; -.
DR   MANE-Select; ENST00000245539.11; ENSP00000245539.6; NM_015971.4; NP_057055.2.
DR   UCSC; uc002jnm.5; human.
DR   AGR; HGNC:14499; -.
DR   CTD; 51081; -.
DR   DisGeNET; 51081; -.
DR   GeneCards; MRPS7; -.
DR   HGNC; HGNC:14499; MRPS7.
DR   HPA; ENSG00000125445; Low tissue specificity.
DR   MalaCards; MRPS7; -.
DR   MIM; 611974; gene.
DR   MIM; 617872; phenotype.
DR   neXtProt; NX_Q9Y2R9; -.
DR   OpenTargets; ENSG00000125445; -.
DR   Orphanet; 457223; Syndromic sensorineural deafness due to combined oxidative phosphorylation defect.
DR   PharmGKB; PA31026; -.
DR   VEuPathDB; HostDB:ENSG00000125445; -.
DR   eggNOG; KOG3291; Eukaryota.
DR   GeneTree; ENSGT00390000014620; -.
DR   HOGENOM; CLU_072226_0_1_1; -.
DR   InParanoid; Q9Y2R9; -.
DR   OMA; HGETHFK; -.
DR   OrthoDB; 2911581at2759; -.
DR   PhylomeDB; Q9Y2R9; -.
DR   TreeFam; TF105978; -.
DR   PathwayCommons; Q9Y2R9; -.
DR   Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR   Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR   Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR   SignaLink; Q9Y2R9; -.
DR   SIGNOR; Q9Y2R9; -.
DR   BioGRID-ORCS; 51081; 347 hits in 1163 CRISPR screens.
DR   ChiTaRS; MRPS7; human.
DR   GeneWiki; MRPS7; -.
DR   GenomeRNAi; 51081; -.
DR   Pharos; Q9Y2R9; Tbio.
DR   PRO; PR:Q9Y2R9; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9Y2R9; Protein.
DR   Bgee; ENSG00000125445; Expressed in gastrocnemius and 202 other cell types or tissues.
DR   ExpressionAtlas; Q9Y2R9; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR   GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd14870; uS7_Mitochondria_Mammalian; 1.
DR   Gene3D; 1.10.455.10; Ribosomal protein S7 domain; 1.
DR   InterPro; IPR000235; Ribosomal_uS7.
DR   InterPro; IPR023798; Ribosomal_uS7_dom.
DR   InterPro; IPR036823; Ribosomal_uS7_dom_sf.
DR   PANTHER; PTHR11205:SF19; 28S RIBOSOMAL PROTEIN S7, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11205; RIBOSOMAL PROTEIN S7; 1.
DR   Pfam; PF00177; Ribosomal_S7; 1.
DR   SUPFAM; SSF47973; Ribosomal protein S7; 1.
DR   Genevisible; Q9Y2R9; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Disease variant; Mitochondrion;
KW   Primary mitochondrial disease; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..242
FT                   /note="Small ribosomal subunit protein uS7m"
FT                   /id="PRO_0000273056"
FT   MOD_RES         208
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         228
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VARIANT         2
FT                   /note="A -> V (in dbSNP:rs8075276)"
FT                   /evidence="ECO:0000269|PubMed:11042152,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_030076"
FT   VARIANT         184
FT                   /note="M -> V (in COXPD34; results in decreased
FT                   mitochondrial protein synthesis and reduced levels of
FT                   respiratory complexes; MRPS7 mRNA and protein levels are
FT                   reduced; dbSNP:rs115047866)"
FT                   /evidence="ECO:0000269|PubMed:25556185"
FT                   /id="VAR_080411"
FT   CONFLICT        223
FT                   /note="K -> S (in Ref. 3; BAD96715)"
FT                   /evidence="ECO:0000305"
FT   HELIX           48..51
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           60..71
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           89..98
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           104..127
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           133..136
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           141..151
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          155..173
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           176..191
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:8CSR"
FT   HELIX           201..213
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           218..231
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           234..239
FT                   /evidence="ECO:0007829|PDB:8CSS"
SQ   SEQUENCE   242 AA;  28134 MW;  945BC3E948B41CCA CRC64;
     MAAPAVKVAR GWSGLALGVR RAVLQLPGLT QVRWSRYSPE FKDPLIDKEY YRKPVEELTE
     EEKYVRELKK TQLIKAAPAG KTSSVFEDPV ISKFTNMMMI GGNKVLARSL MIQTLEAVKR
     KQFEKYHAAS AEEQATIERN PYTIFHQALK NCEPMIGLVP ILKGGRFYQV PVPLPDRRRR
     FLAMKWMITE CRDKKHQRTL MPEKLSHKLL EAFHNQGPVI KRKHDLHKMA EANRALAHYR
     WW
//