RT27_HUMAN
ID RT27_HUMAN Reviewed; 414 AA.
AC Q92552; B4DRT2; Q6P1S1;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=28S ribosomal protein S27, mitochondrial {ECO:0000305};
DE Short=MRP-S27;
DE Short=S27mt;
DE AltName: Full=Mitochondrial ribosomal protein S27 {ECO:0000312|HGNC:HGNC:14512};
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS27 {ECO:0000303|PubMed:25838379};
DE Flags: Precursor;
GN Name=MRPS27 {ECO:0000312|HGNC:HGNC:14512}; Synonyms=KIAA0264;
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] (ISOFORM 1), AND VARIANT ASP-284.
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
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 GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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=11344316; DOI=10.1110/ps.35301;
RA Koc E.C., Burkhart W., Blackburn K., Koc H., Moseley A., Spremulli L.L.;
RT "Identification of four proteins from the small subunit of the mammalian
RT mitochondrial ribosome using a proteomics approach.";
RL Protein Sci. 10:471-481(2001).
RN [7]
RP INTERACTION WITH NOA1.
RX PubMed=19103604; DOI=10.1074/jbc.m807797200;
RA Tang T., Zheng B., Chen S.H., Murphy A.N., Kudlicka K., Zhou H.,
RA Farquhar M.G.;
RT "hNOA1 interacts with complex I and DAP3 and regulates mitochondrial
RT respiration and apoptosis.";
RL J. Biol. Chem. 284:5414-5424(2009).
RN [8]
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 [9]
RP FUNCTION IN MITOCHONDRIAL MRNA TRANSLATION, ASSOCIATION WITH SMALL SUBUNIT
RP OF MITOCHONDRIAL RIBOSOMES, BINDS TO RRNA AND TRNA, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=22841715; DOI=10.1016/j.febslet.2012.07.043;
RA Davies S.M., Lopez Sanchez M.I., Narsai R., Shearwood A.M., Razif M.F.,
RA Small I.D., Whelan J., Rackham O., Filipovska A.;
RT "MRPS27 is a pentatricopeptide repeat domain protein required for the
RT translation of mitochondrially encoded proteins.";
RL FEBS Lett. 586:3555-3561(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28714366; DOI=10.1177/1010428317709127;
RA Pu M., Wang J., Huang Q., Zhao G., Xia C., Shang R., Zhang Z., Bian Z.,
RA Yang X., Tao K.;
RT "High MRPS23 expression contributes to hepatocellular carcinoma
RT proliferation and indicates poor survival outcomes.";
RL Tumor Biol. 39:1010428317709127-1010428317709127(2017).
RN [13]
RP INTERACTION WITH MIEF1 UPSTREAM OPEN READING FRAME PROTEIN.
RX PubMed=30215512; DOI=10.1021/acs.biochem.8b00726;
RA Rathore A., Chu Q., Tan D., Martinez T.F., Donaldson C.J., Diedrich J.K.,
RA Yates J.R. III, Saghatelian A.;
RT "MIEF1 microprotein regulates mitochondrial translation.";
RL Biochemistry 57:5564-5575(2018).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), 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).
RN [15]
RP VARIANT ASP-284, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17488105; DOI=10.1021/pr0700908;
RA Bunger M.K., Cargile B.J., Sevinsky J.R., Deyanova E., Yates N.A.,
RA Hendrickson R.C., Stephenson J.L. Jr.;
RT "Detection and validation of non-synonymous coding SNPs from orthogonal
RT analysis of shotgun proteomics data.";
RL J. Proteome Res. 6:2331-2340(2007).
CC -!- FUNCTION: RNA-binding component of the mitochondrial small ribosomal
CC subunit (mt-SSU) that plays a role in mitochondrial protein synthesis
CC (PubMed:22841715). Stimulates mitochondrial mRNA translation of subunit
CC components of the mitochondrial electron transport chain
CC (PubMed:22841715). Binds to the mitochondrial 12S rRNA (12S mt-rRNA)
CC and tRNA(Glu) (PubMed:22841715). Involved also in positive regulation
CC of cell proliferation and tumor cell growth (PubMed:28714366).
CC {ECO:0000269|PubMed:22841715, ECO:0000269|PubMed:28714366}.
CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC SSU) (PubMed:22841715, PubMed:25838379). Mature mammalian 55S
CC mitochondrial ribosomes consist of a small (28S) and a large (39S)
CC subunit (PubMed:25838379). The 28S small subunit contains a 12S
CC ribosomal RNA (12S mt-rRNA) and 30 different proteins
CC (PubMed:25838379). The 39S large subunit contains a 16S rRNA (16S mt-
CC rRNA), a copy of mitochondrial valine transfer RNA (mt-tRNA(Val)),
CC which plays an integral structural role, and 52 different proteins
CC (PubMed:25838379). Interacts with NOA1 (PubMed:19103604). Interacts
CC with MIEF1 upstream open reading frame protein (PubMed:30215512).
CC Interacts with METTL17 (By similarity). {ECO:0000250|UniProtKB:Q8BK72,
CC ECO:0000269|PubMed:19103604, ECO:0000269|PubMed:22841715,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:30215512}.
CC -!- INTERACTION:
CC Q92552; Q9Y676: MRPS18B; NbExp=3; IntAct=EBI-2211879, EBI-750085;
CC Q92552-2; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-10278573, EBI-10172876;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28714366}.
CC Mitochondrion {ECO:0000269|PubMed:22841715,
CC ECO:0000269|PubMed:25838379}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92552-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92552-2; Sequence=VSP_054882;
CC -!- TISSUE SPECIFICITY: Overexpressed in hepatocellular carcinoma tissues
CC compared with adjacent non-tumoral liver tissues (at protein level)
CC (PubMed:28714366). Ubiquitous (PubMed:22841715).
CC {ECO:0000269|PubMed:22841715, ECO:0000269|PubMed:28714366}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS27 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13394.1; Type=Erroneous initiation; Evidence={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 EMBL; D87453; BAA13394.1; ALT_INIT; mRNA.
DR EMBL; AK299412; BAG61394.1; -; mRNA.
DR EMBL; AC012609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471084; EAW95701.1; -; Genomic_DNA.
DR EMBL; BC064902; AAH64902.1; -; mRNA.
DR CCDS; CCDS4013.1; -. [Q92552-1]
DR CCDS; CCDS68890.1; -. [Q92552-2]
DR RefSeq; NP_001273677.1; NM_001286748.1. [Q92552-2]
DR RefSeq; NP_055899.2; NM_015084.2. [Q92552-1]
DR PDB; 3J9M; EM; 3.50 A; AV=1-414.
DR PDB; 6NU2; EM; 3.90 A; AV=36-400.
DR PDB; 6NU3; EM; 4.40 A; AV=1-414.
DR PDB; 6RW4; EM; 2.97 A; V=1-414.
DR PDB; 6RW5; EM; 3.14 A; V=1-414.
DR PDB; 6VLZ; EM; 2.97 A; AV=1-414.
DR PDB; 6VMI; EM; 2.96 A; AV=1-414.
DR PDB; 6ZM5; EM; 2.89 A; AV=1-414.
DR PDB; 6ZM6; EM; 2.59 A; AV=1-414.
DR PDB; 6ZS9; EM; 4.00 A; AV=1-414.
DR PDB; 6ZSA; EM; 4.00 A; AV=1-414.
DR PDB; 6ZSB; EM; 4.50 A; AV=1-414.
DR PDB; 6ZSC; EM; 3.50 A; AV=1-414.
DR PDB; 6ZSD; EM; 3.70 A; AV=1-414.
DR PDB; 6ZSE; EM; 5.00 A; AV=1-414.
DR PDB; 6ZSG; EM; 4.00 A; AV=1-414.
DR PDB; 7A5F; EM; 4.40 A; V6=1-414.
DR PDB; 7A5G; EM; 4.33 A; V6=1-414.
DR PDB; 7A5I; EM; 3.70 A; V6=1-414.
DR PDB; 7A5K; EM; 3.70 A; V6=1-414.
DR PDB; 7L08; EM; 3.49 A; AV=1-414.
DR PDB; 7OG4; EM; 3.80 A; AV=1-414.
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 AlphaFoldDB; Q92552; -.
DR SMR; Q92552; -.
DR BioGRID; 116731; 296.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; Q92552; -.
DR DIP; DIP-44136N; -.
DR IntAct; Q92552; 111.
DR MINT; Q92552; -.
DR STRING; 9606.ENSP00000426941; -.
DR GlyGen; Q92552; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92552; -.
DR PhosphoSitePlus; Q92552; -.
DR SwissPalm; Q92552; -.
DR BioMuta; MRPS27; -.
DR DMDM; 209572725; -.
DR EPD; Q92552; -.
DR jPOST; Q92552; -.
DR MassIVE; Q92552; -.
DR MaxQB; Q92552; -.
DR PaxDb; Q92552; -.
DR PeptideAtlas; Q92552; -.
DR PRIDE; Q92552; -.
DR ProteomicsDB; 4971; -.
DR ProteomicsDB; 75311; -. [Q92552-1]
DR Antibodypedia; 24192; 406 antibodies from 28 providers.
DR DNASU; 23107; -.
DR Ensembl; ENST00000261413.10; ENSP00000261413.5; ENSG00000113048.17. [Q92552-1]
DR Ensembl; ENST00000513900.5; ENSP00000426941.1; ENSG00000113048.17. [Q92552-2]
DR GeneID; 23107; -.
DR KEGG; hsa:23107; -.
DR MANE-Select; ENST00000261413.10; ENSP00000261413.5; NM_015084.3; NP_055899.2.
DR UCSC; uc003kbz.5; human. [Q92552-1]
DR CTD; 23107; -.
DR DisGeNET; 23107; -.
DR GeneCards; MRPS27; -.
DR HGNC; HGNC:14512; MRPS27.
DR HPA; ENSG00000113048; Low tissue specificity.
DR MIM; 611989; gene.
DR neXtProt; NX_Q92552; -.
DR OpenTargets; ENSG00000113048; -.
DR PharmGKB; PA31015; -.
DR VEuPathDB; HostDB:ENSG00000113048; -.
DR eggNOG; KOG4570; Eukaryota.
DR GeneTree; ENSGT00390000007246; -.
DR InParanoid; Q92552; -.
DR OMA; ANLMDRT; -.
DR PhylomeDB; Q92552; -.
DR TreeFam; TF316446; -.
DR PathwayCommons; Q92552; -.
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; Q92552; -.
DR SIGNOR; Q92552; -.
DR BioGRID-ORCS; 23107; 378 hits in 1097 CRISPR screens.
DR ChiTaRS; MRPS27; human.
DR GenomeRNAi; 23107; -.
DR Pharos; Q92552; Tbio.
DR PRO; PR:Q92552; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q92552; protein.
DR Bgee; ENSG00000113048; Expressed in heart left ventricle and 208 other tissues.
DR ExpressionAtlas; Q92552; baseline and differential.
DR Genevisible; Q92552; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR019266; MRPS27.
DR InterPro; IPR034913; MRPS27/PTCD2.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR21393; PTHR21393; 1.
DR Pfam; PF10037; MRP-S27; 1.
DR PROSITE; PS51375; PPR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Mitochondrion;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Transit peptide; Translation regulation;
KW tRNA-binding.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..414
FT /note="28S ribosomal protein S27, mitochondrial"
FT /id="PRO_0000087712"
FT REPEAT 105..139
FT /note="PPR 1"
FT REPEAT 140..175
FT /note="PPR 2"
FT COILED 368..414
FT /evidence="ECO:0000255"
FT VAR_SEQ 94
FT /note="K -> KKGECSSSNPQNYSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054882"
FT VARIANT 284
FT /note="G -> D (confirmed at protein level;
FT dbSNP:rs3209157)"
FT /evidence="ECO:0000269|PubMed:17488105,
FT ECO:0000269|PubMed:9039502"
FT /id="VAR_047026"
SQ SEQUENCE 414 AA; 47611 MW; AF8E8D6FC738AA77 CRC64;
MAASIVRRGM LLARQVVLPQ LSPAGKRYLL SSAYVDSHKW EAREKEHYCL ADLASLMDKT
FERKLPVSSL TISRLIDNIS SREEIDHAEY YLYKFRHSPN CWYLRNWTIH TWIRQCLKYD
AQDKALYTLV NKVQYGIFPD NFTFNLLMDS FIKKENYKDA LSVVFEVMMQ EAFEVPSTQL
LSLYVLFHCL AKKTDFSWEE ERNFGASLLL PGLKQKNSVG FSSQLYGYAL LGKVELQQGL
RAVYHNMPLI WKPGYLDRAL QVMEKVAASP EDIKLCREAL DVLGAVLKAL TSADGASEEQ
SQNDEDNQGS EKLVEQLDIE ETEQSKLPQY LERFKALHSK LQALGKIESE GLLSLTTQLV
KEKLSTCEAE DIATYEQNLQ QWHLDLVQLI QREQQQREQA KQEYQAQKAA KASA
