ERAL1_HUMAN
ID ERAL1_HUMAN Reviewed; 437 AA.
AC O75616; B3KN21; C9JEC6; O75617; Q8WUY4; Q96LE2; Q96TC0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=GTPase Era, mitochondrial;
DE Short=H-ERA;
DE Short=hERA;
DE AltName: Full=Conserved ERA-like GTPase;
DE Short=CEGA;
DE AltName: Full=ERA-W;
DE AltName: Full=ERA-like protein 1;
DE Flags: Precursor;
GN Name=ERAL1; Synonyms=HERA;
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 [MRNA] (ISOFORMS HERA-A AND HERA-B).
RX PubMed=10945472; DOI=10.1006/geno.2000.6243;
RA Britton R.A., Chen S.M., Wallis D., Koeuth T., Powell B.S., Shaffer L.G.,
RA Largaespada D., Jenkins N.A., Copeland N.G., Court D.L., Lupski J.R.;
RT "Isolation and preliminary characterization of the human and mouse
RT homologues of the bacterial cell cycle gene era.";
RL Genomics 67:78-82(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HERA-A), AND RNA-BINDING.
RX PubMed=11733036; DOI=10.1046/j.1365-2443.2001.00480.x;
RA Akiyama T., Gohda J., Shibata S., Nomura Y., Azuma S., Ohmori Y.,
RA Sugano S., Arai H., Yamamoto T., Inoue J.;
RT "Mammalian homologue of E. coli Ras-like GTPase (ERA) is a possible
RT apoptosis regulator with RNA binding activity.";
RL Genes Cells 6:987-1001(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HERA-A).
RC TISSUE=Colon;
RA Chen S., Chen N., Ji Z.;
RT "cDNA cloning and characterization of human ERA.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HERA-A).
RC TISSUE=Ovary;
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HERA-A).
RC 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 [8]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=20604745; DOI=10.1042/bj20100757;
RA Dennerlein S., Rozanska A., Wydro M., Chrzanowska-Lightowlers Z.M.,
RA Lightowlers R.N.;
RT "Human ERAL1 is a mitochondrial RNA chaperone involved in the assembly of
RT the 28S small mitochondrial ribosomal subunit.";
RL Biochem. J. 430:551-558(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=20430825; DOI=10.1093/nar/gkq305;
RA Uchiumi T., Ohgaki K., Yagi M., Aoki Y., Sakai A., Matsumoto S., Kang D.;
RT "ERAL1 is associated with mitochondrial ribosome and elimination of ERAL1
RT leads to mitochondrial dysfunction and growth retardation.";
RL Nucleic Acids Res. 38:5554-5568(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
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 [15]
RP VARIANT PRLTS6 ILE-236, CHARACTERIZATION OF VARIANT PRLTS6 ILE-236, AND
RP FUNCTION.
RX PubMed=28449065; DOI=10.1093/hmg/ddx152;
RA Chatzispyrou I.A., Alders M., Guerrero-Castillo S., Zapata Perez R.,
RA Haagmans M.A., Mouchiroud L., Koster J., Ofman R., Baas F., Waterham H.R.,
RA Spelbrink J.N., Auwerx J., Mannens M.M., Houtkooper R.H., Plomp A.S.;
RT "A homozygous missense mutation in ERAL1, encoding a mitochondrial rRNA
RT chaperone, causes Perrault syndrome.";
RL Hum. Mol. Genet. 26:2541-2550(2017).
CC -!- FUNCTION: Probable GTPase that plays a role in the mitochondrial
CC ribosomal small subunit assembly. Specifically binds the 12S
CC mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating
CC the 3' terminal stem-loop region. May act as a chaperone that protects
CC the 12S mt-rRNA on the 28S mitoribosomal subunit during ribosomal small
CC subunit assembly. {ECO:0000269|PubMed:20430825,
CC ECO:0000269|PubMed:20604745, ECO:0000269|PubMed:28449065}.
CC -!- INTERACTION:
CC O75616; P01023: A2M; NbExp=3; IntAct=EBI-6393536, EBI-640741;
CC O75616; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-6393536, EBI-744115;
CC O75616; Q16637: SMN2; NbExp=3; IntAct=EBI-6393536, EBI-395421;
CC O75616; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-6393536, EBI-2212028;
CC O75616; O14656-2: TOR1A; NbExp=3; IntAct=EBI-6393536, EBI-25847109;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion inner
CC membrane; Peripheral membrane protein. Note=Localizes on the matrix
CC side on the mitochondrial inner membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=HERA-A;
CC IsoId=O75616-1; Sequence=Displayed;
CC Name=HERA-B;
CC IsoId=O75616-2; Sequence=VSP_001453;
CC -!- DISEASE: Perrault syndrome 6 (PRLTS6) [MIM:617565]: A form of Perrault
CC syndrome, a sex-influenced disorder characterized by sensorineural
CC deafness in both males and females, and ovarian dysgenesis in females.
CC Affected females have primary amenorrhea, streak gonads, and
CC infertility, whereas affected males show normal pubertal development
CC and are fertile. PRLTS6 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:28449065}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform HERA-B]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Era GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01050, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG12978.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF082657; AAC31603.1; -; mRNA.
DR EMBL; AF082658; AAC31604.1; -; mRNA.
DR EMBL; AB049388; BAB56112.1; -; mRNA.
DR EMBL; AY007435; AAG12978.1; ALT_INIT; mRNA.
DR EMBL; AK023342; BAG51183.1; -; mRNA.
DR EMBL; AC024267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471159; EAW51147.1; -; Genomic_DNA.
DR EMBL; BC019094; AAH19094.1; -; mRNA.
DR CCDS; CCDS11244.1; -. [O75616-1]
DR RefSeq; NP_001304914.1; NM_001317985.1.
DR RefSeq; NP_001304915.1; NM_001317986.1.
DR RefSeq; NP_005693.1; NM_005702.3. [O75616-1]
DR AlphaFoldDB; O75616; -.
DR SMR; O75616; -.
DR BioGRID; 117666; 234.
DR IntAct; O75616; 60.
DR MINT; O75616; -.
DR STRING; 9606.ENSP00000254928; -.
DR GlyGen; O75616; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75616; -.
DR PhosphoSitePlus; O75616; -.
DR BioMuta; ERAL1; -.
DR EPD; O75616; -.
DR jPOST; O75616; -.
DR MassIVE; O75616; -.
DR MaxQB; O75616; -.
DR PaxDb; O75616; -.
DR PeptideAtlas; O75616; -.
DR PRIDE; O75616; -.
DR ProteomicsDB; 50120; -. [O75616-1]
DR ProteomicsDB; 50121; -. [O75616-2]
DR Antibodypedia; 14896; 223 antibodies from 27 providers.
DR DNASU; 26284; -.
DR Ensembl; ENST00000254928.10; ENSP00000254928.5; ENSG00000132591.12. [O75616-1]
DR GeneID; 26284; -.
DR KEGG; hsa:26284; -.
DR MANE-Select; ENST00000254928.10; ENSP00000254928.5; NM_005702.4; NP_005693.1.
DR UCSC; uc002hcy.2; human. [O75616-1]
DR CTD; 26284; -.
DR DisGeNET; 26284; -.
DR GeneCards; ERAL1; -.
DR GeneReviews; ERAL1; -.
DR HGNC; HGNC:3424; ERAL1.
DR HPA; ENSG00000132591; Low tissue specificity.
DR MalaCards; ERAL1; -.
DR MIM; 607435; gene.
DR MIM; 617565; phenotype.
DR neXtProt; NX_O75616; -.
DR OpenTargets; ENSG00000132591; -.
DR Orphanet; 2855; Perrault syndrome.
DR PharmGKB; PA27843; -.
DR VEuPathDB; HostDB:ENSG00000132591; -.
DR eggNOG; KOG1423; Eukaryota.
DR GeneTree; ENSGT00390000013800; -.
DR HOGENOM; CLU_038009_2_1_1; -.
DR InParanoid; O75616; -.
DR OMA; WAEVDVI; -.
DR OrthoDB; 586738at2759; -.
DR PhylomeDB; O75616; -.
DR TreeFam; TF321650; -.
DR PathwayCommons; O75616; -.
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; O75616; -.
DR BioGRID-ORCS; 26284; 230 hits in 1091 CRISPR screens.
DR ChiTaRS; ERAL1; human.
DR GenomeRNAi; 26284; -.
DR Pharos; O75616; Tbio.
DR PRO; PR:O75616; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75616; protein.
DR Bgee; ENSG00000132591; Expressed in mucosa of transverse colon and 171 other tissues.
DR ExpressionAtlas; O75616; baseline and differential.
DR Genevisible; O75616; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:UniProtKB.
DR CDD; cd04163; Era; 1.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00367; GTPase_Era; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTP-bd_Era.
DR InterPro; IPR015946; KH_dom-like_a/b.
DR InterPro; IPR009019; KH_sf_prok-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR42698; PTHR42698; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54814; SSF54814; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51713; G_ERA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Deafness; Disease variant; GTP-binding; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA-binding; Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..437
FT /note="GTPase Era, mitochondrial"
FT /id="PRO_0000180081"
FT DOMAIN 112..330
FT /note="Era-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 360..437
FT /note="KH type-2"
FT REGION 120..127
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 146..150
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 167..170
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 236..239
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 271..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..310
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 120..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 167..171
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 236..239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 257..437
FT /note="GVVNGKKLKMRQAFHSHPGTHCPSPAVKDPNTQSVGNPQRIGWPHFKEIFML
FT SALSQEDVKTLKQYLLTQAQPGPWEYHSAVLTSQTPEEICANIIREKLLEHLPQEVPYN
FT VQQKTAVWEEGPGGELVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLCD
FT VDIRLSVKLLK -> AIPSDTGPARALGVPQCSPH (in isoform HERA-B)"
FT /evidence="ECO:0000303|PubMed:10945472"
FT /id="VSP_001453"
FT VARIANT 236
FT /note="N -> I (in PRLTS6; decreased protein abundance;
FT reduced assembly of the mitochondrial ribosomal small
FT subunit; dbSNP:rs1131692170)"
FT /evidence="ECO:0000269|PubMed:28449065"
FT /id="VAR_079209"
FT CONFLICT 1
FT /note="M -> V (in Ref. 1; AAC31603/AAC31604)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="V -> A (in Ref. 1; AAC31603/AAC31604)"
FT /evidence="ECO:0000305"
FT CONFLICT 17..18
FT /note="RV -> KI (in Ref. 3; AAG12978)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="P -> T (in Ref. 2; BAB56112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 48350 MW; 5C2454A1D9AFF5AA CRC64;
MAAPSWRGAR LVQSVLRVWQ VGPHVARERV IPFSSLLGFQ RRCVSCVAGS AFSGPRLASA
SRSNGQGSAL DHFLGFSQPD SSVTPCVPAV SMNRDEQDVL LVHHPDMPEN SRVLRVVLLG
APNAGKSTLS NQLLGRKVFP VSRKVHTTRC QALGVITEKE TQVILLDTPG IISPGKQKRH
HLELSLLEDP WKSMESADLV VVLVDVSDKW TRNQLSPQLL RCLTKYSQIP SVLVMNKVDC
LKQKSVLLEL TAALTEGVVN GKKLKMRQAF HSHPGTHCPS PAVKDPNTQS VGNPQRIGWP
HFKEIFMLSA LSQEDVKTLK QYLLTQAQPG PWEYHSAVLT SQTPEEICAN IIREKLLEHL
PQEVPYNVQQ KTAVWEEGPG GELVIQQKLL VPKESYVKLL IGPKGHVISQ IAQEAGHDLM
DIFLCDVDIR LSVKLLK
