ID   ERAL1_MOUSE             Reviewed;         437 AA.
AC   Q9CZU4; Q6NV78; Q8VE60; Q925U1;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=GTPase Era, mitochondrial;
DE            Short=M-ERA;
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=Mera;
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=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129/Sv X 129SvCp, and Czech II; TISSUE=Mammary tumor;
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).
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 (By similarity). {ECO:0000250|UniProtKB:O75616}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Mitochondrion
CC       inner membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Note=Localizes on the matrix side on the mitochondrial
CC       inner membrane. {ECO:0000250}.
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}.
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DR   EMBL; AB049389; BAB56113.1; -; mRNA.
DR   EMBL; AK012155; BAB28065.1; -; mRNA.
DR   EMBL; AL669840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC019728; AAH19728.1; -; mRNA.
DR   EMBL; BC068271; AAH68271.1; -; mRNA.
DR   CCDS; CCDS48856.1; -.
DR   RefSeq; NP_071708.2; NM_022313.2.
DR   AlphaFoldDB; Q9CZU4; -.
DR   SMR; Q9CZU4; -.
DR   STRING; 10090.ENSMUSP00000021183; -.
DR   PhosphoSitePlus; Q9CZU4; -.
DR   EPD; Q9CZU4; -.
DR   MaxQB; Q9CZU4; -.
DR   PaxDb; 10090-ENSMUSP00000021183; -.
DR   PeptideAtlas; Q9CZU4; -.
DR   ProteomicsDB; 275644; -.
DR   Pumba; Q9CZU4; -.
DR   Antibodypedia; 14896; 263 antibodies from 27 providers.
DR   DNASU; 57837; -.
DR   Ensembl; ENSMUST00000021183.4; ENSMUSP00000021183.4; ENSMUSG00000020832.15.
DR   GeneID; 57837; -.
DR   KEGG; mmu:57837; -.
DR   UCSC; uc007kia.2; mouse.
DR   AGR; MGI:1889295; -.
DR   CTD; 26284; -.
DR   MGI; MGI:1889295; Eral1.
DR   VEuPathDB; HostDB:ENSMUSG00000020832; -.
DR   eggNOG; KOG1423; Eukaryota.
DR   GeneTree; ENSGT00390000013800; -.
DR   HOGENOM; CLU_038009_2_1_1; -.
DR   InParanoid; Q9CZU4; -.
DR   OMA; WAEVDVI; -.
DR   OrthoDB; 5490026at2759; -.
DR   PhylomeDB; Q9CZU4; -.
DR   TreeFam; TF321650; -.
DR   Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR   Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR   BioGRID-ORCS; 57837; 25 hits in 77 CRISPR screens.
DR   ChiTaRS; Eral1; mouse.
DR   PRO; PR:Q9CZU4; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9CZU4; Protein.
DR   Bgee; ENSMUSG00000020832; Expressed in hindlimb stylopod muscle and 221 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB.
DR   GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; ISS:UniProtKB.
DR   CDD; cd04163; Era; 1.
DR   CDD; cd22534; KH-II_Era; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00367; GTPase_Era; 1.
DR   InterPro; IPR030388; G_ERA_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR005662; GTPase_Era.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004044; KH_dom_type_2.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42698; GTPASE ERA; 1.
DR   PANTHER; PTHR42698:SF4; GTPASE ERA, MITOCHONDRIAL; 1.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 1.
DR   PROSITE; PS51713; G_ERA; 1.
DR   Genevisible; Q9CZU4; MM.
PE   2: Evidence at transcript level;
KW   GTP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; RNA-binding; rRNA-binding; Transit peptide.
FT   TRANSIT         1..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..437
FT                   /note="GTPase Era, mitochondrial"
FT                   /id="PRO_0000180082"
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          270..292
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:0000250|UniProtKB:P06616"
FT   BINDING         167..171
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P06616"
FT   BINDING         236..239
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P06616"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75616"
FT   CONFLICT        154
FT                   /note="G -> W (in Ref. 1; BAB56113)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        407
FT                   /note="L -> S (in Ref. 4; AAH68271)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   437 AA;  48187 MW;  D6118FD53DC9A7E1 CRC64;
     MAAPRRYCAG LVRALLGARQ VGSHAGREWL APPGCLLGNQ ARCVSCVVGS TFSGPLLASA
     SSRYGQDSAL DRILGFSQPD SSLVPSVPAV SVHRDEQNLL LVHTPDMPEN PRVLRVVLLG
     APNAGKSTLS NQLLGRKVFP VSKKVHTTRC QALGVITEKE TQVILLDTPG IISPVKQKRH
     HLERSLLEDP WTSMESADLV VVLVDVSDKW TRSRLNPQVL QCLTKFSQVP SILVLNKVDC
     LKQKSVLLEL TAALTEGVVN GKKLNIKQAL RSRSSTHCPG PETEGPNAHS VRNPQRIGWP
     YFQEIFMLSA LNNKDVNTLK QYLLTQAQPG PWEFHSGVLT SQTPEEICAN KIREKLLEYL
     PEEVPYGVQQ KTVIWEEGPS GELVIQQNLL VPKESHVRIL IGQKGLLISQ IAQEVGRDLM
     DIFHCDVLIR LSVKLLK
//