ERAL1_MOUSE
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 03-AUG-2022, entry version 144.
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; Q9CZU4; -.
DR PeptideAtlas; Q9CZU4; -.
DR PRIDE; Q9CZU4; -.
DR ProteomicsDB; 275644; -.
DR Antibodypedia; 14896; 223 antibodies from 27 providers.
DR DNASU; 57837; -.
DR Ensembl; ENSMUST00000021183; ENSMUSP00000021183; ENSMUSG00000020832.
DR GeneID; 57837; -.
DR KEGG; mmu:57837; -.
DR UCSC; uc007kia.2; mouse.
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; 586738at2759; -.
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; 24 hits in 72 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 218 other tissues.
DR Genevisible; Q9CZU4; MM.
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 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; 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 PANTHER; PTHR42698; PTHR42698; 1.
DR Pfam; PF07650; KH_2; 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 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: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: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
