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GTPase Era, mitochondrial (M-ERA) (Conserved ERA-like GTPase) (CEGA) (ERA-W) (ERA-like protein 1)

 ERAL1_MOUSE             Reviewed;         437 AA.
Q9CZU4; Q6NV78; Q8VE60; Q925U1;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
07-NOV-2018, entry version 126.
RecName: Full=GTPase Era, mitochondrial;
Short=M-ERA;
AltName: Full=Conserved ERA-like GTPase;
Short=CEGA;
AltName: Full=ERA-W;
AltName: Full=ERA-like protein 1;
Flags: Precursor;
Name=Eral1; Synonyms=Mera;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11733036; DOI=10.1046/j.1365-2443.2001.00480.x;
Akiyama T., Gohda J., Shibata S., Nomura Y., Azuma S., Ohmori Y.,
Sugano S., Arai H., Yamamoto T., Inoue J.;
"Mammalian homologue of E. coli Ras-like GTPase (ERA) is a possible
apoptosis regulator with RNA binding activity.";
Genes Cells 6:987-1001(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=129/Sv X 129SvCp, and Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Probable GTPase that plays a role in the mitochondrial
ribosomal small subunit assembly. Specifically binds the 12S
mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section
delineating the 3' terminal stem-loop region. May act as a
chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal
subunit during ribosomal small subunit assembly (By similarity).
{ECO:0000250|UniProtKB:O75616}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane
protein {ECO:0000250}. Note=Localizes on the matrix side on the
mitochondrial inner membrane. {ECO:0000250}.
-!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
like GTPase superfamily. Era GTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB049389; BAB56113.1; -; mRNA.
EMBL; AK012155; BAB28065.1; -; mRNA.
EMBL; AL669840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC019728; AAH19728.1; -; mRNA.
EMBL; BC068271; AAH68271.1; -; mRNA.
CCDS; CCDS48856.1; -.
RefSeq; NP_071708.2; NM_022313.2.
UniGene; Mm.21096; -.
ProteinModelPortal; Q9CZU4; -.
SMR; Q9CZU4; -.
STRING; 10090.ENSMUSP00000021183; -.
PhosphoSitePlus; Q9CZU4; -.
EPD; Q9CZU4; -.
MaxQB; Q9CZU4; -.
PaxDb; Q9CZU4; -.
PeptideAtlas; Q9CZU4; -.
PRIDE; Q9CZU4; -.
Ensembl; ENSMUST00000021183; ENSMUSP00000021183; ENSMUSG00000020832.
GeneID; 57837; -.
KEGG; mmu:57837; -.
UCSC; uc007kia.2; mouse.
CTD; 26284; -.
MGI; MGI:1889295; Eral1.
eggNOG; KOG1423; Eukaryota.
eggNOG; COG1159; LUCA.
GeneTree; ENSGT00390000013800; -.
HOGENOM; HOG000245598; -.
HOVERGEN; HBG051495; -.
InParanoid; Q9CZU4; -.
KO; K03595; -.
OMA; KVAKDWQ; -.
OrthoDB; EOG091G0BPI; -.
PhylomeDB; Q9CZU4; -.
TreeFam; TF321650; -.
Reactome; R-MMU-5389840; Mitochondrial translation elongation.
Reactome; R-MMU-5419276; Mitochondrial translation termination.
PRO; PR:Q9CZU4; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020832; Expressed in 295 organ(s), highest expression level in brown adipose tissue.
CleanEx; MM_ERAL1; -.
Genevisible; Q9CZU4; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB.
GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
GO; GO:0000028; P:ribosomal small subunit assembly; ISS:UniProtKB.
CDD; cd04163; Era; 1.
Gene3D; 3.30.300.20; -; 1.
HAMAP; MF_00367; GTPase_Era; 1.
InterPro; IPR030388; G_ERA_dom.
InterPro; IPR005662; GTP-bd_Era.
InterPro; IPR006073; GTP_binding_domain.
InterPro; IPR015946; KH_dom-like_a/b.
InterPro; IPR004044; KH_dom_type_2.
InterPro; IPR009019; KH_sf_prok-type.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
Pfam; PF07650; KH_2; 1.
Pfam; PF01926; MMR_HSR1; 1.
PRINTS; PR00326; GTP1OBG.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF54814; SSF54814; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51713; G_ERA; 1.
2: Evidence at transcript level;
Complete proteome; GTP-binding; Membrane; Mitochondrion;
Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding;
Transit peptide.
TRANSIT 1 20 Mitochondrion. {ECO:0000255}.
CHAIN 21 437 GTPase Era, mitochondrial.
/FTId=PRO_0000180082.
DOMAIN 112 330 Era-type G.
DOMAIN 360 437 KH type-2.
NP_BIND 120 127 GTP. {ECO:0000255}.
NP_BIND 167 171 GTP. {ECO:0000255}.
NP_BIND 236 239 GTP. {ECO:0000255}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000250|UniProtKB:O75616}.
CONFLICT 154 154 G -> W (in Ref. 1; BAB56113).
{ECO:0000305}.
CONFLICT 407 407 L -> S (in Ref. 4; AAH68271).
{ECO:0000305}.
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


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