EFL1_MOUSE
ID EFL1_MOUSE Reviewed; 1127 AA.
AC Q8C0D5; Q80W46; Q8C198; Q8K0B8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Elongation factor-like GTPase 1;
DE AltName: Full=Elongation factor Tu GTP-binding domain-containing protein 1;
DE AltName: Full=Elongation factor-like 1;
DE AltName: Full=Protein FAM42A;
GN Name=Efl1; Synonyms=Eftud1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit and
CC translational activation of ribosomes. Together with SBDS, triggers the
CC GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm,
CC thereby activating ribosomes for translation competence by allowing 80S
CC ribosome assembly and facilitating EIF6 recycling to the nucleus, where
CC it is required for 60S rRNA processing and nuclear export. Has low
CC intrinsic GTPase activity. GTPase activity is increased by contact with
CC 60S ribosome subunits (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with the 60S ribosomal subunit. Found in a complex
CC consisting of the 60S ribosomal subunit, SBDS and EFL1.
CC {ECO:0000250|UniProtKB:Q7Z2Z2}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; AK028676; BAC26061.1; -; mRNA.
DR EMBL; AK031647; BAC27493.1; -; mRNA.
DR EMBL; BC031852; AAH31852.1; -; mRNA.
DR EMBL; BC045616; AAH45616.1; -; mRNA.
DR CCDS; CCDS21410.1; -.
DR RefSeq; NP_001153144.1; NM_001159672.1.
DR RefSeq; NP_780526.2; NM_175317.3.
DR AlphaFoldDB; Q8C0D5; -.
DR SMR; Q8C0D5; -.
DR BioGRID; 221694; 8.
DR STRING; 10090.ENSMUSP00000046046; -.
DR iPTMnet; Q8C0D5; -.
DR PhosphoSitePlus; Q8C0D5; -.
DR EPD; Q8C0D5; -.
DR MaxQB; Q8C0D5; -.
DR PaxDb; Q8C0D5; -.
DR PeptideAtlas; Q8C0D5; -.
DR PRIDE; Q8C0D5; -.
DR ProteomicsDB; 277553; -.
DR Antibodypedia; 55408; 89 antibodies from 18 providers.
DR DNASU; 101592; -.
DR Ensembl; ENSMUST00000039881; ENSMUSP00000046046; ENSMUSG00000038563.
DR Ensembl; ENSMUST00000179489; ENSMUSP00000137061; ENSMUSG00000038563.
DR GeneID; 101592; -.
DR KEGG; mmu:101592; -.
DR UCSC; uc009ide.2; mouse.
DR CTD; 79631; -.
DR MGI; MGI:2141969; Efl1.
DR VEuPathDB; HostDB:ENSMUSG00000038563; -.
DR eggNOG; KOG0467; Eukaryota.
DR GeneTree; ENSGT00550000074806; -.
DR HOGENOM; CLU_002794_3_1_1; -.
DR InParanoid; Q8C0D5; -.
DR OMA; ERFARCE; -.
DR OrthoDB; 140796at2759; -.
DR PhylomeDB; Q8C0D5; -.
DR TreeFam; TF105909; -.
DR BioGRID-ORCS; 101592; 22 hits in 71 CRISPR screens.
DR ChiTaRS; Efl1; mouse.
DR PRO; PR:Q8C0D5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8C0D5; protein.
DR Bgee; ENSMUSG00000038563; Expressed in seminiferous tubule of testis and 215 other tissues.
DR ExpressionAtlas; Q8C0D5; baseline and differential.
DR Genevisible; Q8C0D5; MM.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0042256; P:mature ribosome assembly; ISS:UniProtKB.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..1127
FT /note="Elongation factor-like GTPase 1"
FT /id="PRO_0000313806"
FT DOMAIN 17..272
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 429..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 92..96
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 146..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 528
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2Z2"
FT CONFLICT 249
FT /note="A -> P (in Ref. 2; AAH45616)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="K -> N (in Ref. 1; BAC26061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1127 AA; 125777 MW; 333623236F83E4E6 CRC64;
MVLSGVDKMI RLQKNTANIR NICVLAHVDH GKTTLADCLI SSNGIISSRL AGKLRYMDSR
EDEQVRGITM KSSAISLHYA EGHEEYLINL IDSPGHVDFS SEVSTAVRIC DGCIIVVDAV
EGVCPQTQAV LRQAWLENIR PVLVINKIDR LIVELKFTPQ EAYSHLKNIL EQINALTGTL
FTSKVLEERA ERETESQAKP HSEQGEQVYD WSAGLEDVDD SQLYFSPEQG NVVFTSAIDG
WGFGIEHFAR IYSQKIGIKK EVLLKTLWGD YYINMKAKKI MKVDQAKGKK PLFVQLILEN
IWSLYDAVLK KDKEKIDKIV TSLGLKIGAR EARHSDPKVQ INAICSQWLP ISHAVLAMVC
HKLPSPLDMT SERVEKLLCT GSQTFESLPP ETQALKAAFM KCGSEDTAPV IIFVSKMFAV
DVKALPQNKP RPLTQEEMAQ RRERARQRHA EKLAAAQGQT SQGPTQDGGA LETSPHEDEP
RGDEPDVASV SRQPVSQEES SQEAFIAFAR VFSGIARRGK KIFVLGPKYS PVDFLQRVPL
GFSAPLEDLP PVPHMACCTL ENLYLLMGRE LEDLEEVPPG NVLGIGGLQD FVLKSATLCS
LPSCPPFIPL NFEATPIVRV AVEPKHPSEM PQLVKGMKLL NQADPCVQVL IQETGEHVLV
TAGEVHLQRC LDDLRERFAK IHISVSEPII PFRETITKPP KVDMVNEEIG RQQKVAVIHQ
TKEEQSKIPE GIHVDSDGLI TIPTPNKLAT LSVRAIPLPE EVTRILEENS DLIRSMELLT
SSLNEGRNTQ AIHQKTQEKI WEFKGKLEKH LTGRKWRNTV DQIWSFGPRK CGPNILVSRS
EDFQNSVWSG PAGRESKEAS RFRDFGNSIV SGFQLATLSG PMCEEPLMGV CFVLEKWELN
KCAEQGASDK QHQGQCDLAG EGQGGGKTCH VGDENQEQQD VCSEPFEETS QKGDSPVIDC
YGPFSGQLIA TMKEACRYAL QVKPQRLMAA MYTCDIMATS DVLGRVYAVL SKREGRVLQE
EMKEGTDMFI IKAVLPVAES FGFADEIRKR TSGLASPQLV FSHWEVIPSD PFWVPTTEEE
YLHFGEKADS ENQARKYMNA VRKRKGLYVE EKIVEHAEKQ RTLSKNK
