GUF1_MOUSE
ID GUF1_MOUSE Reviewed; 651 AA.
AC Q8C3X4; Q6PEN7; Q8BPS6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Translation factor Guf1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03137};
DE EC=3.6.5.-;
DE AltName: Full=Elongation factor 4 homolog {ECO:0000255|HAMAP-Rule:MF_03137};
DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_03137};
DE AltName: Full=GTPase Guf1 {ECO:0000255|HAMAP-Rule:MF_03137};
DE AltName: Full=Ribosomal back-translocase {ECO:0000255|HAMAP-Rule:MF_03137};
DE Flags: Precursor;
GN Name=Guf1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic heart, and Eye;
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] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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=Brown adipose tissue, Heart, and Kidney;
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: Promotes mitochondrial protein synthesis. May act as a
CC fidelity factor of the translation reaction, by catalyzing a one-codon
CC backward translocation of tRNAs on improperly translocated ribosomes.
CC Binds to mitochondrial ribosomes in a GTP-dependent manner.
CC {ECO:0000255|HAMAP-Rule:MF_03137}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03137};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03137}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03137}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03137}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C3X4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C3X4-2; Sequence=VSP_021345;
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. LepA subfamily.
CC {ECO:0000305}.
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DR EMBL; AK053420; BAC35380.2; -; mRNA.
DR EMBL; AK084627; BAC39234.1; -; mRNA.
DR EMBL; BC057962; AAH57962.1; -; mRNA.
DR CCDS; CCDS19322.1; -. [Q8C3X4-1]
DR CCDS; CCDS80296.1; -. [Q8C3X4-2]
DR RefSeq; NP_001297560.1; NM_001310631.1. [Q8C3X4-2]
DR RefSeq; NP_766299.1; NM_172711.3. [Q8C3X4-1]
DR AlphaFoldDB; Q8C3X4; -.
DR SMR; Q8C3X4; -.
DR BioGRID; 231103; 2.
DR STRING; 10090.ENSMUSP00000084480; -.
DR iPTMnet; Q8C3X4; -.
DR PhosphoSitePlus; Q8C3X4; -.
DR EPD; Q8C3X4; -.
DR MaxQB; Q8C3X4; -.
DR PaxDb; Q8C3X4; -.
DR PeptideAtlas; Q8C3X4; -.
DR PRIDE; Q8C3X4; -.
DR ProteomicsDB; 271112; -. [Q8C3X4-1]
DR ProteomicsDB; 271113; -. [Q8C3X4-2]
DR Antibodypedia; 1337; 140 antibodies from 26 providers.
DR DNASU; 231279; -.
DR Ensembl; ENSMUST00000031113; ENSMUSP00000031113; ENSMUSG00000029208. [Q8C3X4-2]
DR Ensembl; ENSMUST00000087228; ENSMUSP00000084480; ENSMUSG00000029208. [Q8C3X4-1]
DR GeneID; 231279; -.
DR KEGG; mmu:231279; -.
DR UCSC; uc008xqm.1; mouse. [Q8C3X4-1]
DR UCSC; uc008xqn.1; mouse. [Q8C3X4-2]
DR CTD; 60558; -.
DR MGI; MGI:2140726; Guf1.
DR VEuPathDB; HostDB:ENSMUSG00000029208; -.
DR eggNOG; KOG0462; Eukaryota.
DR GeneTree; ENSGT00550000074940; -.
DR InParanoid; Q8C3X4; -.
DR OMA; MVQIAIQ; -.
DR OrthoDB; 165663at2759; -.
DR PhylomeDB; Q8C3X4; -.
DR TreeFam; TF314751; -.
DR BioGRID-ORCS; 231279; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Guf1; mouse.
DR PRO; PR:Q8C3X4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C3X4; protein.
DR Bgee; ENSMUSG00000029208; Expressed in embryonic post-anal tail and 212 other tissues.
DR ExpressionAtlas; Q8C3X4; baseline and differential.
DR Genevisible; Q8C3X4; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.2570; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00071; LepA; 1.
DR InterPro; IPR006297; EF-4.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
DR InterPro; IPR035654; LepA_IV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43512; PTHR43512; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF06421; LepA_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR01393; lepA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTP-binding; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT CHAIN 32..651
FT /note="Translation factor Guf1, mitochondrial"
FT /id="PRO_0000256252"
FT DOMAIN 48..229
FT /note="tr-type G"
FT BINDING 57..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 122..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 176..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT VAR_SEQ 296..383
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021345"
SQ SEQUENCE 651 AA; 72463 MW; 7DA56A6C43753960 CRC64;
MWALVGRALA PWAAGARHAA ASEPRAACRL FSAAELKEKP DMSRFPVEDI RNFSIIAHVD
HGKSTLADRL LELTGTIDKT KKNKQVLDKL QVERERGITV KAQTASLFYS FGGKQYLLNL
IDTPGHVDFS YEVSRSLSAC QGVLLVVDAN EGIQAQTVAN FFLAFEAQLS VIPVINKIDL
KNADPERVGK QIEKVFDIPS EECIKISAKL GTNVDSVLQA VIERIPPPKV HRENPLKALV
FDSTFDQYRG VIANIALFDG VVSKGDKIVS AHTKKAYEVN EVGILNPNEQ PTHKLYAGQV
GFLIAGMKDV TEAQIGDTLY LHNHPVEPLP GFKSAKPMVF AGVYPIDQSE YNNLKSAIEK
LTLNDSSVTV HRDSSLALGA GWRLGFLGLL HMEVFNQRLE QEYNASVILT TPTVPYKAVL
SSAKLIKEYK EKEITIINPA QFPEKSQVTE YLEPVVLGTV ITPTEYTGKI MALCQARRAI
QKNMTFIDEN RVMLKYLFPL NEIVVDFYDS LKSLSSGYAS FDYEDAGYQT AELVKMDILL
NGNMVEELVT VVHREKAYTV GKSICERLKE SLPRQLYEIA IQAAVGSKVI ARETVKAYRK
NVLAKCYGGD ITRKMKLLKR QSEGKKKLRK IGNIEIPKDA FIKVLKTQPN K
