MTG1_HUMAN
ID MTG1_HUMAN Reviewed; 334 AA.
AC Q9BT17; Q5VWX8; Q6PIY9; Q8IYJ4; Q8NC48; Q9BVU8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Mitochondrial ribosome-associated GTPase 1;
DE AltName: Full=GTP-binding protein 7;
DE AltName: Full=Mitochondrial GTPase 1;
DE Flags: Precursor;
GN Name=MTG1; Synonyms=GTPBP7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-293.
RC TISSUE=Ovary, Pancreas, Placenta, and Skin;
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 [4]
RP POSSIBLE FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12808030; DOI=10.1091/mbc.e02-10-0636;
RA Barrientos A., Korr D., Barwell K.J., Sjulsen C., Gajewski C.D.,
RA Manfredi G., Ackerman S., Tzagoloff A.;
RT "MTG1 codes for a conserved protein required for mitochondrial
RT translation.";
RL Mol. Biol. Cell 14:2292-2302(2003).
RN [5]
RP FUNCTION, ASSOCIATION WITH MITOCHONDRIAL RIBOSOME LARGE SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23396448; DOI=10.1093/nar/gkt079;
RA Kotani T., Akabane S., Takeyasu K., Ueda T., Takeuchi N.;
RT "Human G-proteins, ObgH1 and Mtg1, associate with the large mitochondrial
RT ribosome subunit and are involved in translation and assembly of
RT respiratory complexes.";
RL Nucleic Acids Res. 41:3713-3722(2013).
CC -!- FUNCTION: Plays a role in the regulation of the mitochondrial ribosome
CC assembly and of translational activity. Displays mitochondrial GTPase
CC activity. {ECO:0000269|PubMed:23396448}.
CC -!- SUBUNIT: Associates with the mitochondrial ribosome large subunit; the
CC association occurs in a GTP-dependent manner (PubMed:23396448).
CC {ECO:0000269|PubMed:23396448}.
CC -!- INTERACTION:
CC Q9BT17; Q86X53: ERICH1; NbExp=3; IntAct=EBI-2602570, EBI-12902263;
CC Q9BT17; O76014: KRT37; NbExp=3; IntAct=EBI-2602570, EBI-1045716;
CC Q9BT17; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2602570, EBI-79165;
CC Q9BT17; P32856-2: STX2; NbExp=3; IntAct=EBI-2602570, EBI-11956649;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:12808030, ECO:0000269|PubMed:23396448}; Peripheral
CC membrane protein {ECO:0000269|PubMed:12808030,
CC ECO:0000269|PubMed:23396448}; Matrix side {ECO:0000269|PubMed:12808030,
CC ECO:0000269|PubMed:23396448}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BT17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BT17-2; Sequence=VSP_023581, VSP_023582;
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04409.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH35721.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK074976; BAC11327.1; -; mRNA.
DR EMBL; AL161645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000920; AAH00920.1; -; mRNA.
DR EMBL; BC004409; AAH04409.1; ALT_INIT; mRNA.
DR EMBL; BC026039; AAH26039.1; -; mRNA.
DR EMBL; BC035721; AAH35721.1; ALT_INIT; mRNA.
DR CCDS; CCDS31320.1; -. [Q9BT17-1]
DR RefSeq; NP_612393.2; NM_138384.2. [Q9BT17-1]
DR PDB; 7O9K; EM; 3.10 A; C=1-334.
DR PDB; 7O9M; EM; 2.50 A; C=1-333.
DR PDB; 7PD3; EM; 3.40 A; z=1-334.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7PD3; -.
DR AlphaFoldDB; Q9BT17; -.
DR SMR; Q9BT17; -.
DR BioGRID; 124916; 153.
DR IntAct; Q9BT17; 16.
DR MINT; Q9BT17; -.
DR STRING; 9606.ENSP00000323047; -.
DR iPTMnet; Q9BT17; -.
DR PhosphoSitePlus; Q9BT17; -.
DR BioMuta; MTG1; -.
DR DMDM; 134034174; -.
DR EPD; Q9BT17; -.
DR jPOST; Q9BT17; -.
DR MassIVE; Q9BT17; -.
DR MaxQB; Q9BT17; -.
DR PaxDb; Q9BT17; -.
DR PeptideAtlas; Q9BT17; -.
DR PRIDE; Q9BT17; -.
DR ProteomicsDB; 78941; -. [Q9BT17-1]
DR ProteomicsDB; 78942; -. [Q9BT17-2]
DR Antibodypedia; 32682; 111 antibodies from 21 providers.
DR DNASU; 92170; -.
DR Ensembl; ENST00000317502.11; ENSP00000323047.6; ENSG00000148824.19. [Q9BT17-1]
DR GeneID; 92170; -.
DR KEGG; hsa:92170; -.
DR MANE-Select; ENST00000317502.11; ENSP00000323047.6; NM_138384.4; NP_612393.2.
DR UCSC; uc001lnd.4; human. [Q9BT17-1]
DR CTD; 92170; -.
DR DisGeNET; 92170; -.
DR GeneCards; MTG1; -.
DR HGNC; HGNC:32159; MTG1.
DR HPA; ENSG00000148824; Low tissue specificity.
DR neXtProt; NX_Q9BT17; -.
DR OpenTargets; ENSG00000148824; -.
DR PharmGKB; PA142671306; -.
DR VEuPathDB; HostDB:ENSG00000148824; -.
DR eggNOG; KOG2485; Eukaryota.
DR GeneTree; ENSGT00500000044923; -.
DR InParanoid; Q9BT17; -.
DR OMA; GVLWPKF; -.
DR OrthoDB; 583045at2759; -.
DR PhylomeDB; Q9BT17; -.
DR PathwayCommons; Q9BT17; -.
DR SignaLink; Q9BT17; -.
DR BioGRID-ORCS; 92170; 194 hits in 1082 CRISPR screens.
DR ChiTaRS; MTG1; human.
DR GeneWiki; MTG1; -.
DR GenomeRNAi; 92170; -.
DR Pharos; Q9BT17; Tbio.
DR PRO; PR:Q9BT17; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BT17; protein.
DR Bgee; ENSG00000148824; Expressed in right lobe of liver and 139 other tissues.
DR ExpressionAtlas; Q9BT17; baseline and differential.
DR Genevisible; Q9BT17; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005761; C:mitochondrial ribosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0070129; P:regulation of mitochondrial translation; IMP:UniProtKB.
DR GO; GO:0044065; P:regulation of respiratory system process; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR019991; GTP-bd_ribosome_bgen.
DR InterPro; IPR016478; GTPase_MTG1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PIRSF; PIRSF006230; MG442; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03596; GTPase_YlqF; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTP-binding; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transit peptide; Translation regulation.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..334
FT /note="Mitochondrial ribosome-associated GTPase 1"
FT /id="PRO_0000280262"
FT DOMAIN 36..209
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT BINDING 83..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 193..267
FT /note="SERPLMFLLDTPGVLAPRIESVETGLKLALCGTVLDHLVGEETMADYLLYTL
FT NKHQRFGYVQHYGLGSACDNVER -> ESSGARPSTLSRALQASGTCRPLCGFRLLTTL
FT PSPPLSVPAEHPRGRHCPCPYSTVVIVFAPNLWGRHAVFPISR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023581"
FT VAR_SEQ 268..334
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023582"
FT VARIANT 293
FT /note="I -> V (in dbSNP:rs2255246)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_062181"
SQ SEQUENCE 334 AA; 37237 MW; CEE3812DA5B588DA CRC64;
MRLTPRALCS AAQAAWRENF PLCGRDVARW FPGHMAKGLK KMQSSLKLVD CIIEVHDARI
PLSGRNPLFQ ETLGLKPHLL VLNKMDLADL TEQQKIMQHL EGEGLKNVIF TNCVKDENVK
QIIPMVTELI GRSHRYHRKE NLEYCIMVIG VPNVGKSSLI NSLRRQHLRK GKATRVGGEP
GITRAVMSKI QVSERPLMFL LDTPGVLAPR IESVETGLKL ALCGTVLDHL VGEETMADYL
LYTLNKHQRF GYVQHYGLGS ACDNVERVLK SVAVKLGKTQ KVKVLTGTGN VNIIQPNYPA
AARDFLQTFR RGLLGSVMLD LDVLRGHPPA ETLP
