ID MIRO1_HUMAN Reviewed; 618 AA. AC Q8IXI2; A4FVB6; A6NFV0; B4DG48; J9JIH9; Q6NUR3; Q6P9F8; Q6PJG1; Q6YMW8; AC Q86UB0; Q8IW28; Q8IXJ7; Q9H067; Q9H9N8; Q9NUZ2; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 2. DT 24-JAN-2024, entry version 184. DE RecName: Full=Mitochondrial Rho GTPase 1; DE Short=MIRO-1; DE Short=hMiro-1; DE EC=3.6.5.-; DE AltName: Full=Rac-GTP-binding protein-like protein; DE AltName: Full=Ras homolog gene family member T1; GN Name=RHOT1; Synonyms=ARHT1; 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 [MRNA] (ISOFORM 3). RX PubMed=12696059; DOI=10.1002/gcc.10206; RA Jenne D.E., Tinschert S., Dorschner M.O., Hameister H., Stephens K., RA Kehrer-Sawatzki H.; RT "Complete physical map and gene content of the human NF1 tumor suppressor RT region in human and mouse."; RL Genes Chromosomes Cancer 37:111-120(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND MUTAGENESIS OF PRO-13 AND THR-18. RX PubMed=12482879; DOI=10.1074/jbc.m208609200; RA Fransson A., Ruusala A., Aspenstroem P.; RT "Atypical Rho GTPases have roles in mitochondrial homeostasis and RT apoptosis."; RL J. Biol. Chem. 278:6495-6502(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Fetal brain; RA Zeng L., Xie Y., Mao Y.; RT "Cloning a novel Rac-GTP binding protein-like gene from human fetal RT brain."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Uterus; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 134-618 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE RP SCALE MRNA] OF 157-618 (ISOFORM 3). RC TISSUE=Amygdala, Placenta, and 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 18-618 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 90-550 (ISOFORM 6). RC TISSUE=Brain, Lung, Testis, and Uterus; 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 [8] RP MUTAGENESIS OF PRO-13. RX PubMed=14521508; DOI=10.1042/bj20031041; RA Aspenstroem P., Fransson A., Saras J.; RT "Rho GTPases have diverse effects on the organization of the actin filament RT system."; RL Biochem. J. 377:327-337(2004). RN [9] RP FUNCTION, INTERACTION WITH TRAK1 AND TRAK2, AND MUTAGENESIS OF PRO-13; RP THR-18; GLU-208; GLU-328; LYS-427 AND SER-432. RX PubMed=16630562; DOI=10.1016/j.bbrc.2006.03.163; RA Fransson S., Ruusala A., Aspenstroem P.; RT "The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in RT mitochondrial trafficking."; RL Biochem. Biophys. Res. Commun. 344:500-510(2006). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=19528298; DOI=10.1083/jcb.200811033; RA Li Y., Lim S., Hoffman D., Aspenstrom P., Federoff H.J., Rempe D.A.; RT "HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial RT distribution and transport."; RL J. Cell Biol. 185:1065-1081(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF SER-156. RX PubMed=22396657; DOI=10.1371/journal.pgen.1002537; RA Liu S., Sawada T., Lee S., Yu W., Silverio G., Alapatt P., Millan I., RA Shen A., Saxton W., Kanao T., Takahashi R., Hattori N., Imai Y., Lu B.; RT "Parkinson's disease-associated kinase PINK1 regulates Miro protein level RT and axonal transport of mitochondria."; RL PLoS Genet. 8:E1002537-E1002537(2012). RN [13] RP INTERACTION WITH KIF5B; OGT; RHOT2 AND TRAK1. RX PubMed=24995978; DOI=10.1016/j.cell.2014.06.007; RA Pekkurnaz G., Trinidad J.C., Wang X., Kong D., Schwarz T.L.; RT "Glucose regulates mitochondrial motility via Milton modification by O- RT GlcNAc transferase."; RL Cell 158:54-68(2014). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP UBIQUITINATION, AND DEUBIQUITINATION. RX PubMed=24896179; DOI=10.1038/nature13418; RA Bingol B., Tea J.S., Phu L., Reichelt M., Bakalarski C.E., Song Q., RA Foreman O., Kirkpatrick D.S., Sheng M.; RT "The mitochondrial deubiquitinase USP30 opposes parkin-mediated RT mitophagy."; RL Nature 510:370-375(2014). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] RP FUNCTION, AND INTERACTION WITH RAP1GDS1. RX PubMed=27716788; DOI=10.1371/journal.pgen.1006359; RA Ding L., Lei Y., Han Y., Li Y., Ji X., Liu L.; RT "Vimar Is a Novel Regulator of Mitochondrial Fission through Miro."; RL PLoS Genet. 12:e1006359-e1006359(2016). CC -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking CC (PubMed:12482879, PubMed:16630562, PubMed:22396657). Probably involved CC in control of anterograde transport of mitochondria and their CC subcellular distribution (PubMed:12482879, PubMed:16630562, CC PubMed:22396657). Promotes mitochondrial fission during high calcium CC conditions (PubMed:27716788). {ECO:0000269|PubMed:12482879, CC ECO:0000269|PubMed:16630562, ECO:0000269|PubMed:22396657, CC ECO:0000269|PubMed:27716788}. CC -!- SUBUNIT: Interacts with the kinesin-binding proteins TRAK1/OIP106 and CC TRAK2/GRIF1, forming a link between mitochondria and the trafficking CC apparatus of the microtubules (PubMed:16630562). Interacts with CC RAP1GDS1 (PubMed:27716788). Interacts with ARMCX1 (By similarity). CC Found in a complex with KIF5B, OGT, RHOT2 and TRAK1 (PubMed:24995978). CC {ECO:0000250|UniProtKB:Q8BG51, ECO:0000269|PubMed:16630562, CC ECO:0000269|PubMed:24995978, ECO:0000269|PubMed:27716788}. CC -!- INTERACTION: CC Q8IXI2; O60282: KIF5C; NbExp=2; IntAct=EBI-1396430, EBI-717170; CC Q8IXI2; Q9BXM7: PINK1; NbExp=3; IntAct=EBI-1396430, EBI-2846068; CC Q8IXI2; O60260: PRKN; NbExp=3; IntAct=EBI-1396430, EBI-716346; CC Q8IXI2; Q9UPV9: TRAK1; NbExp=5; IntAct=EBI-1396430, EBI-1105048; CC Q8IXI2; P56536: Kif5c; Xeno; NbExp=5; IntAct=EBI-1396430, EBI-994504; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000269|PubMed:12482879, ECO:0000269|PubMed:19528298}; Single-pass CC type IV membrane protein {ECO:0000269|PubMed:12482879, CC ECO:0000269|PubMed:19528298}. Note=Colocalizes with MGARP and RHOT2 at CC the mitochondria. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; CC IsoId=Q8IXI2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IXI2-2; Sequence=VSP_019155; CC Name=3; CC IsoId=Q8IXI2-3; Sequence=VSP_019156; CC Name=4; CC IsoId=Q8IXI2-4; Sequence=VSP_019157; CC Name=5; CC IsoId=Q8IXI2-5; Sequence=VSP_019158; CC Name=6; CC IsoId=Q8IXI2-6; Sequence=VSP_019153, VSP_019154; CC Name=7; CC IsoId=Q8IXI2-7; Sequence=VSP_047651; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high level in CC heart and skeletal muscle. {ECO:0000269|PubMed:12482879}. CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation CC and enhancement of mitophagy (PubMed:22396657, PubMed:24896179). CC Deubiquitinated by USP30 (PubMed:24896179). CC {ECO:0000269|PubMed:22396657, ECO:0000269|PubMed:24896179}. CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family. CC {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH41114.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH68463.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAA91969.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB14185.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ496730; CAD43139.1; -; mRNA. DR EMBL; AJ517412; CAD56956.1; -; mRNA. DR EMBL; AY094972; AAM15734.1; -; mRNA. DR EMBL; AL136929; CAB66863.1; -; mRNA. DR EMBL; AK001902; BAA91969.1; ALT_INIT; mRNA. DR EMBL; AK022695; BAB14185.1; ALT_INIT; mRNA. DR EMBL; AK294407; BAG57659.1; -; mRNA. DR EMBL; AC116407; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026620; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015698; AAH15698.1; -; mRNA. DR EMBL; BC041114; AAH41114.1; ALT_INIT; mRNA. DR EMBL; BC051818; AAH51818.1; -; mRNA. DR EMBL; BC060781; AAH60781.2; -; mRNA. DR EMBL; BC068463; AAH68463.1; ALT_INIT; mRNA. DR EMBL; BC125104; AAI25105.1; -; mRNA. DR EMBL; BC125105; AAI25106.1; -; mRNA. DR CCDS; CCDS32610.1; -. [Q8IXI2-3] DR CCDS; CCDS32611.1; -. [Q8IXI2-7] DR CCDS; CCDS32612.1; -. [Q8IXI2-1] DR CCDS; CCDS74030.1; -. [Q8IXI2-2] DR RefSeq; NP_001028738.1; NM_001033566.2. [Q8IXI2-7] DR RefSeq; NP_001028739.2; NM_001033567.2. DR RefSeq; NP_001028740.1; NM_001033568.2. [Q8IXI2-3] DR RefSeq; NP_001275683.1; NM_001288754.1. [Q8IXI2-2] DR RefSeq; NP_001275684.1; NM_001288755.1. DR RefSeq; NP_001275687.1; NM_001288758.1. DR RefSeq; NP_060777.3; NM_018307.4. [Q8IXI2-1] DR PDB; 5KSO; X-ray; 2.25 A; A=411-592. DR PDB; 5KSP; X-ray; 2.16 A; A/B=411-592. DR PDB; 5KSY; X-ray; 2.48 A; A=411-592. DR PDB; 5KSZ; X-ray; 2.50 A; A=177-592. DR PDB; 5KTY; X-ray; 2.52 A; A=177-592. DR PDB; 5KU1; X-ray; 2.50 A; A=177-592. DR PDB; 6D71; X-ray; 1.72 A; A/B=2-180. DR PDBsum; 5KSO; -. DR PDBsum; 5KSP; -. DR PDBsum; 5KSY; -. DR PDBsum; 5KSZ; -. DR PDBsum; 5KTY; -. DR PDBsum; 5KU1; -. DR PDBsum; 6D71; -. DR AlphaFoldDB; Q8IXI2; -. DR SMR; Q8IXI2; -. DR BioGRID; 120576; 88. DR CORUM; Q8IXI2; -. DR DIP; DIP-39114N; -. DR IntAct; Q8IXI2; 30. DR MINT; Q8IXI2; -. DR STRING; 9606.ENSP00000351132; -. DR GlyGen; Q8IXI2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8IXI2; -. DR PhosphoSitePlus; Q8IXI2; -. DR SwissPalm; Q8IXI2; -. DR BioMuta; RHOT1; -. DR DMDM; 108860796; -. DR EPD; Q8IXI2; -. DR jPOST; Q8IXI2; -. DR MassIVE; Q8IXI2; -. DR MaxQB; Q8IXI2; -. DR PeptideAtlas; Q8IXI2; -. DR ProteomicsDB; 71002; -. [Q8IXI2-1] DR ProteomicsDB; 71003; -. [Q8IXI2-2] DR ProteomicsDB; 71004; -. [Q8IXI2-3] DR ProteomicsDB; 71005; -. [Q8IXI2-4] DR ProteomicsDB; 71006; -. [Q8IXI2-5] DR ProteomicsDB; 71007; -. [Q8IXI2-6] DR Pumba; Q8IXI2; -. DR Antibodypedia; 2419; 266 antibodies from 26 providers. DR DNASU; 55288; -. DR Ensembl; ENST00000333942.10; ENSP00000334724.6; ENSG00000126858.19. [Q8IXI2-1] DR Ensembl; ENST00000358365.7; ENSP00000351132.3; ENSG00000126858.19. [Q8IXI2-3] DR Ensembl; ENST00000394692.6; ENSP00000378184.2; ENSG00000126858.19. [Q8IXI2-2] DR Ensembl; ENST00000545287.7; ENSP00000439737.2; ENSG00000126858.19. [Q8IXI2-7] DR Ensembl; ENST00000581031.5; ENSP00000464094.1; ENSG00000126858.19. [Q8IXI2-5] DR Ensembl; ENST00000581094.5; ENSP00000462669.1; ENSG00000126858.19. [Q8IXI2-4] DR GeneID; 55288; -. DR KEGG; hsa:55288; -. DR MANE-Select; ENST00000545287.7; ENSP00000439737.2; NM_001033566.3; NP_001028738.1. [Q8IXI2-7] DR UCSC; uc002hgv.4; human. [Q8IXI2-1] DR AGR; HGNC:21168; -. DR CTD; 55288; -. DR DisGeNET; 55288; -. DR GeneCards; RHOT1; -. DR HGNC; HGNC:21168; RHOT1. DR HPA; ENSG00000126858; Low tissue specificity. DR MIM; 613888; gene. DR neXtProt; NX_Q8IXI2; -. DR OpenTargets; ENSG00000126858; -. DR PharmGKB; PA134906318; -. DR VEuPathDB; HostDB:ENSG00000126858; -. DR eggNOG; KOG1707; Eukaryota. DR GeneTree; ENSGT00940000155641; -. DR HOGENOM; CLU_014255_3_1_1; -. DR InParanoid; Q8IXI2; -. DR OMA; IILRKFH; -. DR OrthoDB; 5481412at2759; -. DR PhylomeDB; Q8IXI2; -. DR TreeFam; TF300814; -. DR PathwayCommons; Q8IXI2; -. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-9013425; RHOT1 GTPase cycle. DR SignaLink; Q8IXI2; -. DR SIGNOR; Q8IXI2; -. DR BioGRID-ORCS; 55288; 32 hits in 1155 CRISPR screens. DR ChiTaRS; RHOT1; human. DR GeneWiki; RHOT1; -. DR GenomeRNAi; 55288; -. DR Pharos; Q8IXI2; Tbio. DR PRO; PR:Q8IXI2; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q8IXI2; Protein. DR Bgee; ENSG00000126858; Expressed in endothelial cell and 203 other cell types or tissues. DR ExpressionAtlas; Q8IXI2; baseline and differential. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; NAS:ParkinsonsUK-UCL. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0019725; P:cellular homeostasis; IMP:UniProtKB. DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IMP:UniProtKB. DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central. DR GO; GO:0047497; P:mitochondrion transport along microtubule; IMP:UniProtKB. DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR CDD; cd01893; Miro1; 1. DR CDD; cd01892; Miro2; 1. DR Gene3D; 1.10.238.10; EF-hand; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR013566; EF_hand_assoc_1. DR InterPro; IPR013567; EF_hand_assoc_2. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR021181; Miro. DR InterPro; IPR020860; MIRO_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR InterPro; IPR003578; Small_GTPase_Rho. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1. DR Pfam; PF08355; EF_assoc_1; 1. DR Pfam; PF08356; EF_assoc_2; 1. DR Pfam; PF00071; Ras; 1. DR PIRSF; PIRSF037488; Mt_Rho_GTPase; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00054; EFh; 2. DR SMART; SM00175; RAB; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; 2. DR PROSITE; PS51423; MIRO; 2. DR Genevisible; Q8IXI2; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; GTP-binding; Hydrolase; KW Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane; KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT CHAIN 1..618 FT /note="Mitochondrial Rho GTPase 1" FT /id="PRO_0000239313" FT TOPO_DOM 1..592 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 593..615 FT /note="Helical; Anchor for type IV membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 616..618 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT DOMAIN 2..168 FT /note="Miro 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757" FT DOMAIN 184..219 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 304..339 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 416..579 FT /note="Miro 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757" FT BINDING 11..18 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="1" FT BINDING 57..61 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 118..121 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 197 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 199 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 201 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 203 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 208 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 317 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 319 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 321 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 328 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 425..432 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="2" FT BINDING 463..467 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 527..530 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="2" FT /evidence="ECO:0000255" FT VAR_SEQ 224..247 FT /note="QALEDVKNVVRKHISDGVADSGLT -> RFGFEQVLVLLFLQFWALLCTKHY FT (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_019153" FT VAR_SEQ 248..618 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_019154" FT VAR_SEQ 580 FT /note="P -> PEDHYRDRLSRDMGHTDRIENLRKIWVFLKTAL (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_019155" FT VAR_SEQ 580 FT /note="P -> PEDHYRDRLSRDMGHTDRIENLRKIWVFLKTAFHARLRCMCTCNRCT FT FCICQNFLNSDLLQSVKNKIFTAVLNR (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12696059, FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3" FT /id="VSP_019156" FT VAR_SEQ 580 FT /note="P -> PHARLRCMCTCNRCTFCICQNFLNSDLLQSVKNKIFTAVLNR (in FT isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_047651" FT VAR_SEQ 581..618 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11230166" FT /id="VSP_019157" FT VAR_SEQ 582..618 FT /note="VTQADLKSSTFWLRASFGATVFAVLGFAMYKALLKQR -> ARLRCMCTCNR FT CTFCICQNFLNSDLLQSVKNKIFTAVLNRIISA (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_019158" FT MUTAGEN 13 FT /note="P->V: Causes constitutive activation inducing an FT aggregation of the mitochondrial network." FT /evidence="ECO:0000269|PubMed:12482879, FT ECO:0000269|PubMed:14521508, ECO:0000269|PubMed:16630562" FT MUTAGEN 18 FT /note="T->N: Causes constitutive inactivation." FT /evidence="ECO:0000269|PubMed:12482879, FT ECO:0000269|PubMed:16630562" FT MUTAGEN 156 FT /note="S->A: No effect on PINK1-PRKN-mediated degradation." FT /evidence="ECO:0000269|PubMed:22396657" FT MUTAGEN 208 FT /note="E->K: Abolishes the formation of thread-like FT mitochondria." FT /evidence="ECO:0000269|PubMed:16630562" FT MUTAGEN 328 FT /note="E->K: Abolishes the formation of thread-like FT mitochondria." FT /evidence="ECO:0000269|PubMed:16630562" FT MUTAGEN 427 FT /note="K->V: No effect." FT /evidence="ECO:0000269|PubMed:16630562" FT MUTAGEN 432 FT /note="S->N: No effect." FT /evidence="ECO:0000269|PubMed:16630562" FT CONFLICT 75 FT /note="A -> V (in Ref. 3; AAM15734)" FT /evidence="ECO:0000305" FT CONFLICT 246 FT /note="L -> F (in Ref. 7; AAH60781 and 5; BAA91969)" FT /evidence="ECO:0000305" FT CONFLICT 331 FT /note="D -> G (in Ref. 7; AAH60781)" FT /evidence="ECO:0000305" FT CONFLICT 587 FT /note="L -> P (in Ref. 2; CAD56956)" FT /evidence="ECO:0000305" FT STRAND 5..12 FT /evidence="ECO:0007829|PDB:6D71" FT HELIX 17..26 FT /evidence="ECO:0007829|PDB:6D71" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:6D71" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:6D71" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:6D71" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:6D71" FT HELIX 65..74 FT /evidence="ECO:0007829|PDB:6D71" FT STRAND 76..83 FT /evidence="ECO:0007829|PDB:6D71" FT HELIX 87..95 FT /evidence="ECO:0007829|PDB:6D71" FT HELIX 97..101 FT /evidence="ECO:0007829|PDB:6D71" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:6D71" FT HELIX 120..122 FT /evidence="ECO:0007829|PDB:6D71" FT HELIX 128..137 FT /evidence="ECO:0007829|PDB:6D71" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:6D71" FT TURN 149..152 FT /evidence="ECO:0007829|PDB:6D71" FT HELIX 155..167 FT /evidence="ECO:0007829|PDB:6D71" FT HELIX 183..196 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 206..217 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 225..234 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 238..242 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 248..259 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:5KU1" FT HELIX 266..273 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 280..282 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 284..287 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 299..301 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 303..316 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 321..324 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 326..332 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 333..335 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 359..372 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 374..383 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 386..389 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 395..398 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 399..401 FT /evidence="ECO:0007829|PDB:5KSZ" FT HELIX 405..410 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 418..424 FT /evidence="ECO:0007829|PDB:5KSP" FT HELIX 431..438 FT /evidence="ECO:0007829|PDB:5KSP" FT HELIX 443..446 FT /evidence="ECO:0007829|PDB:5KSP" FT HELIX 451..453 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 457..464 FT /evidence="ECO:0007829|PDB:5KSP" FT STRAND 467..476 FT /evidence="ECO:0007829|PDB:5KSP" FT HELIX 484..487 FT /evidence="ECO:0007829|PDB:5KSP" FT STRAND 490..497 FT /evidence="ECO:0007829|PDB:5KSP" FT TURN 501..503 FT /evidence="ECO:0007829|PDB:5KU1" FT HELIX 504..514 FT /evidence="ECO:0007829|PDB:5KSP" FT TURN 515..517 FT /evidence="ECO:0007829|PDB:5KSP" FT STRAND 518..520 FT /evidence="ECO:0007829|PDB:5KSZ" FT STRAND 522..527 FT /evidence="ECO:0007829|PDB:5KSP" FT STRAND 537..540 FT /evidence="ECO:0007829|PDB:5KSP" FT HELIX 542..548 FT /evidence="ECO:0007829|PDB:5KSP" FT STRAND 562..564 FT /evidence="ECO:0007829|PDB:5KSP" FT HELIX 568..577 FT /evidence="ECO:0007829|PDB:5KSP" SQ SEQUENCE 618 AA; 70784 MW; FE47AC3A4AF6F6C2 CRC64; MKKDVRILLV GEPRVGKTSL IMSLVSEEFP EEVPPRAEEI TIPADVTPER VPTHIVDYSE AEQSDEQLHQ EISQANVICI VYAVNNKHSI DKVTSRWIPL INERTDKDSR LPLILVGNKS DLVEYSSMET ILPIMNQYTE IETCVECSAK NLKNISELFY YAQKAVLHPT GPLYCPEEKE MKPACIKALT RIFKISDQDN DGTLNDAELN FFQRICFNTP LAPQALEDVK NVVRKHISDG VADSGLTLKG FLFLHTLFIQ RGRHETTWTV LRRFGYDDDL DLTPEYLFPL LKIPPDCTTE LNHHAYLFLQ STFDKHDLDR DCALSPDELK DLFKVFPYIP WGPDVNNTVC TNERGWITYQ GFLSQWTLTT YLDVQRCLEY LGYLGYSILT EQESQASAVT VTRDKKIDLQ KKQTQRNVFR CNVIGVKNCG KSGVLQALLG RNLMRQKKIR EDHKSYYAIN TVYVYGQEKY LLLHDISESE FLTEAEIICD VVCLVYDVSN PKSFEYCARI FKQHFMDSRI PCLIVAAKSD LHEVKQEYSI SPTDFCRKHK MPPPQAFTCN TADAPSKDIF VKLTTMAMYP HVTQADLKSS TFWLRASFGA TVFAVLGFAM YKALLKQR //