MIRO1_HUMAN
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 03-AUG-2022, entry version 176.
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};
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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; 84.
DR CORUM; Q8IXI2; -.
DR DIP; DIP-39114N; -.
DR IntAct; Q8IXI2; 30.
DR MINT; Q8IXI2; -.
DR GlyGen; Q8IXI2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IXI2; -.
DR PhosphoSitePlus; Q8IXI2; -.
DR BioMuta; RHOT1; -.
DR DMDM; 108860796; -.
DR EPD; Q8IXI2; -.
DR jPOST; Q8IXI2; -.
DR MassIVE; Q8IXI2; -.
DR MaxQB; Q8IXI2; -.
DR PaxDb; Q8IXI2; -.
DR PeptideAtlas; Q8IXI2; -.
DR PRIDE; 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 Antibodypedia; 2419; 246 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 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; HVSVTWN; -.
DR OrthoDB; 538388at2759; -.
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 BioGRID-ORCS; 55288; 32 hits in 1078 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 201 other tissues.
DR ExpressionAtlas; Q8IXI2; baseline and differential.
DR Genevisible; Q8IXI2; HS.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
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: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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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; IPR029506; Miro-1.
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 PANTHER; PTHR24072; PTHR24072; 1.
DR PANTHER; PTHR24072:SF124; PTHR24072:SF124; 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 SMART; SM00054; EFh; 2.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51423; MIRO; 2.
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
