MIRO2_MOUSE
ID MIRO2_MOUSE Reviewed; 620 AA.
AC Q8JZN7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Mitochondrial Rho GTPase 2;
DE Short=MIRO-2;
DE EC=3.6.5.-;
DE AltName: Full=Ras homolog gene family member T2;
GN Name=Rhot2; Synonyms=Arht2;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=15218247; DOI=10.1159/000078568;
RA Shan Y., Hexige S., Guo Z., Wan B., Chen K., Chen X., Ma L., Huang C.,
RA Zhao S., Yu L.;
RT "Cloning and characterization of the mouse Arht2 gene which encodes a
RT putative atypical GTPase.";
RL Cytogenet. Genome Res. 106:91-97(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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).
RN [4]
RP INTERACTION WITH ARMCX3.
RX PubMed=22569362; DOI=10.1038/ncomms1829;
RA Lopez-Domenech G., Serrat R., Mirra S., D'Aniello S., Somorjai I., Abad A.,
RA Vitureira N., Garcia-Arumi E., Alonso M.T., Rodriguez-Prados M.,
RA Burgaya F., Andreu A.L., Garcia-Sancho J., Trullas R., Garcia-Fernandez J.,
RA Soriano E.;
RT "The eutherian Armcx genes regulate mitochondrial trafficking in neurons
RT and interact with Miro and Trak2.";
RL Nat. Commun. 3:814-814(2012).
CC -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking.
CC Probably involved in control of anterograde transport of mitochondria
CC and their subcellular distribution (By similarity). {ECO:0000250}.
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 (By similarity). Interacts with ARMCX3
CC (PubMed:22569362). Found in a complex with KIF5B, OGT, RHOT1 and TRAK1
CC (By similarity). {ECO:0000250|UniProtKB:Q8IXI1,
CC ECO:0000269|PubMed:22569362}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass type IV membrane protein {ECO:0000250}. Note=Colocalizes
CC with MGARP and RHOT2 at the mitochondria. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15218247}.
CC -!- PTM: Ubiquitinated by PRKN in a PINK1-dependent manner, leading to its
CC degradation. {ECO:0000250|UniProtKB:Q8IXI1}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
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DR EMBL; AY311390; AAP78906.1; -; mRNA.
DR EMBL; BC029777; AAH29777.1; -; mRNA.
DR EMBL; BC034062; AAH34062.1; -; mRNA.
DR CCDS; CCDS37505.1; -.
DR RefSeq; NP_666111.1; NM_145999.2.
DR AlphaFoldDB; Q8JZN7; -.
DR SMR; Q8JZN7; -.
DR BioGRID; 229580; 1.
DR STRING; 10090.ENSMUSP00000044639; -.
DR iPTMnet; Q8JZN7; -.
DR PhosphoSitePlus; Q8JZN7; -.
DR SwissPalm; Q8JZN7; -.
DR EPD; Q8JZN7; -.
DR jPOST; Q8JZN7; -.
DR MaxQB; Q8JZN7; -.
DR PaxDb; Q8JZN7; -.
DR PeptideAtlas; Q8JZN7; -.
DR PRIDE; Q8JZN7; -.
DR ProteomicsDB; 252569; -.
DR DNASU; 214952; -.
DR Ensembl; ENSMUST00000043897; ENSMUSP00000044639; ENSMUSG00000025733.
DR GeneID; 214952; -.
DR KEGG; mmu:214952; -.
DR UCSC; uc008bch.1; mouse.
DR CTD; 89941; -.
DR MGI; MGI:2384892; Rhot2.
DR VEuPathDB; HostDB:ENSMUSG00000025733; -.
DR eggNOG; KOG1707; Eukaryota.
DR GeneTree; ENSGT00940000158109; -.
DR HOGENOM; CLU_014255_3_1_1; -.
DR InParanoid; Q8JZN7; -.
DR OMA; ELHATSF; -.
DR OrthoDB; 538388at2759; -.
DR PhylomeDB; Q8JZN7; -.
DR TreeFam; TF300814; -.
DR Reactome; R-MMU-9013419; RHOT2 GTPase cycle.
DR BioGRID-ORCS; 214952; 9 hits in 74 CRISPR screens.
DR ChiTaRS; Rhot2; mouse.
DR PRO; PR:Q8JZN7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8JZN7; protein.
DR Bgee; ENSMUSG00000025733; Expressed in retinal neural layer and 246 other tissues.
DR ExpressionAtlas; Q8JZN7; baseline and differential.
DR Genevisible; Q8JZN7; MM.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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; ISS:UniProtKB.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IBA:GO_Central.
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; IPR020860; MIRO_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 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 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 Calcium; GTP-binding; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..620
FT /note="Mitochondrial Rho GTPase 2"
FT /id="PRO_0000239319"
FT TOPO_DOM 1..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..617
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..620
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 415..578
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 /evidence="ECO:0000255"
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:0000305"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 424..431
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 461..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 526..529
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 620 AA; 69071 MW; 439D7AA800730B53 CRC64;
MRRDVRILLL GEAQVGKTSL ILSLVGEEFP EEVPARAEEI TIPADVTPEK VPTHIVDYSE
AEQTEEELQE EIHKANVVCV VYDVSEETTI EKIRTKWIPL VNGRTATGPR LPIILVGNKS
DLRPGSTMEA VLPIMSQFPE IETCVECSAK HLRNISELFY YAQKAVLHPT APLYDPEAKQ
LRPACAQALT RIFRLSDQDR DHGLSDEELN AFQKSCFGHP LAPQALEDVK RVVCKNVSGG
VQNDRLTLEG FLFLNTLFIQ RGRHETTWTI LRRFGYSDSL ELTPDYLYPA LHVPPGCSTE
LNHRGYQFVQ RMFEKHDQDH DGVLSPTELQ NLFSVFSGAP WGPELLHTVP TQAGCLPLHG
YLCQWTLMTY LDVQQCLAHL GYLGYPTLCE QDSQAQAITV TREKKLDQEK GQTQRSVLMC
KVLGARGVGK SAFLQAFLGN SLGEARDPPE KFPLHTINTV RVNGQEKYLI LCEVNADSLL
DTSLDTTCDV ACLMFDSSDP KTFVHCATIY KRYYMDGQTP CLFIASKADL PEGVAPPGLS
PAEFCRRHRL PAPASFSCLG PAMPSTDVFT QLATMATFPH LVHTELHPTS FWLRGVLVAV
GTAVAAVLSF SLYRVLVKSR
