MIRO2_RAT
ID MIRO2_RAT Reviewed; 622 AA.
AC Q7TSA0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 INTERACTION WITH KIF5B; OGT; RHOT1 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).
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 (By similarity). Found in a complex with KIF5B, OGT, RHOT1 and TRAK1
CC (PubMed:24995978). {ECO:0000250|UniProtKB:Q8IXI1,
CC ECO:0000250|UniProtKB:Q8JZN7, ECO:0000269|PubMed:24995978}.
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 -!- 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; AY303973; AAP60015.1; -; mRNA.
DR RefSeq; NP_861544.1; NM_181823.1.
DR RefSeq; XP_017452558.1; XM_017597069.1.
DR AlphaFoldDB; Q7TSA0; -.
DR SMR; Q7TSA0; -.
DR BioGRID; 252047; 1.
DR STRING; 10116.ENSRNOP00000027083; -.
DR PhosphoSitePlus; Q7TSA0; -.
DR jPOST; Q7TSA0; -.
DR PaxDb; Q7TSA0; -.
DR PRIDE; Q7TSA0; -.
DR ABCD; Q7TSA0; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000027083; ENSRNOP00000027083; ENSRNOG00000019930.
DR GeneID; 287156; -.
DR KEGG; rno:287156; -.
DR UCSC; RGD:727970; rat.
DR CTD; 89941; -.
DR RGD; 727970; Rhot2.
DR eggNOG; KOG1707; Eukaryota.
DR GeneTree; ENSGT00940000158109; -.
DR HOGENOM; CLU_014255_3_1_1; -.
DR InParanoid; Q7TSA0; -.
DR OMA; ELHATSF; -.
DR OrthoDB; 538388at2759; -.
DR PhylomeDB; Q7TSA0; -.
DR TreeFam; TF300814; -.
DR Reactome; R-RNO-9013419; RHOT2 GTPase cycle.
DR PRO; PR:Q7TSA0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000019930; Expressed in stomach and 20 other tissues.
DR Genevisible; Q7TSA0; RN.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
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; 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..622
FT /note="Mitochondrial Rho GTPase 2"
FT /id="PRO_0000239321"
FT TOPO_DOM 1..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..619
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..622
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..580
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 463..467
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 528..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 69153 MW; 8152E533C5591CE6 CRC64;
MRRDVRILLL GEAQVGKTSL ILSLVGEEFP EEVPARAEEI TIPADVTPEK VPTHIVDYSE
AEQTEEELQE EIHKANVVCV VYDVSEEATI EKIRTKWIPL VNGRTATGPR LPIILVGNKS
DLRPGSTIEA VLPIMSQFPE IETCVECSAK HLRNISELFY YAQKAVLHPT APLYDPEAKQ
LRPACAQALT RIFRLSDQDL DHALSDKELN AFQKSCFGHP LAPQALEDVK RVVCKNVAGG
VQDDRLTLEG FLFLNTLFIQ RGRHETTWTI LRRFGYSDSL ELTPDYLCPP LYVPPGCSTE
LNHRGYQFVQ RVFEKHDQDH DGVLSPTELE SLFSVFSVAP WGPELLHTVP TEAGCLSLRG
YLCQWTLVTY LDVQHCLAHL GYLGYPTLCE QDSQAQAITV TREKRLDQEK GQTQRSVLMC
KVLGARGVGK SAFLQAFLGH SLGEARDRDA PEKLPTHTIN TVRVSGQEKY LILCEVNADS
LLDTSLDTTC DVACLMFDSS DPETFVQCAT IYKRYYMDGQ TPCLFISSKA DLPEGVAPPG
LSPAEFCRRH RLPAPASFSC LGPAQSSIDV FTQLATMATF PHLAHTELHP TPFWLRGVLV
AVGTAVAAVL SFSLYRVLVK SR
