MIRO2_BOVIN
ID MIRO2_BOVIN Reviewed; 618 AA.
AC Q5E9M9; A6H7G4; Q7YSE6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:Q8IXI1,
CC ECO:0000250|UniProtKB:Q8JZN7}.
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; AY247740; AAP04409.2; -; mRNA.
DR EMBL; BT020891; AAX08908.1; -; mRNA.
DR EMBL; BC146236; AAI46237.1; -; mRNA.
DR RefSeq; NP_847886.3; NM_178316.3.
DR AlphaFoldDB; Q5E9M9; -.
DR SMR; Q5E9M9; -.
DR STRING; 9913.ENSBTAP00000005979; -.
DR PaxDb; Q5E9M9; -.
DR PRIDE; Q5E9M9; -.
DR Ensembl; ENSBTAT00000005979; ENSBTAP00000005979; ENSBTAG00000004551.
DR GeneID; 352959; -.
DR KEGG; bta:352959; -.
DR CTD; 89941; -.
DR VEuPathDB; HostDB:ENSBTAG00000004551; -.
DR VGNC; VGNC:33954; RHOT2.
DR eggNOG; KOG1707; Eukaryota.
DR GeneTree; ENSGT00940000158109; -.
DR InParanoid; Q5E9M9; -.
DR OMA; ELHATSF; -.
DR OrthoDB; 538388at2759; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000004551; Expressed in retina and 104 other tissues.
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; SM00054; EFh; 2.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51423; MIRO; 2.
PE 2: Evidence at transcript 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..618
FT /note="Mitochondrial Rho GTPase 2"
FT /id="PRO_0000239317"
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 415..576
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: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 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: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 459..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 524..527
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT CONFLICT 245
FT /note="Q -> P (in Ref. 1; AAP04409)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="D -> E (in Ref. 1; AAP04409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 68152 MW; 1CEA30B829B407E7 CRC64;
MKRDVRILLL GEAQVGKTSL ILSLVGEEFP EEVPARAEEI TIPADVTPEK VPTHIVDYSE
TEQTVEELQG EIDKADVVCV VYDVSEEATV EKIRTKWIPL VNGDTKRGPR VPIILVGNKS
DLRPGGSMEA VLPIMSQFPE IETCVECSAK NLKNISELFY YAQKAVLHPT APLYDPEAKQ
LRPACAQALT RIFRLSDQDM DQALSDQELN AFQTSCFGHP LAPQALEDVK MVVSKNVVGG
VRDDQLTLDG FLFLNTLFIQ RGRHETTWTI LRRFGYGDSL ELTADYLCPP LRVPPGCSAE
LNHRGYQFVQ RMFEKHDQDR DGALSPAELQ SLFSVFPAAP WGPHLPSTVR TKAGRLPLHG
YLCQWTLVTY LDVRRSLEHL GYLGYPTLCE QDSQAHAITV TREKRLDQEK GQTQRNVLLC
KVVGARGVGK SSFLRAFLGH SLGHQDAGEP SVYAIDTVQV NGQEKYLILC EVAADSLLTA
SADASCDVAC LMFDGSDLRS FALCASVYKQ HYMDGQTPCL FVCSKADLPG GVPLPGLSPA
EFCRRHRLPT PTLFSCAGPV EPCMGIFTRL ATMATFPHLV HGQLQATSFW LRVALGAMGA
AVAAILSFSL YRVLVKSR
