MIRO1_BOVIN
ID MIRO1_BOVIN Reviewed; 631 AA.
AC Q2HJF8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Mitochondrial Rho GTPase 1;
DE Short=MIRO-1;
DE EC=3.6.5.-;
DE AltName: Full=Ras homolog gene family member T1;
GN Name=RHOT1; Synonyms=ARHT1;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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. Promotes mitochondrial fission
CC during high calcium conditions (By similarity).
CC {ECO:0000250|UniProtKB:Q8IXI2}.
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 RAP1GDS1
CC (By similarity). Interacts with ARMCX1 (By similarity). Found in a
CC complex with KIF5B, OGT, RHOT2 and TRAK1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BG51, ECO:0000250|UniProtKB:Q8IXI2}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8IXI2}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q8IXI2}. Note=Colocalizes with MGARP and RHOT2
CC at the mitochondria. {ECO:0000250|UniProtKB:Q8IXI2}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30 (By similarity).
CC {ECO:0000250|UniProtKB:Q8IXI2}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00757, 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; BC105456; AAI05457.1; -; mRNA.
DR RefSeq; NP_001039547.1; NM_001046082.1.
DR AlphaFoldDB; Q2HJF8; -.
DR SMR; Q2HJF8; -.
DR STRING; 9913.ENSBTAP00000035196; -.
DR PaxDb; Q2HJF8; -.
DR PRIDE; Q2HJF8; -.
DR Ensembl; ENSBTAT00000035318; ENSBTAP00000035196; ENSBTAG00000010001.
DR GeneID; 511257; -.
DR KEGG; bta:511257; -.
DR CTD; 55288; -.
DR VEuPathDB; HostDB:ENSBTAG00000010001; -.
DR VGNC; VGNC:33953; RHOT1.
DR eggNOG; KOG1707; Eukaryota.
DR GeneTree; ENSGT00940000155641; -.
DR InParanoid; Q2HJF8; -.
DR OrthoDB; 538388at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000010001; Expressed in cardiac ventricle and 107 other tissues.
DR ExpressionAtlas; Q2HJF8; baseline and differential.
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; 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 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..631
FT /note="Mitochondrial Rho GTPase 1"
FT /id="PRO_0000239312"
FT TOPO_DOM 1..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..628
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 629..631
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 15..181
FT /note="Miro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT DOMAIN 197..232
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 317..352
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 429..592
FT /note="Miro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 70..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 438..445
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 476..480
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 540..543
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 631 AA; 72078 MW; 2352D63AF64E41A1 CRC64;
MPAGRGRPLR AADMKKDVRI LLVGEPRVGK TSLIMSLVSE EFPEEVPPRA EEITIPADVT
PERVPTHIVD YSEAEQSDEQ LHQEISQANV ICIVYAVNNK HSIDKVTSRW IPLINERTDK
DSRLPLILVG NKSDLVEYSS METILPIMNQ YTEIETCVEC SAKNLKNISE LFYYAQKAVL
HPTGPLYCPE EKEMKPACIK ALTRIFKISD QDNDGTLNDA ELNFFQRICF NTPLAPQALE
DVKNVVRKHI SDGVADGGLT LKGFLFLHTL FIQRGRHETT WTVLRRFGYD DDLDLTPEYL
FPLLKIPPDC TTELNHHAYL FLQSTFDKHD LDRDCALSPD ELKDLFKVFP YIPWGPDVNN
TVCTNEKGWI TYQGFLSQWT LTTYLDVQRC LEYLGYLGYS ILTEQESQAS AITVTRDKKI
DLQKKQTQRN VFRCNVIGMK NCGKSGVLQA LLGRNLTRQK KIRDDHKSYY AINTVYVYGQ
EKYLLLHDIS ESEFLTEAEI LCDVVCLVYD VSNPKSFEYC ARIFKQHFMD SRIPCLIVAA
KSDLHEVKQE YSISPTDFCR KHKMPPPQAF TCNTADAPSK DIFVKLTTMA MYPHVTQADL
KSSTFWLRAS FGATVFAVLG FAMYKALLKQ R
