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MIRO2_XENTR
ID   MIRO2_XENTR             Reviewed;         616 AA.
AC   Q6DIS1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, 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;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass type IV membrane protein {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; BC075464; AAH75464.1; -; mRNA.
DR   RefSeq; NP_001006725.1; NM_001006724.1.
DR   AlphaFoldDB; Q6DIS1; -.
DR   SMR; Q6DIS1; -.
DR   STRING; 8364.ENSXETP00000007838; -.
DR   PaxDb; Q6DIS1; -.
DR   DNASU; 448378; -.
DR   Ensembl; ENSXETT00000007838; ENSXETP00000007838; ENSXETG00000003628.
DR   GeneID; 448378; -.
DR   KEGG; xtr:448378; -.
DR   CTD; 89941; -.
DR   Xenbase; XB-GENE-489616; rhot2.
DR   eggNOG; KOG1707; Eukaryota.
DR   InParanoid; Q6DIS1; -.
DR   OrthoDB; 538388at2759; -.
DR   Reactome; R-XTR-9013419; RHOT2 GTPase cycle.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000003628; Expressed in 4-cell stage embryo and 13 other tissues.
DR   ExpressionAtlas; Q6DIS1; baseline.
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; IPR005225; Small_GTP-bd_dom.
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; 2.
DR   PIRSF; PIRSF037488; Mt_Rho_GTPase; 1.
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; 1.
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..616
FT                   /note="Mitochondrial Rho GTPase 2"
FT                   /id="PRO_0000239324"
FT   TOPO_DOM        1..590
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        591..613
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        614..616
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:0000305"
FT   DOMAIN          304..339
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          416..577
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         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         425..432
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         462..466
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"
SQ   SEQUENCE   616 AA;  69406 MW;  E0C79F2E7FAAC049 CRC64;
     MKRDVRILLL GEAQVGKTSL IMALVGEEFP DEVPSRAEEI TIPADVTPER IPTHIVDYSG
     VEQTEDELRE EIAKANVVCV VYDVTDLETI EKIGSKWIPM VNGNAERNSR LPIILVGNKS
     DLQCGSSMES ILPIMNQFSE IETCVECSAK NLKNISEVFY YAQKAVLHPT APLYDPEEKQ
     LRPQCKKALT RIFTISEQDN NQILSDEELN FFQQSCFGNP LAPQALEDVK MVVKKNTADG
     VRDNGLTLNG FLFLNTLFIQ RGRHETTWTI LRRFGYDDAL ELTDDYLYPP LRIPHESSTE
     LNHFGYQFLQ KAFEKHDLDE DGALSPSELQ SFFSVFPYTP WGPELASTVC TAQGGYLPLH
     GYLCQWTLVA YLDVHRCLEH LGYLGYPILC EQESQTHAIT VTREKSIDLE KGQTQRNVFL
     CRVIGPRGTG KSAFLRAFLG QSLEEQQQSN KPPSFYSVNT VLVGGQEKYL ILFEVDVDTE
     FLKTSDAPCD VACLMYDVSD SKSFNYCASI YKQHYMESQT PCLFVGCKYD QGEVKQQHGI
     SPAEFCHKHR LPPPYHFTCQ GTPDRTIYSK LATAAAFPHL HDTELSTASF WLRVALGATV
     AAVVGFTLYK ALLRSK
 
 
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