MIRO2_PIG
ID MIRO2_PIG Reviewed; 620 AA.
AC Q864R5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
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).
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; AY247739; AAP04408.1; -; mRNA.
DR RefSeq; NP_999490.1; NM_214325.1.
DR AlphaFoldDB; Q864R5; -.
DR SMR; Q864R5; -.
DR STRING; 9823.ENSSSCP00000008541; -.
DR PaxDb; Q864R5; -.
DR PeptideAtlas; Q864R5; -.
DR PRIDE; Q864R5; -.
DR GeneID; 397596; -.
DR KEGG; ssc:397596; -.
DR CTD; 89941; -.
DR eggNOG; KOG1707; Eukaryota.
DR InParanoid; Q864R5; -.
DR OrthoDB; 538388at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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; 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; 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; 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..620
FT /note="Mitochondrial Rho GTPase 2"
FT /id="PRO_0000239320"
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 REGION 340..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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; 67619 MW; D6689E5EE1C0E6BE CRC64;
MKRDVRILLL GEAQVGKTSL ILSLVGEEFP EEVPPRAEEI TIPADVTPEK VPTHIVDYSE
AEQTAEELQD EIQKASVVCV VYDVSEETTV EKIRTKWIPL VNGGTRRGPR VPIILVGNKS
DLRPGGSMEA VLPIMSQFPE IETCVECSAK NLKNISELFY YAQKAVLHPT APLYDPEAKQ
LRPACAQALT RIFRLSDQDM DQALSDQELN AFQTCCFGHP LAPQALEDVK LVVSRNVAGG
VQDDRLTLDG FLFLNTLFIQ RGRHETTWTI LRRFGYSDSL ELTPDYLFPA LHVPPGCSAE
LNHHGYQFAQ RMLEKHDQDR DGALSPAELE SLFSVFPGPP WGPQLPRHRP HRGRSAAPAR
VPLPVDPGDL LGRPALSRAP WLPGLPHPLR AGLAGARHHS HQGEEAGPGK GQTQRNVLLC
KVLGARGVGK SSFLRAFLGR GLGDARGPPE EPSVYAIDTV RVGGQEKYLI LCEVAADSLL
TAEADASCDV ACLMFDSSDP GSFALCASVY KRHYMDGQIP CLFISSKADL PEGLSPPGLS
PSEFCRRHRL PAPTLFSCAG PAEPSTAVFA RLATMATFPH LVHGELHTTS FWLRVALGAV
GAAVAAILSF SLYRVLVKSR
