MIRO_DROPS
ID MIRO_DROPS Reviewed; 649 AA.
AC Q298L5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Mitochondrial Rho GTPase;
DE Short=Miro;
DE EC=3.6.5.-;
GN Name=Miro; ORFNames=GA18862;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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 -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL27940.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM000070; EAL27940.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_003736596.1; XM_003736548.2.
DR AlphaFoldDB; Q298L5; -.
DR SMR; Q298L5; -.
DR STRING; 7237.FBpp0282009; -.
DR EnsemblMetazoa; FBtr0368129; FBpp0330947; FBgn0078862.
DR KEGG; dpo:Dpse_GA18862; -.
DR eggNOG; KOG1707; Eukaryota.
DR HOGENOM; CLU_014255_3_1_1; -.
DR InParanoid; Q298L5; -.
DR PhylomeDB; Q298L5; -.
DR ChiTaRS; cpa; fly.
DR Proteomes; UP000001819; Genome assembly.
DR Bgee; FBgn0078862; Expressed in male reproductive system and 3 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; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0019725; P:cellular homeostasis; ISS:UniProtKB.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; ISS:UniProtKB.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; ISS:UniProtKB.
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; 2.
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 3: Inferred from homology;
KW Calcium; GTP-binding; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..649
FT /note="Mitochondrial Rho GTPase"
FT /id="PRO_0000239328"
FT TOPO_DOM 1..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..649
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 9..192
FT /note="Miro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT DOMAIN 208..243
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 328..363
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 441..604
FT /note="Miro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
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 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 450..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 488..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 555..558
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 649 AA; 73475 MW; C76DF5A3E6AFF9BA CRC64;
MGQYTVSTRK NVRILLVGDA GVGKTSLILS LVSEEYPEEV PPRAEEITIP ANVTPEQVPT
SIVDFSSVEQ TEETLGLEIN KAHVVCIVYS VDDDDSLDRI TSHWLPLIRS KCNATLEGDA
ETEAETEAAG EGLRKPIVLV GNKIDLIDYS TMDSVLAIME DFPEIESCVE CSAKTLHNIS
EMFYYAQKAV LHPTSPLYIM EDQELTPACK KSLVRIFKIC DTDGDNLLND YELNLFQRRC
FNTPLQPQIL DEVKAVIQKN VPDGIYNDAV TLKGFLFLHC LFIQRGRNET TWAVLRRFGY
NDQLEMCQEY LRPPLKIPPG SSTELSHRGQ KFLISVFERY DRDCDGALSP EEHKMLFSVC
PSSPWSYSTD IRKSCPINDK GWVTLHGWLC RWTLMTLIDV VKTMEYLAYL GFNVHENDSL
LAAIHVTRER RIDLAKRQSS RSVYKCHVIG PNGSGKTGLC RGFLVDEMQK LIGKEFKTNV
VHCINSVQVY GQEKHLILRD IDVRHALDPL QPQEVNCDVA CLVYDSSNPR SFEYVARIYI
KYYAESKIPV MIVGTKCDMD ERRQDYLMQP AEFCAKYKLL PPHLFSLRTN KKELYTKLAT
MAAFPHLRHF GLLTEDSKLL WKAGLGLAAA TMLGFIVLKT LSAAGSHSR
