MIRO1_CAEEL
ID MIRO1_CAEEL Reviewed; 625 AA.
AC Q94263;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Mitochondrial Rho GTPase 1;
DE Short=Miro;
DE EC=3.6.5.-;
GN Name=miro-1 {ECO:0000312|WormBase:K08F11.5};
GN ORFNames=K08F11.5 {ECO:0000312|WormBase:K08F11.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25190516; DOI=10.15252/embj.201489039;
RA Ackema K.B., Hench J., Boeckler S., Wang S.C., Sauder U., Mergentaler H.,
RA Westermann B., Bard F., Frank S., Spang A.;
RT "The small GTPase Arf1 modulates mitochondrial morphology and function.";
RL EMBO J. 33:2659-2675(2014).
CC -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking
CC (By similarity). Probably involved in control of anterograde transport
CC of mitochondria and their subcellular distribution (By similarity).
CC Plays a role in maintaining mitochondrial morphology (PubMed:25190516).
CC {ECO:0000250|UniProtKB:Q8IXI2, ECO:0000269|PubMed:25190516}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8IXI2}; Single-pass type IV membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a hyper-
CC connected mitochondrial network in body wall muscle cells.
CC {ECO:0000269|PubMed:25190516}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000305}.
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DR EMBL; BX284604; CCD68726.1; -; Genomic_DNA.
DR PIR; T30022; T30022.
DR RefSeq; NP_500620.1; NM_068219.3.
DR AlphaFoldDB; Q94263; -.
DR SMR; Q94263; -.
DR STRING; 6239.K08F11.5; -.
DR EPD; Q94263; -.
DR PaxDb; Q94263; -.
DR PeptideAtlas; Q94263; -.
DR PRIDE; Q94263; -.
DR EnsemblMetazoa; K08F11.5.1; K08F11.5.1; WBGene00019544.
DR GeneID; 177238; -.
DR KEGG; cel:CELE_K08F11.5; -.
DR UCSC; K08F11.5.1; c. elegans.
DR CTD; 177238; -.
DR WormBase; K08F11.5; CE11958; WBGene00019544; miro-1.
DR eggNOG; KOG1707; Eukaryota.
DR GeneTree; ENSGT00940000173880; -.
DR HOGENOM; CLU_014255_3_1_1; -.
DR InParanoid; Q94263; -.
DR OMA; HVSVTWN; -.
DR OrthoDB; 538388at2759; -.
DR PhylomeDB; Q94263; -.
DR Reactome; R-CEL-9013419; RHOT2 GTPase cycle.
DR Reactome; R-CEL-9013425; RHOT1 GTPase cycle.
DR PRO; PR:Q94263; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00019544; Expressed in pharyngeal muscle cell (C elegans) 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; 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; IMP:WormBase.
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; PF13202; EF-hand_5; 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 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..625
FT /note="Mitochondrial Rho GTPase 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000239326"
FT TOPO_DOM 1..601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 623..625
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 3..170
FT /note="Miro 1"
FT DOMAIN 188..223
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 308..343
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 420..625
FT /note="Miro 2"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
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 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 207
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 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 433..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 470..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 537..540
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 625 AA; 70222 MW; 1568FBA1315806C9 CRC64;
MSDDETLADV RIVLIGDEGC GKTSLVMSLL EDEWVDAVPR RLDRVLIPAD VTPENVTTSI
VDLSIKEEDE NWIVSEIRQA NVICVVYSVT DESTVDGIQT KWLPLIRQSF GEYHETPVIL
VGNKSDGTAN NTDKILPIME ANTEVETCVE CSARTMKNVS EIFYYAQKAV IYPTRPLYDA
DTKQLTDRAR KALIRVFKIC DRDNDGYLSD TELNDFQKLC FGIPLTSTAL EDVKRAVSDG
CPDGVANDSL MLAGFLYLHL LFIERGRHET TWAVLRKFGY ETSLKLSEDY LYPRITIPVG
CSTELSPEGV QFVSALFEKY DEDKDGCLSP SELQNLFSVC PVPVITKDNI LALETNQRGW
LTYNGYMAYW NMTTLINLTQ TFEQLAYLGF PVGRSGPGRA GNTLDSIRVT RERKKDLENH
GTDRKVFQCL VVGAKDAGKT VFMQSLAGRG MADVAQIGRR HSPFVINRVR VKEESKYLLL
REVDVLSPQD ALGSGETSAD VVAFLYDISN PDSFAFCATV YQKYFYRTKT PCVMIATKVE
REEVDQRWEV PPEEFCRQFE LPKPIKFSTG NIGQSSSPIF EQLAMMAVYP HLRRVFYLND
SNLLSKITFG AAIVALAGFL VLKNL
