MIRO1_DANRE
ID MIRO1_DANRE Reviewed; 619 AA.
AC Q6NVC5; Q803L2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Mitochondrial Rho GTPase 1-A;
DE Short=MIRO-1-A;
DE EC=3.6.5.-;
DE AltName: Full=Ras homolog gene family member T1-A;
GN Name=rhot1a; ORFNames=zgc:55581;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-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 -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
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DR EMBL; BC044431; AAH44431.1; -; mRNA.
DR EMBL; BC068190; AAH68190.1; -; mRNA.
DR RefSeq; NP_997869.1; NM_212704.1.
DR AlphaFoldDB; Q6NVC5; -.
DR SMR; Q6NVC5; -.
DR STRING; 7955.ENSDARP00000024337; -.
DR PaxDb; Q6NVC5; -.
DR Ensembl; ENSDART00000163500; ENSDARP00000141563; ENSDARG00000099996.
DR GeneID; 327143; -.
DR KEGG; dre:327143; -.
DR CTD; 327143; -.
DR ZFIN; ZDB-GENE-030131-5354; rhot1a.
DR eggNOG; KOG1707; Eukaryota.
DR GeneTree; ENSGT00940000155641; -.
DR HOGENOM; CLU_014255_3_1_1; -.
DR InParanoid; Q6NVC5; -.
DR OMA; HVSVTWN; -.
DR OrthoDB; 538388at2759; -.
DR PhylomeDB; Q6NVC5; -.
DR TreeFam; TF300814; -.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR Reactome; R-DRE-9013425; RHOT1 GTPase cycle.
DR PRO; PR:Q6NVC5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000099996; Expressed in heart and 30 other tissues.
DR ExpressionAtlas; Q6NVC5; baseline.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:ZFIN.
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; 2.
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.
FT CHAIN 1..619
FT /note="Mitochondrial Rho GTPase 1-A"
FT /id="PRO_0000239316"
FT TOPO_DOM 1..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..616
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..619
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 416..580
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 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:0000305"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 425..432
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 463..467
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 528..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT CONFLICT 185
FT /note="C -> R (in Ref. 1; AAH44431)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="Q -> L (in Ref. 1; AAH44431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 71198 MW; CE13F88A5AF8B1DF CRC64;
MRKDVRILLV GEPKVGKTSL IMSLVSEEFP DEVPPRAEEI TIPADVTPER VPTHIVDYSE
AEQSDEQLYQ EITKANVICI VYSVNNKKSI EKVTSHWIPL INERTDKDSR VPLILVGNKS
DLVEHSSMET ILPIMNQYSE IETCVECSAK NLKNISELFY YAQKAVLHPT GPLYSPEEKE
MKPSCIKALT RIFKISDLDN DGILNDNELN FFQRTCFNIP LAPQALEDVK NVVRKNMTDG
VKDNGLTLKG FLFLHTLFIQ RGRHETTWTV LRRFGYDDDL ELTQEYLFPL FKIPPDCTTE
LNHNAYLFLQ SVFDKHDKDR DCALSPDELK DLFKVFPYMP WGPDVNNTVC TNEQGWITYQ
GYLSQWTLTT YLDVQRCLEY LGYLGYSIIQ EQESQAAAIT VTRNKRIDLQ KKQTQRSVFR
CNVLGARGCG KSGFLQAFLG RNLVRQKRIR EDHKSYYAIS TTYVYGQEKY LLLHEVLPDV
EFLSEADLAC DVVCLVYDIS NPRSFEYCAK VYKKHFMDSK TPCVIIAAKS DLHEARQYYS
LSPLDFCRKH KLHPPQLFTC NTTEAPSKDL YTKLTTMAMY PHMTQADLKN STFWLRASVG
ATVFAVLGFA MYKALLKQR
