MIRO3_ARATH
ID MIRO3_ARATH Reviewed; 648 AA.
AC Q9MA88;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Mitochondrial Rho GTPase 3;
DE Short=AtMIRO3 {ECO:0000303|PubMed:21494602};
DE EC=3.6.5.- {ECO:0000305};
DE AltName: Full=Miro-related GTPase 3 {ECO:0000305};
GN Name=MIRO3 {ECO:0000303|PubMed:18344283};
GN OrderedLocusNames=At3g05310 {ECO:0000312|Araport:AT3G05310};
GN ORFNames=T12H1.28 {ECO:0000312|EMBL:AAF27037.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=18344283; DOI=10.1105/tpc.107.055756;
RA Yamaoka S., Leaver C.J.;
RT "EMB2473/MIRO1, an Arabidopsis Miro GTPase, is required for embryogenesis
RT and influences mitochondrial morphology in pollen.";
RL Plant Cell 20:589-601(2008).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=21494602; DOI=10.1371/journal.pone.0018530;
RA Sormo C.G., Brembu T., Winge P., Bones A.M.;
RT "Arabidopsis thaliana MIRO1 and MIRO2 GTPases are unequally redundant in
RT pollen tube growth and fusion of polar nuclei during female
RT gametogenesis.";
RL PLoS ONE 6:E18530-E18530(2011).
CC -!- FUNCTION: Mitochondrial GTPase that may be involved in mitochondrion
CC development. {ECO:0000250|UniProtKB:Q8RXF8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q8RXF8}; Single-pass type IV membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at very low levels in roots, leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:18344283}.
CC -!- DEVELOPMENTAL STAGE: Hihly expressed in both chalazal and peripheral
CC endosperm during embryo development (from pre-globular to heart stage).
CC {ECO:0000305|PubMed:21494602}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
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DR EMBL; AC009177; AAF27037.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74218.1; -; Genomic_DNA.
DR RefSeq; NP_187182.1; NM_111404.1.
DR AlphaFoldDB; Q9MA88; -.
DR SMR; Q9MA88; -.
DR STRING; 3702.AT3G05310.1; -.
DR PaxDb; Q9MA88; -.
DR PRIDE; Q9MA88; -.
DR EnsemblPlants; AT3G05310.1; AT3G05310.1; AT3G05310.
DR GeneID; 819695; -.
DR Gramene; AT3G05310.1; AT3G05310.1; AT3G05310.
DR KEGG; ath:AT3G05310; -.
DR Araport; AT3G05310; -.
DR TAIR; locus:2096224; AT3G05310.
DR eggNOG; KOG1707; Eukaryota.
DR HOGENOM; CLU_014255_2_1_1; -.
DR InParanoid; Q9MA88; -.
DR OMA; PLIERCY; -.
DR OrthoDB; 538388at2759; -.
DR PhylomeDB; Q9MA88; -.
DR PRO; PR:Q9MA88; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MA88; baseline and differential.
DR Genevisible; Q9MA88; AT.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
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:0007005; P:mitochondrion organization; IBA:GO_Central.
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; IPR006073; GTP-bd.
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; PF01926; MMR_HSR1; 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; 1.
PE 2: Evidence at transcript level;
KW Calcium; GTP-binding; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..648
FT /note="Mitochondrial Rho GTPase 3"
FT /id="PRO_0000431717"
FT TOPO_DOM 1..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 622..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..648
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT DOMAIN 12..179
FT /note="Miro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT DOMAIN 195..230
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 316..351
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 425..599
FT /note="Miro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
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 210
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 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8RXF8"
SQ SEQUENCE 648 AA; 73067 MW; D22FD23B724D8B7B CRC64;
MWMGVGDSSG SPKPIRIVVV GEKGSGKSSL IMAAARNTFH PNIPSLLPYT NLPSEFFPDR
IPATVIDTSS RPEDKGKVVK EVRQADAIVL TFAFDRPETL DRLSKYWLPL FRQLEVRVPI
IVAGYEVDNK EAYNHFSIEQ ITSALMKQYR EVETSIQWSA QRLDQAKDVL YYAQKAVIDP
VGPVFDQENN VLKPRCIAAL KRIFLLSDHN MDGILSDEEL NELQKKCFDT PLVPCEIKQM
KNVMQVTFPQ GVNERGLTLD GFLFLNTRLI EEARIQTLWT MLRKFGYSND LRLGDDLVPY
SSFKRQADQS VELTNVAIEF LREVYEFFDS NGDNNLEPHE MGYLFETAPE SPWTKPLYKD
VTEENMDGGL SLEAFLSLWS LMTLIDPPRS LEYLMYIRFP SDDPSSAVRV TRKRVLDRKE
KKSERKVVQC FVFGPKNAGK SALLNQFIGR SYDDDSNNNN GSTDEHYAVN MVKEPGVISD
TDKTLVLKEV RIKDDGFMLS KEALAACDVA IFIYDSSDEY SWNRAVDMLA EVATIAKDSG
YVFPCLMVAA KTDLDPFPVA IQESTRVTQD IGIDAPIPIS SKLGDVSNLF RKILTAAENP
HLNIPEIESK KKRSCKLNNR SLMAVSIGTA VLIAGLASFR LYTARKQS
