MIRO1_ARATH
ID MIRO1_ARATH Reviewed; 648 AA.
AC Q8RXF8;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Mitochondrial Rho GTPase 1 {ECO:0000305};
DE Short=AtMIRO1 {ECO:0000303|PubMed:21494602};
DE EC=3.6.5.- {ECO:0000305};
DE AltName: Full=Miro-related GTPase 1 {ECO:0000305};
GN Name=MIRO1 {ECO:0000303|PubMed:18344283};
GN OrderedLocusNames=At5g27540 {ECO:0000312|Araport:AT5G27540};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20931334; DOI=10.1007/s00299-010-0926-5;
RA Yamaoka S., Nakajima M., Fujimoto M., Tsutsumi N.;
RT "MIRO1 influences the morphology and intracellular distribution of
RT mitochondria during embryonic cell division in Arabidopsis.";
RL Plant Cell Rep. 30:239-244(2011).
RN [8]
RP FUNCTION.
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 required to maintain proper development,
CC morphology and intracellular distribution of mitochondria, which in
CC turn are essential for the progress of embryonic cell division,
CC development of haploid male and female gametes, and pollen tube growth.
CC {ECO:0000269|PubMed:18344283, ECO:0000269|PubMed:20931334,
CC ECO:0000269|PubMed:21494602}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000305|PubMed:18344283}; Single-pass type IV membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. {ECO:0000269|PubMed:18344283}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality between the apical 2-cell and
CC the 4-terminal-cell embryo stage (PubMed:18344283, PubMed:20931334).
CC Impaired in pollen germination and pollen tube growth
CC (PubMed:18344283). {ECO:0000269|PubMed:18344283,
CC ECO:0000269|PubMed:20931334}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
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DR EMBL; AC007478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93698.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93699.1; -; Genomic_DNA.
DR EMBL; AY081280; AAL91169.1; -; mRNA.
DR EMBL; BT003352; AAO29970.1; -; mRNA.
DR RefSeq; NP_001031953.1; NM_001036876.2.
DR RefSeq; NP_198106.1; NM_122636.4.
DR AlphaFoldDB; Q8RXF8; -.
DR SMR; Q8RXF8; -.
DR IntAct; Q8RXF8; 5.
DR STRING; 3702.AT5G27540.1; -.
DR iPTMnet; Q8RXF8; -.
DR SwissPalm; Q8RXF8; -.
DR PaxDb; Q8RXF8; -.
DR PRIDE; Q8RXF8; -.
DR ProteomicsDB; 237032; -.
DR EnsemblPlants; AT5G27540.1; AT5G27540.1; AT5G27540.
DR EnsemblPlants; AT5G27540.2; AT5G27540.2; AT5G27540.
DR GeneID; 832814; -.
DR Gramene; AT5G27540.1; AT5G27540.1; AT5G27540.
DR Gramene; AT5G27540.2; AT5G27540.2; AT5G27540.
DR KEGG; ath:AT5G27540; -.
DR Araport; AT5G27540; -.
DR TAIR; locus:2146385; AT5G27540.
DR eggNOG; KOG1707; Eukaryota.
DR HOGENOM; CLU_014255_2_1_1; -.
DR InParanoid; Q8RXF8; -.
DR OMA; EGFISKW; -.
DR OrthoDB; 538388at2759; -.
DR PhylomeDB; Q8RXF8; -.
DR PRO; PR:Q8RXF8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8RXF8; baseline and differential.
DR Genevisible; Q8RXF8; AT.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0007005; P:mitochondrion organization; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
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; 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; PS51423; MIRO; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein 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 1"
FT /id="PRO_0000431715"
FT TOPO_DOM 1..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 641..648
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT DOMAIN 15..182
FT /note="Miro 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT DOMAIN 198..233
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 319..354
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 427..595
FT /note="Miro 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 338
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 MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 648 AA; 72322 MW; 204A762BAA0A9AA2 CRC64;
MARYAAGAVD CPGSPKSVRI VVVGDKGTGK SSLIVAAATD SFPPNVPPVL PDYKLPIEFF
PDGIPVTIVD TSSRPEDRDI VAEELKRADA VVLTYACDRP ETLERLSEYW LPELRRLEVK
IPIIVAGCKL DFRDDNNQVS LEQVMSPIMQ QFREIETCIE CSALKQLQAQ EVFYYAQKTV
LHPTGPLFDQ DSQALKPRCV RALKRIFILC DHDRDGALSE AELNDFQVKC FHAPLQPSEI
EGVKRVVQEK LPEGVNERGL TVTGFLFLHA LFIEKGRLET TWTVLRKFGY NNDIRLAEEL
LPSAIFKRAP DQSFELTNAA IDFLKGMYML FDDDQDNNLR PQEIEDLFST APESPWKEAP
YEDAAEKTAL GGLSFDAFLS MWSLMTLLEP ARSVENLIYI GFPGDPSTAI RVTRRRRLDR
KKQQCERKVF QCFVFGPNNA GKSALLNCFL GRSYTDNQES TTDERYAVNM VDESGAKKTL
IMREIPEDGV QGLFSSKESL AACDIAVFVY DSSDESSWKR ATQLLVEVAN YGEATGYEVP
CLMVSAKDDL DSSPISIQES TRMTQDMGIE PPVSISSKLG DFNNLFRKIL TAAQHPHLSI
PETEAGKSRK HYNRLINRSL MAVSIGAAAV VVGLAAYRVY ATRKSSSA
