MIRO2_ARATH
ID MIRO2_ARATH Reviewed; 643 AA.
AC F4J0W4; Q93Z33; Q9LYA8;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Mitochondrial Rho GTPase 2;
DE Short=AtMIRO2 {ECO:0000303|PubMed:21494602};
DE EC=3.6.5.- {ECO:0000269|PubMed:16832621};
DE AltName: Full=Calcium-binding GTPase {ECO:0000303|PubMed:16832621};
DE Short=AtCBG {ECO:0000303|PubMed:16832621};
DE AltName: Full=Miro-related GTPase 2 {ECO:0000305};
GN Name=MIRO2 {ECO:0000303|PubMed:18344283};
GN OrderedLocusNames=At3g63150 {ECO:0000312|Araport:AT3G63150};
GN ORFNames=T20O10.250 {ECO:0000312|EMBL:CAB87760.1};
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 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 FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16832621; DOI=10.1007/s00299-006-0195-5;
RA Jayasekaran K., Kim K.N., Vivekanandan M., Shin J.S., Ok S.H.;
RT "Novel calcium-binding GTPase (AtCBG) involved in ABA-mediated salt stress
RT signaling in Arabidopsis.";
RL Plant Cell Rep. 25:1255-1262(2006).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION 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 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: Calcium-binding mitochondrial GTPase involved in calcium
CC signaling during salt stress response (PubMed:16832621). May play a
CC role in the progression of embryonic cell division, development of
CC haploid male and female gametes, and pollen tube growth
CC (PubMed:21494602). {ECO:0000269|PubMed:16832621,
CC ECO:0000269|PubMed:21494602}.
CC -!- ACTIVITY REGULATION: Activated by calcium.
CC {ECO:0000269|PubMed:16832621}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000305|PubMed:18344283}; Single-pass type IV membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed roots, rosette and cauline leaves, stems,
CC flowers and siliques. {ECO:0000269|PubMed:16832621,
CC ECO:0000269|PubMed:18344283}.
CC -!- INDUCTION: By abscisic acid (ABA) and NaCl.
CC {ECO:0000269|PubMed:16832621}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:16832621, PubMed:18344283). Mutant plants show
CC increased sensitivity to ABA, NaCl or mannitol during germination
CC (PubMed:16832621). {ECO:0000269|PubMed:16832621,
CC ECO:0000269|PubMed:18344283}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87760.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163816; CAB87760.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80441.1; -; Genomic_DNA.
DR EMBL; AY058178; AAL25592.1; -; mRNA.
DR EMBL; AY142018; AAM98282.1; -; mRNA.
DR PIR; T48104; T48104.
DR RefSeq; NP_567139.1; NM_116180.4.
DR AlphaFoldDB; F4J0W4; -.
DR SMR; F4J0W4; -.
DR IntAct; F4J0W4; 2.
DR STRING; 3702.AT3G63150.1; -.
DR iPTMnet; F4J0W4; -.
DR PaxDb; F4J0W4; -.
DR PRIDE; F4J0W4; -.
DR ProteomicsDB; 250713; -.
DR EnsemblPlants; AT3G63150.1; AT3G63150.1; AT3G63150.
DR GeneID; 825490; -.
DR Gramene; AT3G63150.1; AT3G63150.1; AT3G63150.
DR KEGG; ath:AT3G63150; -.
DR Araport; AT3G63150; -.
DR TAIR; locus:2099232; AT3G63150.
DR eggNOG; KOG1707; Eukaryota.
DR HOGENOM; CLU_014255_2_1_1; -.
DR InParanoid; F4J0W4; -.
DR OMA; ELHATSF; -.
DR OrthoDB; 538388at2759; -.
DR PRO; PR:F4J0W4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J0W4; baseline and differential.
DR Genevisible; F4J0W4; 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:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IDA:TAIR.
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:0009737; P:response to abscisic acid; IMP:TAIR.
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 2: Evidence at transcript level;
KW Calcium; GTP-binding; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW Repeat; Stress response; Transmembrane; Transmembrane helix.
FT CHAIN 1..643
FT /note="Mitochondrial Rho GTPase 2"
FT /id="PRO_0000431716"
FT TOPO_DOM 1..611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..643
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 315..350
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 423..592
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:0000305"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 330
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 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 437
FT /note="G -> R (in Ref. 3; AAL25592/AAM98282)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="M -> I (in Ref. 3; AAL25592/AAM98282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 71408 MW; 84CA7E170059F4C1 CRC64;
MMLGGKSSAG GRTSLRVAVA GDKGTGKSSL ISAVASETFP DNVPRVLPPI TLPADAFPDY
IPITIVDTPS SIDNRIKLIE EFRKADVVLL TYACDQPSTL DRLSSYWLPE LRRLEIKAPV
IVVGCKLDLR DERSPARLED IMSPIMKEYR EIETCIECSA LTLIQVPDVF YFASKAVLHP
TFPLFDQEKQ CLKPRLRRAV QRIFNLCDHD LDGALNDAEL NDFQVNCFGA PLDPVELMGV
KKVVQERQPD GVTDLGLTLP GFLFLFSLFI ERGRPETAWA ILRKCGYNDS LELHAELLPV
PAKQSPDQSI ELTNEAMDFL SGIFQLYDLD NDGALQPAEL DDLFQTAPDS PWLEDPYKEA
AEKTPGGSLT INGFLSEWAL MTLLDPRKSL ANLTYIGYGH DPASTFSVTR KRSVDRKKQR
TERNVFQCFV FGPKKSGKSA LLDSFLGRKF SNSYKATMGE RYAANVIDQP GGSKKTLILR
EIPEDRVKKF LTNKESLAAC DVAVVVYDSS DVYSWRKARE ILMEVARRGE ERGYGTPCLL
VAAKDDLDPY PMSVQESDRV CMELGIDIPV SLSMKLGEPN SLFSRIVSTA ENPHMSIPET
ESGRRSRNIR QLVNSSLLFV SVGTAVGFAG LAAYRAYSAR KNA
