MIRO2_HUMAN
ID MIRO2_HUMAN Reviewed; 618 AA.
AC Q8IXI1; A2IDC2; Q8NF53; Q96C13; Q96S17; Q9BT60; Q9H7M8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Mitochondrial Rho GTPase 2;
DE Short=MIRO-2;
DE Short=hMiro-2;
DE EC=3.6.5.-;
DE AltName: Full=Ras homolog gene family member T2;
GN Name=RHOT2; Synonyms=ARHT2, C16orf39;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANTS GLN-245 AND CYS-425.
RX PubMed=12482879; DOI=10.1074/jbc.m208609200;
RA Fransson A., Ruusala A., Aspenstroem P.;
RT "Atypical Rho GTPases have roles in mitochondrial homeostasis and
RT apoptosis.";
RL J. Biol. Chem. 278:6495-6502(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=15218247; DOI=10.1159/000078568;
RA Shan Y., Hexige S., Guo Z., Wan B., Chen K., Chen X., Ma L., Huang C.,
RA Zhao S., Yu L.;
RT "Cloning and characterization of the mouse Arht2 gene which encodes a
RT putative atypical GTPase.";
RL Cytogenet. Genome Res. 106:91-97(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP MUTAGENESIS OF ALA-13.
RX PubMed=14521508; DOI=10.1042/bj20031041;
RA Aspenstroem P., Fransson A., Saras J.;
RT "Rho GTPases have diverse effects on the organization of the actin filament
RT system.";
RL Biochem. J. 377:327-337(2004).
RN [10]
RP FUNCTION, INTERACTION WITH TRAK1 AND TRAK2, AND MUTAGENESIS OF ALA-13 AND
RP THR-18.
RX PubMed=16630562; DOI=10.1016/j.bbrc.2006.03.163;
RA Fransson S., Ruusala A., Aspenstroem P.;
RT "The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in
RT mitochondrial trafficking.";
RL Biochem. Biophys. Res. Commun. 344:500-510(2006).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=19528298; DOI=10.1083/jcb.200811033;
RA Li Y., Lim S., Hoffman D., Aspenstrom P., Federoff H.J., Rempe D.A.;
RT "HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial
RT distribution and transport.";
RL J. Cell Biol. 185:1065-1081(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION, AND UBIQUITINATION.
RX PubMed=22396657; DOI=10.1371/journal.pgen.1002537;
RA Liu S., Sawada T., Lee S., Yu W., Silverio G., Alapatt P., Millan I.,
RA Shen A., Saxton W., Kanao T., Takahashi R., Hattori N., Imai Y., Lu B.;
RT "Parkinson's disease-associated kinase PINK1 regulates Miro protein level
RT and axonal transport of mitochondria.";
RL PLoS Genet. 8:E1002537-E1002537(2012).
RN [14]
RP INTERACTION WITH KIF5B; OGT; RHOT1 AND TRAK1.
RX PubMed=24995978; DOI=10.1016/j.cell.2014.06.007;
RA Pekkurnaz G., Trinidad J.C., Wang X., Kong D., Schwarz T.L.;
RT "Glucose regulates mitochondrial motility via Milton modification by O-
RT GlcNAc transferase.";
RL Cell 158:54-68(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking
CC (PubMed:16630562, PubMed:22396657). Probably involved in control of
CC anterograde transport of mitochondria and their subcellular
CC distribution (PubMed:22396657). {ECO:0000269|PubMed:16630562,
CC ECO:0000269|PubMed:22396657}.
CC -!- SUBUNIT: Interacts with the kinesin-binding proteins TRAK1/OIP106 and
CC TRAK2/GRIF1, forming a link between mitochondria and the trafficking
CC apparatus of the microtubules (PubMed:16630562). Interacts with ARMCX3
CC (By similarity). Found in a complex with KIF5B, OGT, RHOT1 and TRAK1
CC (PubMed:24995978). {ECO:0000250|UniProtKB:Q8JZN7,
CC ECO:0000269|PubMed:16630562, ECO:0000269|PubMed:24995978}.
CC -!- INTERACTION:
CC Q8IXI1; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-1396563, EBI-3920694;
CC Q8IXI1; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-1396563, EBI-8638294;
CC Q8IXI1; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-1396563, EBI-2548832;
CC Q8IXI1; Q9UPV9: TRAK1; NbExp=3; IntAct=EBI-1396563, EBI-1105048;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:12482879, ECO:0000269|PubMed:19528298}; Single-pass
CC type IV membrane protein {ECO:0000269|PubMed:12482879,
CC ECO:0000269|PubMed:19528298}. Note=Colocalizes with MGARP and RHOT2 at
CC the mitochondria.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IXI1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IXI1-2; Sequence=VSP_019162, VSP_019163, VSP_019164;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in heart,
CC liver, skeletal muscle, kidney and pancreas.
CC {ECO:0000269|PubMed:12482879, ECO:0000269|PubMed:15218247}.
CC -!- PTM: Ubiquitinated by PRKN in a PINK1-dependent manner, leading to its
CC degradation. {ECO:0000269|PubMed:22396657}.
CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK61240.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB15740.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC03407.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ517413; CAD56957.1; -; mRNA.
DR EMBL; AY207375; AAP46090.1; -; mRNA.
DR EMBL; AK024450; BAB15740.1; ALT_INIT; mRNA.
DR EMBL; AK090426; BAC03407.1; ALT_INIT; mRNA.
DR EMBL; AE006464; AAK61240.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z92544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85763.1; -; Genomic_DNA.
DR EMBL; BC004327; AAH04327.1; -; mRNA.
DR EMBL; BC014942; AAH14942.1; -; mRNA.
DR CCDS; CCDS10417.1; -. [Q8IXI1-1]
DR RefSeq; NP_620124.1; NM_138769.2. [Q8IXI1-1]
DR PDB; 5KUT; X-ray; 1.69 A; A/B/C=409-588.
DR PDBsum; 5KUT; -.
DR AlphaFoldDB; Q8IXI1; -.
DR SMR; Q8IXI1; -.
DR BioGRID; 124646; 323.
DR CORUM; Q8IXI1; -.
DR IntAct; Q8IXI1; 49.
DR MINT; Q8IXI1; -.
DR STRING; 9606.ENSP00000321971; -.
DR iPTMnet; Q8IXI1; -.
DR PhosphoSitePlus; Q8IXI1; -.
DR SwissPalm; Q8IXI1; -.
DR BioMuta; RHOT2; -.
DR DMDM; 108860798; -.
DR EPD; Q8IXI1; -.
DR jPOST; Q8IXI1; -.
DR MassIVE; Q8IXI1; -.
DR MaxQB; Q8IXI1; -.
DR PaxDb; Q8IXI1; -.
DR PeptideAtlas; Q8IXI1; -.
DR PRIDE; Q8IXI1; -.
DR ProteomicsDB; 71000; -. [Q8IXI1-1]
DR ProteomicsDB; 71001; -. [Q8IXI1-2]
DR ABCD; Q8IXI1; 1 sequenced antibody.
DR Antibodypedia; 2477; 151 antibodies from 27 providers.
DR DNASU; 89941; -.
DR Ensembl; ENST00000315082.9; ENSP00000321971.4; ENSG00000140983.14. [Q8IXI1-1]
DR GeneID; 89941; -.
DR KEGG; hsa:89941; -.
DR MANE-Select; ENST00000315082.9; ENSP00000321971.4; NM_138769.3; NP_620124.1.
DR UCSC; uc002cip.4; human. [Q8IXI1-1]
DR CTD; 89941; -.
DR DisGeNET; 89941; -.
DR GeneCards; RHOT2; -.
DR HGNC; HGNC:21169; RHOT2.
DR HPA; ENSG00000140983; Low tissue specificity.
DR MIM; 613889; gene.
DR neXtProt; NX_Q8IXI1; -.
DR OpenTargets; ENSG00000140983; -.
DR PharmGKB; PA134889674; -.
DR VEuPathDB; HostDB:ENSG00000140983; -.
DR eggNOG; KOG1707; Eukaryota.
DR GeneTree; ENSGT00940000158109; -.
DR HOGENOM; CLU_014255_3_1_1; -.
DR InParanoid; Q8IXI1; -.
DR OMA; ELHATSF; -.
DR OrthoDB; 538388at2759; -.
DR PhylomeDB; Q8IXI1; -.
DR TreeFam; TF300814; -.
DR PathwayCommons; Q8IXI1; -.
DR Reactome; R-HSA-9013419; RHOT2 GTPase cycle.
DR SignaLink; Q8IXI1; -.
DR BioGRID-ORCS; 89941; 26 hits in 1082 CRISPR screens.
DR ChiTaRS; RHOT2; human.
DR GeneWiki; RHOT2; -.
DR GenomeRNAi; 89941; -.
DR Pharos; Q8IXI1; Tbio.
DR PRO; PR:Q8IXI1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8IXI1; protein.
DR Bgee; ENSG00000140983; Expressed in right hemisphere of cerebellum and 174 other tissues.
DR ExpressionAtlas; Q8IXI1; baseline and differential.
DR Genevisible; Q8IXI1; HS.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
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; IMP:UniProtKB.
DR GO; GO:0097345; P:mitochondrial outer membrane permeabilization; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; IMP: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; 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; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; GTP-binding; Hydrolase;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..618
FT /note="Mitochondrial Rho GTPase 2"
FT /id="PRO_0000239318"
FT TOPO_DOM 1..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..615
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..618
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 414..576
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:0000305"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 423..430
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 459..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 524..527
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_019162"
FT VAR_SEQ 251..340
FT /note="FLFLNTLFIQRGRHETTWTILRRFGYSDALELTADYLSPLIHVPPGCSTELN
FT HLGYQFVQRVFEKHDQDRDGALSPVELQSLFSVFPAAP -> EAGCPPVPGECGEGAVP
FT GAPPALSRCRFPLPEHALHPARPARDHLDHPAALRLQRCPGADCGLSLPSDPRAPRLQH
FT GAQPPWLPVCAESV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_019163"
FT VAR_SEQ 341..618
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.4"
FT /id="VSP_019164"
FT VARIANT 245
FT /note="R -> Q (in dbSNP:rs1139897)"
FT /evidence="ECO:0000269|PubMed:12482879"
FT /id="VAR_026637"
FT VARIANT 425
FT /note="R -> C (in dbSNP:rs3177338)"
FT /evidence="ECO:0000269|PubMed:12482879"
FT /id="VAR_026638"
FT MUTAGEN 13
FT /note="A->V: Causes constitutive activation inducing an
FT aggregation of the mitochondrial network."
FT /evidence="ECO:0000269|PubMed:14521508,
FT ECO:0000269|PubMed:16630562"
FT MUTAGEN 18
FT /note="T->N: Induces an aggregation of the mitochondrial
FT network."
FT /evidence="ECO:0000269|PubMed:16630562"
FT CONFLICT 139
FT /note="P -> S (in Ref. 1; CAD56957)"
FT /evidence="ECO:0000305"
FT STRAND 415..423
FT /evidence="ECO:0007829|PDB:5KUT"
FT HELIX 429..436
FT /evidence="ECO:0007829|PDB:5KUT"
FT STRAND 453..460
FT /evidence="ECO:0007829|PDB:5KUT"
FT STRAND 463..473
FT /evidence="ECO:0007829|PDB:5KUT"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:5KUT"
FT STRAND 486..494
FT /evidence="ECO:0007829|PDB:5KUT"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:5KUT"
FT TURN 512..514
FT /evidence="ECO:0007829|PDB:5KUT"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:5KUT"
FT STRAND 519..524
FT /evidence="ECO:0007829|PDB:5KUT"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:5KUT"
FT HELIX 539..545
FT /evidence="ECO:0007829|PDB:5KUT"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:5KUT"
FT HELIX 565..575
FT /evidence="ECO:0007829|PDB:5KUT"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:5KUT"
SQ SEQUENCE 618 AA; 68118 MW; C72ECBCA33D04B6B CRC64;
MRRDVRILLL GEAQVGKTSL ILSLVGEEFP EEVPPRAEEI TIPADVTPEK VPTHIVDYSE
AEQTDEELRE EIHKANVVCV VYDVSEEATI EKIRTKWIPL VNGGTTQGPR VPIILVGNKS
DLRSGSSMEA VLPIMSQFPE IETCVECSAK NLRNISELFY YAQKAVLHPT APLYDPEAKQ
LRPACAQALT RIFRLSDQDL DQALSDEELN AFQKSCFGHP LAPQALEDVK TVVCRNVAGG
VREDRLTLDG FLFLNTLFIQ RGRHETTWTI LRRFGYSDAL ELTADYLSPL IHVPPGCSTE
LNHLGYQFVQ RVFEKHDQDR DGALSPVELQ SLFSVFPAAP WGPELPRTVR TEAGRLPLHG
YLCQWTLVTY LDVRSCLGHL GYLGYPTLCE QDQAHAITVT REKRLDQEKG QTQRSVLLCK
VVGARGVGKS AFLQAFLGRG LGHQDTREQP PGYAIDTVQV NGQEKYLILC EVGTDGLLAT
SLDATCDVAC LMFDGSDPKS FAHCASVYKH HYMDGQTPCL FVSSKADLPE GVAVSGPSPA
EFCRKHRLPA PVPFSCAGPA EPSTTIFTQL ATMAAFPHLV HAELHPSSFW LRGLLGVVGA
AVAAVLSFSL YRVLVKSQ
