ID   GEM1_YEAST              Reviewed;         662 AA.
AC   P39722; D6VPG8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=Mitochondrial Rho GTPase 1;
DE            EC=3.6.5.-;
DE   AltName: Full=GTPase EF-hand protein of mitochondria 1;
GN   Name=GEM1; OrderedLocusNames=YAL048C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
RN   [4]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA   Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA   Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT   "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT   accumulation of a subclass of preproteins.";
RL   Mol. Biol. Cell 17:1436-1450(2006).
RN   [5]
RP   PRELIMINARY FUNCTION.
RX   PubMed=10220001;
RX   DOI=10.1002/(sici)1097-0061(19990330)15:5<427::aid-yea362>3.0.co;2-5;
RA   Wolff A.M., Petersen J.G., Nilsson-Tillgren T., Din N.;
RT   "The open reading frame YAL048c affects the secretion of proteinase A in S.
RT   cerevisiae.";
RL   Yeast 15:427-434(1999).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF LYS-18; SER-19;
RP   THR-33; GLU-225; GLU-354; LYS-461; SER-462 AND THR-480, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15479738; DOI=10.1083/jcb.200405100;
RA   Frederick R.L., McCaffery J.M., Cunningham K.W., Okamoto K., Shaw J.M.;
RT   "Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel
RT   pathway.";
RL   J. Cell Biol. 167:87-98(2004).
CC   -!- FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking.
CC       Probably involved in control of anterograde transport of mitochondria
CC       and their subcellular distribution (Probable).
CC       {ECO:0000305|PubMed:15479738}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:15479738, ECO:0000269|PubMed:16407407,
CC       ECO:0000269|PubMed:16823961}; Single-pass type IV membrane protein
CC       {ECO:0000269|PubMed:15479738, ECO:0000269|PubMed:16407407,
CC       ECO:0000269|PubMed:16823961}.
CC   -!- DISRUPTION PHENOTYPE: Collapsed, globular, or grape-like mitochondria.
CC       {ECO:0000269|PubMed:15479738}.
CC   -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00757, ECO:0000305}.
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DR   EMBL; U12980; AAC04983.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06938.1; -; Genomic_DNA.
DR   PIR; S51971; S51971.
DR   RefSeq; NP_009351.1; NM_001178193.1.
DR   AlphaFoldDB; P39722; -.
DR   SMR; P39722; -.
DR   BioGRID; 31779; 358.
DR   ComplexPortal; CPX-3196; ERMES complex.
DR   DIP; DIP-8142N; -.
DR   IntAct; P39722; 18.
DR   MINT; P39722; -.
DR   STRING; 4932.YAL048C; -.
DR   iPTMnet; P39722; -.
DR   MaxQB; P39722; -.
DR   PaxDb; 4932-YAL048C; -.
DR   PeptideAtlas; P39722; -.
DR   EnsemblFungi; YAL048C_mRNA; YAL048C; YAL048C.
DR   GeneID; 851249; -.
DR   KEGG; sce:YAL048C; -.
DR   AGR; SGD:S000000046; -.
DR   SGD; S000000046; GEM1.
DR   VEuPathDB; FungiDB:YAL048C; -.
DR   eggNOG; KOG1707; Eukaryota.
DR   GeneTree; ENSGT00940000173880; -.
DR   HOGENOM; CLU_014255_3_0_1; -.
DR   InParanoid; P39722; -.
DR   OMA; IILRKFH; -.
DR   OrthoDB; 5481412at2759; -.
DR   BioCyc; YEAST:G3O-28855-MONOMER; -.
DR   Reactome; R-SCE-9013419; RHOT2 GTPase cycle.
DR   Reactome; R-SCE-9013425; RHOT1 GTPase cycle.
DR   BioGRID-ORCS; 851249; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P39722; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P39722; Protein.
DR   GO; GO:0032865; C:ERMES complex; IPI:SGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0098799; C:outer mitochondrial membrane protein complex; NAS:ComplexPortal.
DR   GO; GO:0005509; F:calcium ion binding; IDA:SGD.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IMP:SGD.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0015886; P:heme transport; IMP:SGD.
DR   GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IMP:SGD.
DR   GO; GO:0055091; P:phospholipid homeostasis; IGI:SGD.
DR   GO; GO:0010821; P:regulation of mitochondrion organization; IMP:SGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd01892; Miro2; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
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:SF73; MITOCHONDRIAL RHO GTPASE; 1.
DR   PANTHER; PTHR24072; RHO FAMILY GTPASE; 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   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS51423; MIRO; 2.
PE   1: Evidence at protein 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..662
FT                   /note="Mitochondrial Rho GTPase 1"
FT                   /id="PRO_0000202422"
FT   TOPO_DOM        1..634
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        635..655
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        656..662
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          3..185
FT                   /note="Miro 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT   DOMAIN          201..236
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          330..365
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          446..611
FT                   /note="Miro 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00757"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         62..64
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         116..119
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         214
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         216
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         218
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         220
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         225
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
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   BINDING         345
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         347
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         354
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         455..462
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         491..495
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         560..563
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         18
FT                   /note="K->A: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:15479738"
FT   MUTAGEN         19
FT                   /note="S->N: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:15479738"
FT   MUTAGEN         33
FT                   /note="T->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:15479738"
FT   MUTAGEN         225
FT                   /note="E->K: Induces collapsed, globular or grape-like
FT                   mitochondria; when associated with A-354."
FT                   /evidence="ECO:0000269|PubMed:15479738"
FT   MUTAGEN         354
FT                   /note="E->K: Induces collapsed, globular or grape-like
FT                   mitochondria; when associated with A-225."
FT                   /evidence="ECO:0000269|PubMed:15479738"
FT   MUTAGEN         461
FT                   /note="K->A: Induces collapsed, globular or grape-like
FT                   mitochondria."
FT                   /evidence="ECO:0000269|PubMed:15479738"
FT   MUTAGEN         462
FT                   /note="S->N: Induces collapsed, globular or grape-like
FT                   mitochondria."
FT                   /evidence="ECO:0000269|PubMed:15479738"
FT   MUTAGEN         480
FT                   /note="T->A: Induces collapsed, globular or grape-like
FT                   mitochondria."
FT                   /evidence="ECO:0000269|PubMed:15479738"
SQ   SEQUENCE   662 AA;  75150 MW;  A68CDA15D79E5910 CRC64;
     MTKETIRVVI CGDEGVGKSS LIVSLTKAEF IPTIQDVLPP ISIPRDFSSS PTYSPKNTVL
     IDTSDSDLIA LDHELKSADV IWLVYCDHES YDHVSLFWLP HFRSLGLNIP VILCKNKCDS
     ISNVNANAMV VSENSDDDID TKVEDEEFIP ILMEFKEIDT CIKTSAKTQF DLNQAFYLCQ
     RAITHPISPL FDAMVGELKP LAVMALKRIF LLSDLNQDSY LDDNEILGLQ KKCFNKSIDV
     NELNFIKDLL LDISKHDQEY INRKLYVPGK GITKDGFLVL NKIYAERGRH ETTWAILRTF
     HYTDSLCIND KILHPRLVVP DTSSVELSPK GYRFLVDIFL KFDIDNDGGL NNQELHRLFK
     CTPGLPKLWT STNFPFSTVV NNKGCITLQG WLAQWSMTTF LNYSTTTAYL VYFGFQEDAR
     LALQVTKPRK MRRRSGKLYR SNINDRKVFN CFVIGKPCCG KSSLLEAFLG RSFSEEYSPT
     IKPRIAVNSL ELKGGKQYYL ILQELGEQEY AILENKDKLK ECDVICLTYD SSDPESFSYL
     VSLLDKFTHL QDLPLVFVAS KADLDKQQQR CQIQPDELAD ELFVNHPLHI SSRWLSSLNE
     LFIKITEAAL DPGKNTPGLP EETAAKDVDY RQTALIFGST VGFVALCSFT LMKLFKSSKF
     SK
//