GEM1_YEAST
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 03-AUG-2022, entry version 174.
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; 342.
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; P39722; -.
DR PRIDE; P39722; -.
DR EnsemblFungi; YAL048C_mRNA; YAL048C; YAL048C.
DR GeneID; 851249; -.
DR KEGG; sce:YAL048C; -.
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; HVSVTWN; -.
DR BioCyc; YEAST:G3O-28855-MON; -.
DR Reactome; R-SCE-9013419; RHOT2 GTPase cycle.
DR Reactome; R-SCE-9013425; RHOT1 GTPase cycle.
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:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
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; IC: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: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: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; 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; 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
