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Protein

Mitochondrial Rho GTPase 1

Gene

GEM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (Probable).1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTP 1Curated
Nucleotide bindingi62 – 643GTP 1Sequence Analysis
Nucleotide bindingi116 – 1194GTP 1Sequence Analysis
Calcium bindingi214 – 225121CuratedAdd
BLAST
Calcium bindingi343 – 354122CuratedAdd
BLAST
Nucleotide bindingi455 – 4628GTP 2Curated
Nucleotide bindingi491 – 4955GTP 2Sequence Analysis
Nucleotide bindingi560 – 5634GTP 2Sequence Analysis

GO - Molecular functioni

  • calcium ion binding Source: SGD
  • GTPase activity Source: SGD
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • cellular homeostasis Source: InterPro
  • metabolic process Source: GOC
  • mitochondrion-ER tethering Source: SGD
  • mitochondrion inheritance Source: SGD
  • phospholipid homeostasis Source: SGD
  • regulation of mitochondrion organization Source: SGD
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, GTP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-28855-MONOMER.
ReactomeiREACT_347191. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial Rho GTPase 1 (EC:3.6.5.-)
Alternative name(s):
GTPase EF-hand protein of mitochondria 1
Gene namesi
Name:GEM1
Ordered Locus Names:YAL048C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome I

Organism-specific databases

CYGDiYAL048c.
EuPathDBiFungiDB:YAL048C.
SGDiS000000046. GEM1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 634634Mitochondrial intermembraneSequence AnalysisAdd
BLAST
Transmembranei635 – 65521Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini656 – 6627CytoplasmicSequence Analysis

GO - Cellular componenti

  • ERMES complex Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Disruption phenotypei

Collapsed, globular, or grape-like mitochondria.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181K → A: Loss of function. 1 Publication
Mutagenesisi19 – 191S → N: Loss of function. 1 Publication
Mutagenesisi33 – 331T → A: No effect. 1 Publication
Mutagenesisi225 – 2251E → K: Induces collapsed, globular or grape-like mitochondria; when associated with A-354. 1 Publication
Mutagenesisi354 – 3541E → K: Induces collapsed, globular or grape-like mitochondria; when associated with A-225. 1 Publication
Mutagenesisi461 – 4611K → A: Induces collapsed, globular or grape-like mitochondria. 1 Publication
Mutagenesisi462 – 4621S → N: Induces collapsed, globular or grape-like mitochondria. 1 Publication
Mutagenesisi480 – 4801T → A: Induces collapsed, globular or grape-like mitochondria. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 662662Mitochondrial Rho GTPase 1PRO_0000202422Add
BLAST

Proteomic databases

MaxQBiP39722.
PaxDbiP39722.

Expressioni

Gene expression databases

GenevestigatoriP39722.

Interactioni

Protein-protein interaction databases

BioGridi31779. 122 interactions.
DIPiDIP-8142N.
IntActiP39722. 16 interactions.
STRINGi4932.YAL048C.

Structurei

3D structure databases

ProteinModelPortaliP39722.
SMRiP39722. Positions 3-186, 197-612.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 140140Miro 1Add
BLAST
Domaini201 – 23636EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini330 – 36536EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini442 – 662221Miro 2Add
BLAST

Sequence similaritiesi

Belongs to the mitochondrial Rho GTPase family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 2 Miro domains.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00390000014374.
HOGENOMiHOG000215553.
InParanoidiP39722.
KOiK07870.
OMAiSPAEFCY.
OrthoDBiEOG73545F.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR013566. EF_hand_assoc_1.
IPR013567. EF_hand_assoc_2.
IPR002048. EF_hand_dom.
IPR020860. MIRO.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR021181. Rho_GTPase_Mt.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF08355. EF_assoc_1. 1 hit.
PF08356. EF_assoc_2. 1 hit.
PF08477. Miro. 2 hits.
[Graphical view]
PIRSFiPIRSF037488. Mt_Rho_GTPase. 1 hit.
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS50222. EF_HAND_2. 2 hits.
PS51423. MIRO. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39722-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKETIRVVI CGDEGVGKSS LIVSLTKAEF IPTIQDVLPP ISIPRDFSSS
60 70 80 90 100
PTYSPKNTVL IDTSDSDLIA LDHELKSADV IWLVYCDHES YDHVSLFWLP
110 120 130 140 150
HFRSLGLNIP VILCKNKCDS ISNVNANAMV VSENSDDDID TKVEDEEFIP
160 170 180 190 200
ILMEFKEIDT CIKTSAKTQF DLNQAFYLCQ RAITHPISPL FDAMVGELKP
210 220 230 240 250
LAVMALKRIF LLSDLNQDSY LDDNEILGLQ KKCFNKSIDV NELNFIKDLL
260 270 280 290 300
LDISKHDQEY INRKLYVPGK GITKDGFLVL NKIYAERGRH ETTWAILRTF
310 320 330 340 350
HYTDSLCIND KILHPRLVVP DTSSVELSPK GYRFLVDIFL KFDIDNDGGL
360 370 380 390 400
NNQELHRLFK CTPGLPKLWT STNFPFSTVV NNKGCITLQG WLAQWSMTTF
410 420 430 440 450
LNYSTTTAYL VYFGFQEDAR LALQVTKPRK MRRRSGKLYR SNINDRKVFN
460 470 480 490 500
CFVIGKPCCG KSSLLEAFLG RSFSEEYSPT IKPRIAVNSL ELKGGKQYYL
510 520 530 540 550
ILQELGEQEY AILENKDKLK ECDVICLTYD SSDPESFSYL VSLLDKFTHL
560 570 580 590 600
QDLPLVFVAS KADLDKQQQR CQIQPDELAD ELFVNHPLHI SSRWLSSLNE
610 620 630 640 650
LFIKITEAAL DPGKNTPGLP EETAAKDVDY RQTALIFGST VGFVALCSFT
660
LMKLFKSSKF SK
Length:662
Mass (Da):75,150
Last modified:February 1, 1995 - v1
Checksum:iA68CDA15D79E5910
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12980 Genomic DNA. Translation: AAC04983.1.
BK006935 Genomic DNA. Translation: DAA06938.1.
PIRiS51971.
RefSeqiNP_009351.1. NM_001178193.1.

Genome annotation databases

EnsemblFungiiYAL048C; YAL048C; YAL048C.
GeneIDi851249.
KEGGisce:YAL048C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12980 Genomic DNA. Translation: AAC04983.1.
BK006935 Genomic DNA. Translation: DAA06938.1.
PIRiS51971.
RefSeqiNP_009351.1. NM_001178193.1.

3D structure databases

ProteinModelPortaliP39722.
SMRiP39722. Positions 3-186, 197-612.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31779. 122 interactions.
DIPiDIP-8142N.
IntActiP39722. 16 interactions.
STRINGi4932.YAL048C.

Proteomic databases

MaxQBiP39722.
PaxDbiP39722.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL048C; YAL048C; YAL048C.
GeneIDi851249.
KEGGisce:YAL048C.

Organism-specific databases

CYGDiYAL048c.
EuPathDBiFungiDB:YAL048C.
SGDiS000000046. GEM1.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00390000014374.
HOGENOMiHOG000215553.
InParanoidiP39722.
KOiK07870.
OMAiSPAEFCY.
OrthoDBiEOG73545F.

Enzyme and pathway databases

BioCyciYEAST:G3O-28855-MONOMER.
ReactomeiREACT_347191. Rho GTPase cycle.

Miscellaneous databases

NextBioi968192.
PROiP39722.

Gene expression databases

GenevestigatoriP39722.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR013566. EF_hand_assoc_1.
IPR013567. EF_hand_assoc_2.
IPR002048. EF_hand_dom.
IPR020860. MIRO.
IPR013684. MIRO-like.
IPR027417. P-loop_NTPase.
IPR021181. Rho_GTPase_Mt.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF08355. EF_assoc_1. 1 hit.
PF08356. EF_assoc_2. 1 hit.
PF08477. Miro. 2 hits.
[Graphical view]
PIRSFiPIRSF037488. Mt_Rho_GTPase. 1 hit.
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS50222. EF_HAND_2. 2 hits.
PS51423. MIRO. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins."
    Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N., Schoenfisch B., Guiard B., Pfanner N., Meisinger C.
    Mol. Biol. Cell 17:1436-1450(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "The open reading frame YAL048c affects the secretion of proteinase A in S. cerevisiae."
    Wolff A.M., Petersen J.G., Nilsson-Tillgren T., Din N.
    Yeast 15:427-434(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY FUNCTION.
  5. "Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway."
    Frederick R.L., McCaffery J.M., Cunningham K.W., Okamoto K., Shaw J.M.
    J. Cell Biol. 167:87-98(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF LYS-18; SER-19; THR-33; GLU-225; GLU-354; LYS-461; SER-462 AND THR-480, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiGEM1_YEAST
AccessioniPrimary (citable) accession number: P39722
Secondary accession number(s): D6VPG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 29, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome I
    Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.