GTR1_YEAST
ID GTR1_YEAST Reviewed; 310 AA.
AC Q00582; D6W0G3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=GTP-binding protein GTR1 {ECO:0000305};
GN Name=GTR1; OrderedLocusNames=YML121W; ORFNames=YM7056.05;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=1620108; DOI=10.1128/mcb.12.7.2958-2966.1992;
RA Bun-Ya M., Harashima S., Oshima Y.;
RT "Putative GTP-binding protein, Gtr1, associated with the function of the
RT Pho84 inorganic phosphate transporter in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:2958-2966(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP GSE COMPLEX.
RX PubMed=16732272; DOI=10.1038/ncb1419;
RA Gao M., Kaiser C.A.;
RT "A conserved GTPase-containing complex is required for intracellular
RT sorting of the general amino-acid permease in yeast.";
RL Nat. Cell Biol. 8:657-667(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26510498; DOI=10.1091/mbc.e15-08-0581;
RA Kim A., Cunningham K.W.;
RT "A LAPF/phafin1-like protein regulates TORC1 and lysosomal membrane
RT permeabilization in response to endoplasmic reticulum membrane stress.";
RL Mol. Biol. Cell 26:4631-4645(2015).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=28483912; DOI=10.1128/mcb.00075-17;
RA Tanigawa M., Maeda T.;
RT "An In Vitro TORC1 Kinase Assay That Recapitulates the Gtr-Independent
RT Glutamine-Responsive TORC1 Activation Mechanism on Yeast Vacuoles.";
RL Mol. Cell. Biol. 37:e00075-e00075(2017).
RN [9]
RP INTERACTION WITH TOR1, AND DISRUPTION PHENOTYPE.
RX PubMed=29698392; DOI=10.1371/journal.pgen.1007334;
RA Ukai H., Araki Y., Kira S., Oikawa Y., May A.I., Noda T.;
RT "Gtr/Ego-independent TORC1 activation is achieved through a glutamine-
RT sensitive interaction with Pib2 on the vacuolar membrane.";
RL PLoS Genet. 14:e1007334-e1007334(2018).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-20.
RX PubMed=32801125; DOI=10.1242/jcs.245555;
RA Uemura S., Mochizuki T., Amemiya K., Kurosaka G., Yazawa M., Nakamoto K.,
RA Ishikawa Y., Izawa S., Abe F.;
RT "Amino acid homeostatic control by TORC1 in Saccharomyces cerevisiae under
RT high hydrostatic pressure.";
RL J. Cell Sci. 133:jcs245555-jcs245555(2020).
RN [11] {ECO:0007744|PDB:3R7W}
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 8-310 IN COMPLEX WITH GTP AND
RP GTR2, AND INTERACTION WITH GTR2.
RX PubMed=21816923; DOI=10.1101/gad.16968011;
RA Gong R., Li L., Liu Y., Wang P., Yang H., Wang L., Cheng J., Guan K.L.,
RA Xu Y.;
RT "Crystal structure of the Gtr1p-Gtr2p complex reveals new insights into the
RT amino acid-induced TORC1 activation.";
RL Genes Dev. 25:1668-1673(2011).
CC -!- FUNCTION: GTPase involved in activation of the TORC1 signaling pathway,
CC which promotes growth and represses autophagy in nutrient-rich
CC conditions (PubMed:26510498, PubMed:32801125). Also required for TORC1
CC inactivation during nitrogen starvation (By similarity). Required for
CC intracellular sorting of GAP1 out of the endosome (PubMed:16732272).
CC Functionally associated with the inorganic phosphate transporter PHO84,
CC and may be involved in regulating its function or localization
CC (PubMed:1620108). {ECO:0000250|UniProtKB:A0A6A5PR12,
CC ECO:0000269|PubMed:1620108, ECO:0000269|PubMed:16732272,
CC ECO:0000269|PubMed:26510498, ECO:0000269|PubMed:32801125}.
CC -!- SUBUNIT: Heterodimer; with GTR2 (PubMed:21816923). Component of the GSE
CC complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1 (PubMed:16732272).
CC Interacts with GTR2; the interaction is direct (PubMed:21816923).
CC Interacts with TOR1 (PubMed:29698392). {ECO:0000269|PubMed:16732272,
CC ECO:0000269|PubMed:21816923, ECO:0000269|PubMed:29698392}.
CC -!- INTERACTION:
CC Q00582; Q00582: GTR1; NbExp=4; IntAct=EBI-7954, EBI-7954;
CC Q00582; P53290: GTR2; NbExp=4; IntAct=EBI-7954, EBI-7962;
CC Q00582; Q02205: MEH1; NbExp=3; IntAct=EBI-7954, EBI-27062;
CC Q00582; P38247: SLM4; NbExp=5; IntAct=EBI-7954, EBI-21507;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane
CC {ECO:0000250|UniProtKB:A0A6A5PR12}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Decreases and delays activation of TORC1
CC signaling in nitrogen-replete conditions (glutamine nitrogen source)
CC (PubMed:29698392). Abnormal punctate localization of PIB2 and TOR1 in
CC nitrogen-replete conditions (glutamine nitrogen source)
CC (PubMed:29698392, PubMed:32801125). Increases cellular levels of
CC glutamine and alanine during high hydrostatic pressure (mechanical
CC stress) (PubMed:32801125). Sensitive to high hydrostatic pressure
CC (PubMed:32801125). Resistance to tunicamycin (endoplasmic reticulum
CC stressor) administered together with FK506 (calcineurin inhibitor)
CC (PubMed:26510498). Normal localization of KOG1 and TOR1 to the vacuolar
CC membrane (PubMed:28483912). Simultaneous disruption of PIB2 results in
CC TOR1 mislocalization and loss of TORC1 activity and viability
CC (PubMed:29698392). {ECO:0000269|PubMed:26510498,
CC ECO:0000269|PubMed:28483912, ECO:0000269|PubMed:29698392,
CC ECO:0000269|PubMed:32801125}.
CC -!- MISCELLANEOUS: Present with 907 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC {ECO:0000305}.
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DR EMBL; D10018; BAA00907.1; -; Genomic_DNA.
DR EMBL; Z49218; CAA89159.1; -; Genomic_DNA.
DR EMBL; AY692917; AAT92936.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09777.1; -; Genomic_DNA.
DR PIR; S31303; S31303.
DR RefSeq; NP_013585.1; NM_001182484.1.
DR PDB; 3R7W; X-ray; 2.77 A; A/C=8-310.
DR PDB; 4ARZ; X-ray; 3.10 A; A=1-310.
DR PDB; 6JWP; X-ray; 3.20 A; A/F=1-310.
DR PDBsum; 3R7W; -.
DR PDBsum; 4ARZ; -.
DR PDBsum; 6JWP; -.
DR AlphaFoldDB; Q00582; -.
DR SMR; Q00582; -.
DR BioGRID; 35083; 421.
DR ComplexPortal; CPX-3172; EGO complex.
DR ComplexPortal; CPX-3233; GSE complex.
DR DIP; DIP-1358N; -.
DR IntAct; Q00582; 17.
DR MINT; Q00582; -.
DR STRING; 4932.YML121W; -.
DR MaxQB; Q00582; -.
DR PaxDb; Q00582; -.
DR PRIDE; Q00582; -.
DR EnsemblFungi; YML121W_mRNA; YML121W; YML121W.
DR GeneID; 854918; -.
DR KEGG; sce:YML121W; -.
DR SGD; S000004590; GTR1.
DR VEuPathDB; FungiDB:YML121W; -.
DR eggNOG; KOG3886; Eukaryota.
DR GeneTree; ENSGT00950000183031; -.
DR HOGENOM; CLU_044099_0_0_1; -.
DR InParanoid; Q00582; -.
DR OMA; LIPNMQD; -.
DR BioCyc; YEAST:G3O-32701-MON; -.
DR Reactome; R-SCE-165159; MTOR signalling.
DR Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR PRO; PR:Q00582; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q00582; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IPI:SGD.
DR GO; GO:0005770; C:late endosome; IDA:ComplexPortal.
DR GO; GO:0031902; C:late endosome membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0071986; C:Ragulator complex; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; IDA:ComplexPortal.
DR GO; GO:0016237; P:lysosomal microautophagy; IC:ComplexPortal.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:SGD.
DR GO; GO:0006817; P:phosphate ion transport; IMP:SGD.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IBA:GO_Central.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IDA:SGD.
DR GO; GO:1903778; P:protein localization to vacuolar membrane; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IMP:SGD.
DR CDD; cd11384; RagA_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006762; Gtr1_RagA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039397; RagA/B.
DR PANTHER; PTHR11259; PTHR11259; 1.
DR Pfam; PF04670; Gtr1_RagA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Membrane; Nucleotide-binding;
KW Phosphate transport; Protein transport; Reference proteome; Transport;
KW Vacuole.
FT CHAIN 1..310
FT /note="GTP-binding protein GTR1"
FT /id="PRO_0000122486"
FT BINDING 15..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21816923,
FT ECO:0007744|PDB:3R7W"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:21816923,
FT ECO:0007744|PDB:3R7W"
FT MUTAGEN 20
FT /note="S->L: Sensitive to high hydrostatic pressure."
FT /evidence="ECO:0000269|PubMed:32801125"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:6JWP"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:3R7W"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:3R7W"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 98..115
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 133..152
FT /evidence="ECO:0007829|PDB:3R7W"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:3R7W"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:3R7W"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:3R7W"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:3R7W"
SQ SEQUENCE 310 AA; 35847 MW; B79CE7FE7AD2FDBE CRC64;
MSSNNRKKLL LMGRSGSGKS SMRSIIFSNY SAFDTRRLGA TIDVEHSHLR FLGNMTLNLW
DCGGQDVFME NYFTKQKDHI FQMVQVLIHV FDVESTEVLK DIEIFAKALK QLRKYSPDAK
IFVLLHKMDL VQLDKREELF QIMMKNLSET SSEFGFPNLI GFPTSIWDES LYKAWSQIVC
SLIPNMSNHQ SNLKKFKEIM NALEIILFER TTFLVICSSN GENSNENHDS SDNNNVLLDP
KRFEKISNIM KNFKQSCTKL KSGFKTLILN NNIYVSELSS NMVCFIVLKD MNIPQELVLE
NIKKAKEFFQ
