GTR2_YEASX
ID GTR2_YEASX Reviewed; 341 AA.
AC A0A6A5PVF7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=GTP-binding protein GTR2 {ECO:0000250|UniProtKB:P53290};
GN Name=GTR2 {ECO:0000303|PubMed:28993463};
GN ORFNames=GI527_G0002596 {ECO:0000312|EMBL:KAF1908416.1};
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932 {ECO:0000312|EMBL:KAF1908416.1, ECO:0000312|Proteomes:UP000470054};
RN [1] {ECO:0000312|Proteomes:UP000470054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INSC1005 {ECO:0000312|Proteomes:UP000470054};
RA Fiddes I.T., Church D.M.;
RT "Inscripta technologies.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:28993463};
RX PubMed=28993463; DOI=10.1242/jcs.207910;
RA Varlakhanova N.V., Mihalevic M.J., Bernstein K.A., Ford M.G.J.;
RT "Pib2 and the EGO complex are both required for activation of TORC1.";
RL J. Cell Sci. 130:3878-3890(2017).
CC -!- FUNCTION: GTPase involved in activation of the TORC1 signaling pathway,
CC which promotes growth and represses autophagy in nutrient-rich
CC conditions (PubMed:28993463). Also required for TORC1 inactivation
CC during nitrogen starvation (PubMed:28993463). Required for
CC intracellular sorting of GAP1 out of the endosome (By similarity).
CC Involved in the regulation of microautophagy (By similarity).
CC {ECO:0000250|UniProtKB:P53290, ECO:0000269|PubMed:28993463}.
CC -!- SUBUNIT: Heterodimer; with GTR1 (By similarity). Component of the GSE
CC complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1. Component of the
CC EGO complex, at least composed of GTR2, SLM4 and MEH1 (By similarity).
CC Interacts with GTR1; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P53290}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:28993463};
CC Peripheral membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to rapamycin (TORC1 signaling-
CC inhibitor) (PubMed:28993463). Simultaneous disruption of GTR1 results
CC in abnormal localization of TOR1 and PIB2 to vacuoles and abnormal
CC activation of TORC1 in nitrogen-replete conditions (glutamine or
CC leucine nitrogen source) (PubMed:28993463).
CC {ECO:0000269|PubMed:28993463}.
CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC {ECO:0000305}.
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DR EMBL; JAAEAL010000004; KAF1908416.1; -; Genomic_DNA.
DR SMR; A0A6A5PVF7; -.
DR VEuPathDB; FungiDB:YGR163W; -.
DR OMA; DTQRDIM; -.
DR Proteomes; UP000470054; Chromosome vii.
DR GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR CDD; cd11385; RagC_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006762; Gtr1_RagA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039400; RagC/D.
DR PANTHER; PTHR11259; PTHR11259; 1.
DR Pfam; PF04670; Gtr1_RagA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW GTP-binding; Membrane; Nucleotide-binding; Protein transport; Transport;
KW Vacuole.
FT CHAIN 1..341
FT /note="GTP-binding protein GTR2"
FT /id="PRO_0000456201"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P53290"
SQ SEQUENCE 341 AA; 38600 MW; 0A0D16C81F73184D CRC64;
MSLEATDSKA MVLLMGVRRC GKSSICKVVF HNMQPLDTLY LESTSNPSLE HFSTLIDLAV
MELPGQLNYF EPSYDSERLF KSVGALVYVI DSQDEYINAI TNLAMIIEYA YKVNPSINIE
VLIHKVDGLS EDFKVDAQRD IMQRTGEELL ELGLDGVQVS FYLTSIFDHS IYEAFSRIVQ
KLIPELSFLE NMLDNLIQHS KIEKAFLFDV NSKIYVSTDS NPVDIQMYEV CSEFIDVTID
LFDLYKAPVL RNSQKSSDKD NVINPRNELQ NVSQLANGVI IYLRQMIRGL ALVAIIRPNG
TDMESCLTVA DYNIDIFKKG LEDIWANARA SQAKNSIEDD V