位置:首页 > 蛋白库 > GTR1_YEASX
GTR1_YEASX
ID   GTR1_YEASX              Reviewed;         310 AA.
AC   A0A6A5PR12;
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 GTR1 {ECO:0000250|UniProtKB:Q00582};
GN   Name=GTR1 {ECO:0000305|PubMed:28993463};
GN   ORFNames=GI527_G0004296 {ECO:0000312|EMBL:KAF1903594.1};
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932 {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       Functionally associated with the inorganic phosphate transporter PHO84,
CC       and may be involved in regulating its function or localization (By
CC       similarity). {ECO:0000250|UniProtKB:Q00582,
CC       ECO:0000269|PubMed:28993463}.
CC   -!- SUBUNIT: Heterodimer; with GTR2 (By similarity). Component of the GSE
CC       complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1 (By similarity).
CC       Interacts with GTR2; the interaction is direct (By similarity).
CC       Interacts with TOR1 (By similarity). {ECO:0000250|UniProtKB:Q00582}.
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 GTR2 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JAAEAL010000012; KAF1903594.1; -; Genomic_DNA.
DR   SMR; A0A6A5PR12; -.
DR   VEuPathDB; FungiDB:YML121W; -.
DR   Proteomes; UP000470054; Chromosome xiii.
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; 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   3: Inferred from homology;
KW   GTP-binding; Membrane; Nucleotide-binding; Phosphate transport;
KW   Protein transport; Transport; Vacuole.
FT   CHAIN           1..310
FT                   /note="GTP-binding protein GTR1"
FT                   /id="PRO_0000456200"
FT   BINDING         15..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q00582"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q00582"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025