GTR2_YEAST
ID GTR2_YEAST Reviewed; 341 AA.
AC P53290; D6VUU7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=GTP-binding protein GTR2 {ECO:0000303|Ref.1};
GN Name=GTR2 {ECO:0000303|Ref.1}; OrderedLocusNames=YGR163W;
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].
RA Nakashima N.;
RT "Gtr1p and Gtr2p comprise a novel small GTPase subfamily.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP FUNCTION, IDENTIFICATION IN THE EGO COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=15989961; DOI=10.1016/j.molcel.2005.05.020;
RA Dubouloz F., Deloche O., Wanke V., Cameroni E., De Virgilio C.;
RT "The TOR and EGO protein complexes orchestrate microautophagy in yeast.";
RL Mol. Cell 19:15-26(2005).
RN [8]
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 [9]
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 [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLN-66.
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 11-341 IN COMPLEX WITH GTP AND
RP GTR1, AND INTERACTION WITH GTR1.
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:15989961, PubMed:32801125). Also
CC required for TORC1 inactivation during nitrogen starvation (By
CC similarity). Required for intracellular sorting of GAP1 out of the
CC endosome (PubMed:16732272). Involved in the regulation of
CC microautophagy (PubMed:15989961). {ECO:0000250|UniProtKB:A0A6A5PVF7,
CC ECO:0000269|PubMed:15989961, ECO:0000269|PubMed:16732272,
CC ECO:0000269|PubMed:26510498, ECO:0000269|PubMed:32801125}.
CC -!- SUBUNIT: Heterodimer; with GTR1 (PubMed:21816923). Component of the GSE
CC complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1 (PubMed:16732272).
CC Component of the EGO complex, at least composed of GTR2, SLM4 and MEH1
CC (PubMed:15989961). Interacts with GTR1; the interaction is direct
CC (PubMed:21816923). {ECO:0000269|PubMed:15989961,
CC ECO:0000269|PubMed:16732272, ECO:0000269|PubMed:21816923}.
CC -!- INTERACTION:
CC P53290; Q00582: GTR1; NbExp=4; IntAct=EBI-7962, EBI-7954;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15989961}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Abnormal punctate localization of TOR1
CC (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). {ECO:0000269|PubMed:26510498,
CC ECO:0000269|PubMed:32801125}.
CC -!- MISCELLANEOUS: Present with 2610 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; AB015239; BAA28781.1; -; Genomic_DNA.
DR EMBL; Z72948; CAA97187.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08258.1; -; Genomic_DNA.
DR PIR; S64474; S64474.
DR RefSeq; NP_011679.3; NM_001181292.3.
DR PDB; 3R7W; X-ray; 2.77 A; B/D=11-341.
DR PDB; 4ARZ; X-ray; 3.10 A; B=1-341.
DR PDB; 6JWP; X-ray; 3.20 A; B/G=1-341.
DR PDBsum; 3R7W; -.
DR PDBsum; 4ARZ; -.
DR PDBsum; 6JWP; -.
DR AlphaFoldDB; P53290; -.
DR SMR; P53290; -.
DR BioGRID; 33415; 221.
DR ComplexPortal; CPX-3172; EGO complex.
DR ComplexPortal; CPX-3233; GSE complex.
DR DIP; DIP-4521N; -.
DR IntAct; P53290; 31.
DR MINT; P53290; -.
DR STRING; 4932.YGR163W; -.
DR iPTMnet; P53290; -.
DR MaxQB; P53290; -.
DR PaxDb; P53290; -.
DR PRIDE; P53290; -.
DR EnsemblFungi; YGR163W_mRNA; YGR163W; YGR163W.
DR GeneID; 853072; -.
DR KEGG; sce:YGR163W; -.
DR SGD; S000003395; GTR2.
DR VEuPathDB; FungiDB:YGR163W; -.
DR eggNOG; KOG3887; Eukaryota.
DR GeneTree; ENSGT00950000183031; -.
DR HOGENOM; CLU_047421_2_0_1; -.
DR InParanoid; P53290; -.
DR OMA; DTQRDIM; -.
DR BioCyc; YEAST:G3O-30862-MON; -.
DR Reactome; R-SCE-165159; MTOR signalling.
DR Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR PRO; PR:P53290; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53290; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
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: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; IMP:SGD.
DR GO; GO:0010507; P:negative regulation of autophagy; IGI:SGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:SGD.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IBA:GO_Central.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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 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 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Membrane; Nucleotide-binding; Protein transport;
KW Reference proteome; Transport; Vacuole.
FT CHAIN 1..341
FT /note="GTP-binding protein GTR2"
FT /id="PRO_0000122487"
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:0000269|PubMed:21816923,
FT ECO:0007744|PDB:3R7W"
FT MUTAGEN 66
FT /note="Q->L: Sensitive to high hydrostatic pressure."
FT /evidence="ECO:0000269|PubMed:32801125"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3R7W"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:4ARZ"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6JWP"
FT HELIX 132..147
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 199..212
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 225..242
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6JWP"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:3R7W"
FT STRAND 287..296
FT /evidence="ECO:0007829|PDB:3R7W"
FT HELIX 303..322
FT /evidence="ECO:0007829|PDB:3R7W"
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
