GTR1_SCHPO
ID GTR1_SCHPO Reviewed; 308 AA.
AC O74824;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=GTP-binding protein gtr1;
GN Name=gtr1; ORFNames=SPBC337.13c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: GTPase involved in activation of the TORC1 signaling pathway,
CC which promotes growth and represses autophagy in nutrient-rich
CC conditions (By similarity). Also required for TORC1 inactivation during
CC nitrogen starvation (By similarity). {ECO:0000250|UniProtKB:A0A6A5PR12,
CC ECO:0000250|UniProtKB:Q00582}.
CC -!- SUBUNIT: Component of the GSE complex. {ECO:0000250|UniProtKB:Q00582}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane
CC {ECO:0000250|UniProtKB:A0A6A5PR12}; Peripheral membrane protein
CC {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA21283.1; -; Genomic_DNA.
DR PIR; T40266; T40266.
DR RefSeq; NP_595414.1; NM_001021321.2.
DR AlphaFoldDB; O74824; -.
DR SMR; O74824; -.
DR BioGRID; 277470; 22.
DR IntAct; O74824; 1.
DR STRING; 4896.SPBC337.13c.1; -.
DR MaxQB; O74824; -.
DR PaxDb; O74824; -.
DR EnsemblFungi; SPBC337.13c.1; SPBC337.13c.1:pep; SPBC337.13c.
DR GeneID; 2540954; -.
DR KEGG; spo:SPBC337.13c; -.
DR PomBase; SPBC337.13c; gtr1.
DR VEuPathDB; FungiDB:SPBC337.13c; -.
DR eggNOG; KOG3886; Eukaryota.
DR HOGENOM; CLU_044099_0_0_1; -.
DR InParanoid; O74824; -.
DR OMA; LIPNMQD; -.
DR PhylomeDB; O74824; -.
DR Reactome; R-SPO-165159; MTOR signalling.
DR Reactome; R-SPO-9639288; Amino acids regulate mTORC1.
DR PRO; PR:O74824; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IPI:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISO:PomBase.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; EXP:PomBase.
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:0110045; P:negative regulation of cell cycle switching, mitotic to meiotic cell cycle; EXP:PomBase.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IBA:GO_Central.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; EXP:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
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 Cytoplasm; GTP-binding; Membrane; Nucleotide-binding; Nucleus;
KW Phosphate transport; Protein transport; Reference proteome; Transport;
KW Vacuole.
FT CHAIN 1..308
FT /note="GTP-binding protein gtr1"
FT /id="PRO_0000372337"
FT BINDING 11..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q00582"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q00582"
SQ SEQUENCE 308 AA; 35010 MW; 2399B9F3D1C05771 CRC64;
MRKKVLLMGR SGSGKSSMRS IVFSNYVAKD TRRLGATIDI EHSHVRFLGN LVLNLWDCGG
QEAFMENYLS AQRDHIFRNV QVLIYVFDVE SREFERDLVT FRNCLEATVA NSPQARVFCL
IHKMDLVQED LRDLVFEERK AILLETSKDL ETTCLATSIW DETLFKAWSA IVYTLIPNTP
TLESHLREFA KAAEAAEVIL FERTTFLVIS SYSSESNPAT DAHRFEKISN IVKQFKLSCS
KMQAQFTTFE LRGGNFSAFI VPYTEDTYIL VVIADPEIES AVTLMNIQSA RRFIEASKSA
SDGIQLQP
