ID RRAGD_HUMAN Reviewed; 400 AA. AC Q9NQL2; A8K184; Q7L8F9; Q9NPG0; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 03-AUG-2022, entry version 149. DE RecName: Full=Ras-related GTP-binding protein D; DE Short=Rag D; DE Short=RagD; DE EC=3.6.5.- {ECO:0000305|PubMed:24095279}; GN Name=RRAGD {ECO:0000312|HGNC:HGNC:19903}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG32663.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RRAGA AND RRAGB, RP SUBCELLULAR LOCATION, AND GTP-BINDING. RX PubMed=11073942; DOI=10.1074/jbc.m004389200; RA Sekiguchi T., Hirose E., Nakashima N., Ii M., Nishimoto T.; RT "Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag RT A and Rag B."; RL J. Biol. Chem. 276:7246-7257(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] {ECO:0000305, ECO:0000312|EMBL:AL138717} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] {ECO:0000312|EMBL:CAB70775.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-49 (ISOFORM 1). RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] {ECO:0000305, ECO:0000312|EMBL:AAH03088.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-400 (ISOFORM 1). RC TISSUE=Lung {ECO:0000312|EMBL:AAH03088.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] {ECO:0000305} RP INTERACTION WITH NOL8 AND RRAGA. RX PubMed=14660641; DOI=10.1074/jbc.m305935200; RA Sekiguchi T., Todaka Y., Wang Y., Hirose E., Nakashima N., Nishimoto T.; RT "A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG RT A/C/D."; RL J. Biol. Chem. 279:8343-8350(2004). RN [8] RP INTERACTION WITH RPTOR, AND MUTAGENESIS OF SER-76 AND GLN-121. RX PubMed=18497260; DOI=10.1126/science.1157535; RA Sancak Y., Peterson T.R., Shaul Y.D., Lindquist R.A., Thoreen C.C., RA Bar-Peled L., Sabatini D.M.; RT "The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1."; RL Science 320:1496-1501(2008). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=20381137; DOI=10.1016/j.cell.2010.02.024; RA Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.; RT "Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is RT necessary for its activation by amino acids."; RL Cell 141:290-303(2010). RN [10] RP INTERACTION WITH SH3BP4. RX PubMed=22575674; DOI=10.1016/j.molcel.2012.04.007; RA Kim Y.M., Stone M., Hwang T.H., Kim Y.G., Dunlevy J.R., Griffin T.J., RA Kim D.H.; RT "SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1 RT signaling."; RL Mol. Cell 46:833-846(2012). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=24095279; DOI=10.1016/j.molcel.2013.09.016; RA Tsun Z.Y., Bar-Peled L., Chantranupong L., Zoncu R., Wang T., Kim C., RA Spooner E., Sabatini D.M.; RT "The folliculin tumor suppressor is a GAP for the RagC/D GTPases that RT signal amino acid levels to mTORC1."; RL Mol. Cell 52:495-505(2013). RN [12] RP INTERACTION WITH SESN1; SESN2 AND SESN3. RX PubMed=25259925; DOI=10.1016/j.cell.2014.08.038; RA Peng M., Yin N., Li M.O.; RT "Sestrins function as guanine nucleotide dissociation inhibitors for Rag RT GTPases to control mTORC1 signaling."; RL Cell 159:122-133(2014). RN [13] RP SUBUNIT. RX PubMed=25561175; DOI=10.1038/nature14107; RA Rebsamen M., Pochini L., Stasyk T., de Araujo M.E., Galluccio M., RA Kandasamy R.K., Snijder B., Fauster A., Rudashevskaya E.L., Bruckner M., RA Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W., Heinz L.X., RA Kraft C., Bennett K.L., Indiveri C., Huber L.A., Superti-Furga G.; RT "SLC38A9 is a component of the lysosomal amino acid sensing machinery that RT controls mTORC1."; RL Nature 519:477-481(2015). RN [14] RP SUBUNIT. RX PubMed=25567906; DOI=10.1126/science.1257132; RA Wang S., Tsun Z.Y., Wolfson R.L., Shen K., Wyant G.A., Plovanich M.E., RA Yuan E.D., Jones T.D., Chantranupong L., Comb W., Wang T., Bar-Peled L., RA Zoncu R., Straub C., Kim C., Park J., Sabatini B.L., Sabatini D.M.; RT "Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine RT sufficiency to mTORC1."; RL Science 347:188-194(2015). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 60-239 IN COMPLEX WITH GTP ANALOG. RG Structural genomics consortium (SGC); RT "Crystal structure of human Ras-related GTP-binding D."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Guanine nucleotide-binding protein that plays a crucial role CC in the cellular response to amino acid availability through regulation CC of the mTORC1 signaling cascade (PubMed:20381137, PubMed:24095279). CC Forms heterodimeric Rag complexes with RRAGA or RRAGB and cycles CC between an inactive GTP-bound and an active GDP-bound form CC (PubMed:24095279). In its active form participates in the CC relocalization of mTORC1 to the lysosomes and its subsequent activation CC by the GTPase RHEB (PubMed:20381137, PubMed:24095279). This is a CC crucial step in the activation of the TOR signaling cascade by amino CC acids (PubMed:20381137, PubMed:24095279). {ECO:0000269|PubMed:20381137, CC ECO:0000269|PubMed:24095279}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000305|PubMed:24095279}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000305|PubMed:24095279}; CC -!- ACTIVITY REGULATION: In high-amino acid conditions, activated by GTPase CC activating protein (GAP) FLCN that stimulates RRAGD GTPase activity to CC turn it into its active GDP-bound form. {ECO:0000269|PubMed:24095279}. CC -!- SUBUNIT: Forms a heterodimer with RRAGA in a sequence-independent CC manner and RRAGB (PubMed:11073942, PubMed:14660641). Heterodimerization CC stabilizes RRAG proteins (PubMed:11073942, PubMed:14660641, CC PubMed:25561175, PubMed:25567906). In complex with RRAGB, interacts CC with RPTOR; this interaction is particularly efficient with GTP-loaded CC RRAGB and GDP-loaded RRAGC (PubMed:18497260). Component of the CC lysosomal folliculin complex (LFC), composed of FLCN, FNIP1 (or FNIP2), CC RRAGA/RagA or RRAGB/RagB GDP-bound, RRAGC/RagC or RRAGD/RagD GTP-bound, CC and Ragulator (By similarity). Interacts with NOL8 (PubMed:14660641). CC Interacts with SH3BP4; the interaction with this negative regulator is CC most probably direct, preferentially occurs with the inactive GDP-bound CC form of RRAGD and is negatively regulated by amino acids CC (PubMed:22575674). The Rag heterodimer interacts with SLC38A9; the CC probable amino acid sensor (PubMed:25561175, PubMed:25567906). CC Interacts with SESN1, SESN2 and SESN3 (PubMed:25259925). The GDP-bound CC form interacts with TFE3 (By similarity). CC {ECO:0000250|UniProtKB:Q7TT45, ECO:0000250|UniProtKB:Q9HB90, CC ECO:0000269|PubMed:11073942, ECO:0000269|PubMed:14660641, CC ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:22575674, CC ECO:0000269|PubMed:25259925, ECO:0000269|PubMed:25561175, CC ECO:0000269|PubMed:25567906}. CC -!- INTERACTION: CC Q9NQL2; Q9P2J5: LARS1; NbExp=13; IntAct=EBI-992949, EBI-356077; CC Q9NQL2; Q7L523: RRAGA; NbExp=9; IntAct=EBI-992949, EBI-752376; CC Q9NQL2; Q5VZM2: RRAGB; NbExp=7; IntAct=EBI-992949, EBI-993049; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11073942}. Nucleus CC {ECO:0000269|PubMed:11073942}. Lysosome {ECO:0000269|PubMed:20381137}. CC Note=Predominantly cytoplasmic. May shuttle between the cytoplasm and CC nucleus, depending on the bound nucleotide state of associated RRAGA CC (PubMed:11073942). {ECO:0000269|PubMed:11073942}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000269|PubMed:11073942}; CC IsoId=Q9NQL2-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:14574404}; CC IsoId=Q9NQL2-2; Sequence=VSP_052078; CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH03088.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AF272036; AAG32663.1; -; mRNA. DR EMBL; AK289799; BAF82488.1; -; mRNA. DR EMBL; AL138717; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW48554.1; -; Genomic_DNA. DR EMBL; AL137502; CAB70775.2; -; mRNA. DR EMBL; BC003088; AAH03088.1; ALT_INIT; mRNA. DR CCDS; CCDS5022.1; -. [Q9NQL2-1] DR PIR; T46254; T46254. DR RefSeq; NP_067067.1; NM_021244.4. [Q9NQL2-1] DR PDB; 2Q3F; X-ray; 2.10 A; A/B=60-239. DR PDBsum; 2Q3F; -. DR AlphaFoldDB; Q9NQL2; -. DR SMR; Q9NQL2; -. DR BioGRID; 121848; 33. DR IntAct; Q9NQL2; 11. DR STRING; 9606.ENSP00000358423; -. DR GlyGen; Q9NQL2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NQL2; -. DR PhosphoSitePlus; Q9NQL2; -. DR BioMuta; RRAGD; -. DR DMDM; 74752904; -. DR EPD; Q9NQL2; -. DR jPOST; Q9NQL2; -. DR MassIVE; Q9NQL2; -. DR MaxQB; Q9NQL2; -. DR PaxDb; Q9NQL2; -. DR PeptideAtlas; Q9NQL2; -. DR PRIDE; Q9NQL2; -. DR ProteomicsDB; 82161; -. [Q9NQL2-1] DR ProteomicsDB; 82162; -. [Q9NQL2-2] DR Antibodypedia; 31866; 134 antibodies from 27 providers. DR DNASU; 58528; -. DR Ensembl; ENST00000359203.3; ENSP00000352131.2; ENSG00000025039.15. [Q9NQL2-2] DR Ensembl; ENST00000369415.9; ENSP00000358423.4; ENSG00000025039.15. [Q9NQL2-1] DR GeneID; 58528; -. DR KEGG; hsa:58528; -. DR MANE-Select; ENST00000369415.9; ENSP00000358423.4; NM_021244.5; NP_067067.1. DR UCSC; uc003pnd.5; human. [Q9NQL2-1] DR CTD; 58528; -. DR DisGeNET; 58528; -. DR GeneCards; RRAGD; -. DR HGNC; HGNC:19903; RRAGD. DR HPA; ENSG00000025039; Tissue enhanced (skeletal). DR MIM; 608268; gene. DR neXtProt; NX_Q9NQL2; -. DR OpenTargets; ENSG00000025039; -. DR PharmGKB; PA134957148; -. DR VEuPathDB; HostDB:ENSG00000025039; -. DR eggNOG; KOG3887; Eukaryota. DR GeneTree; ENSGT00950000183031; -. DR HOGENOM; CLU_047421_1_1_1; -. DR InParanoid; Q9NQL2; -. DR OMA; DTQRDIM; -. DR OrthoDB; 1216811at2759; -. DR PhylomeDB; Q9NQL2; -. DR TreeFam; TF300659; -. DR PathwayCommons; Q9NQL2; -. DR Reactome; R-HSA-1632852; Macroautophagy. DR Reactome; R-HSA-165159; MTOR signalling. DR Reactome; R-HSA-166208; mTORC1-mediated signalling. DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK. DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription. DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1. DR SignaLink; Q9NQL2; -. DR SIGNOR; Q9NQL2; -. DR BioGRID-ORCS; 58528; 21 hits in 1071 CRISPR screens. DR ChiTaRS; RRAGD; human. DR EvolutionaryTrace; Q9NQL2; -. DR GenomeRNAi; 58528; -. DR Pharos; Q9NQL2; Tbio. DR PRO; PR:Q9NQL2; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9NQL2; protein. DR Bgee; ENSG00000025039; Expressed in body of tongue and 218 other tissues. DR Genevisible; Q9NQL2; HS. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:1990131; C:Gtr1-Gtr2 GTPase complex; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL. DR GO; GO:0019003; F:GDP binding; IMP:CAFA. DR GO; GO:0005525; F:GTP binding; IMP:CAFA. DR GO; GO:0003924; F:GTPase activity; IMP:CAFA. DR GO; GO:0051020; F:GTPase binding; IPI:CAFA. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB. DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB. DR GO; GO:0071233; P:cellular response to leucine; IMP:CAFA. DR GO; GO:1990253; P:cellular response to leucine starvation; IMP:CAFA. DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central. DR GO; GO:0032008; P:positive regulation of TOR signaling; IBA:GO_Central. DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:CAFA. DR GO; GO:0008104; P:protein localization; ISS:UniProtKB. 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; Alternative splicing; Cytoplasm; GTP-binding; Hydrolase; KW Lysosome; Nucleotide-binding; Nucleus; Reference proteome. FT CHAIN 1..400 FT /note="Ras-related GTP-binding protein D" FT /id="PRO_0000239953" FT REGION 1..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 12..29 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 69..77 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|Ref.15" FT BINDING 117..121 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|Ref.15" FT BINDING 179..182 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|Ref.15" FT VAR_SEQ 1..151 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14574404" FT /id="VSP_052078" FT MUTAGEN 76 FT /note="S->L: Increased RPTOR-binding." FT /evidence="ECO:0000269|PubMed:18497260" FT MUTAGEN 121 FT /note="Q->L: Decreased RPTOR-binding." FT /evidence="ECO:0000269|PubMed:18497260" FT STRAND 64..70 FT /evidence="ECO:0007829|PDB:2Q3F" FT HELIX 75..84 FT /evidence="ECO:0007829|PDB:2Q3F" FT HELIX 88..93 FT /evidence="ECO:0007829|PDB:2Q3F" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:2Q3F" FT STRAND 113..117 FT /evidence="ECO:0007829|PDB:2Q3F" FT HELIX 131..136 FT /evidence="ECO:0007829|PDB:2Q3F" FT STRAND 138..146 FT /evidence="ECO:0007829|PDB:2Q3F" FT HELIX 152..168 FT /evidence="ECO:0007829|PDB:2Q3F" FT STRAND 173..179 FT /evidence="ECO:0007829|PDB:2Q3F" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:2Q3F" FT HELIX 188..206 FT /evidence="ECO:0007829|PDB:2Q3F" FT STRAND 214..219 FT /evidence="ECO:0007829|PDB:2Q3F" FT HELIX 225..235 FT /evidence="ECO:0007829|PDB:2Q3F" SQ SEQUENCE 400 AA; 45588 MW; 96FF0854B11AA1BC CRC64; MSQVLGKPQP QDEDDAEEEE EEDELVGLAD YGDGPDSSDA DPDSGTEEGV LDFSDPFSTE VKPRILLMGL RRSGKSSIQK VVFHKMSPNE TLFLESTNKI CREDVSNSSF VNFQIWDFPG QIDFFDPTFD YEMIFRGTGA LIFVIDSQDD YMEALARLHL TVTRAYKVNT DINFEVFIHK VDGLSDDHKI ETQRDIHQRA NDDLADAGLE KIHLSFYLTS IYDHSIFEAF SKVVQKLIPQ LPTLENLLNI FISNSGIEKA FLFDVVSKIY IATDSTPVDM QTYELCCDMI DVVIDISCIY GLKEDGAGTP YDKESTAIIK LNNTTVLYLK EVTKFLALVC FVREESFERK GLIDYNFHCF RKAIHEVFEV RMKVVKSRKV QNRLQKKKRA TPNGTPRVLL //