RRAGD_HUMAN
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};
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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
