MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Ras-related GTP-binding protein D; Short=Rag D; Short=RagD; |
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| MyHits synonyms | RRAGD_HUMAN , Q9NQL2 , A8K184 , Q7L8F9 , Q9NPG0 , 96FF0854B11AA1BC |
 Legends: 1, MUTAGEN S->L: Increased RPTOR-binding. {ECO:0000269|PubMed:18497260}; 2, MUTAGEN Q->L: Decreased RPTOR-binding. {ECO:0000269|PubMed:18497260}; 3, NP_BIND GTP; 4, VAR_SEQ Missing (in isoform 2). {ECO:0000303|PubMed:14574404}; 5, STRAND {ECO:0000244|PDB:2Q3F}; 6, HELIX {ECO:0000244|PDB:2Q3F}.
| |
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 10-MAY-2017, entry version 118.
DE RecName: Full=Ras-related GTP-binding protein D;
DE Short=Rag D;
DE Short=RagD;
GN Name=RRAGD {ECO:0000312|HGNC:HGNC:19903};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG32663.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RRAGA AND
RP RRAGB, 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
RT proteins, Rag 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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:CAB99362.1}
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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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
RT project: 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.,
RA Nishimoto T.;
RT "A novel human nucleolar protein, Nop132, binds to the G proteins,
RT RRAG 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
RT 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.,
RA 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 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
RT Rag GTPases to control mTORC1 signaling.";
RL Cell 159:122-133(2014).
RN [12]
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.,
RA Bruckner M., Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W.,
RA Heinz L.X., Kraft C., Bennett K.L., Indiveri C., Huber L.A.,
RA Superti-Furga G.;
RT "SLC38A9 is a component of the lysosomal amino acid sensing machinery
RT that controls mTORC1.";
RL Nature 519:477-481(2015).
RN [13]
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.,
RA Bar-Peled L., Zoncu R., Straub C., Kim C., Park J., Sabatini B.L.,
RA Sabatini D.M.;
RT "Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine
RT sufficiency to mTORC1.";
RL Science 347:188-194(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 60-239 IN COMPLEX WITH GTP
RP 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 forming heterodimeric
CC Rag complexes required for the amino acid-induced relocalization
CC of mTORC1 to the lysosomes and its subsequent activation by the
CC GTPase RHEB. This is a crucial step in the activation of the TOR
CC signaling cascade by amino acids. {ECO:0000269|PubMed:20381137}.
CC -!- SUBUNIT: Forms a heterodimer with RRAGA in a sequence-independent
CC manner and RRAGB. Heterodimerization stabilizes RRAG proteins. In
CC complex with RRAGB, interacts with RPTOR; this interaction is
CC particularly efficient with GTP-loaded RRAGB and GDP-loaded RRAGC.
CC Interacts with NOL8. Interacts with SH3BP4; the interaction with
CC this negative regulator is most probably direct, preferentially
CC occurs with the inactive GDP-bound form of RRAGD and is negatively
CC regulated by amino acids (PubMed:11073942, PubMed:14660641,
CC PubMed:18497260, PubMed:22575674, Ref.14). The Rag heterodimer
CC interacts with SLC38A9; the probable amino acid sensor
CC (PubMed:25561175, PubMed:25567906). Interacts with SESN1, SESN2
CC AND SESN3 (PubMed:25259925). {ECO:0000269|PubMed:11073942,
CC ECO:0000269|PubMed:14660641, ECO:0000269|PubMed:18497260,
CC ECO:0000269|PubMed:22575674, ECO:0000269|PubMed:25259925,
CC ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906,
CC ECO:0000269|Ref.14}.
CC -!- INTERACTION:
CC Q9P2J5:LARS; NbExp=13; IntAct=EBI-992949, EBI-356077;
CC Q7L523:RRAGA; NbExp=8; IntAct=EBI-992949, EBI-752376;
CC Q5VZM2:RRAGB; NbExp=7; IntAct=EBI-992949, EBI-993049;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11073942}.
CC Nucleus {ECO:0000269|PubMed:11073942}. Lysosome
CC {ECO:0000269|PubMed:20381137}. Note=Predominantly cytoplasmic. May
CC shuttle between the cytoplasm and nucleus, depending on the bound
CC nucleotide state of associated RRAGA (PubMed:11073942).
CC {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 Note=No experimental confirmation available. {ECO:0000305};
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=Translation N-terminally extended.; Evidence={ECO:0000305};
CC -----------------------------------------------------------------------
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DR EMBL; AF272036; AAG32663.1; -; mRNA.
DR EMBL; AK289799; BAF82488.1; -; mRNA.
DR EMBL; AL138717; CAB99361.1; -; Genomic_DNA.
DR EMBL; AL138717; CAB99362.1; -; 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 UniGene; Hs.31712; -.
DR PDB; 2Q3F; X-ray; 2.10 A; A/B=60-239.
DR PDBsum; 2Q3F; -.
DR ProteinModelPortal; Q9NQL2; -.
DR SMR; Q9NQL2; -.
DR BioGrid; 121848; 11.
DR IntAct; Q9NQL2; 10.
DR STRING; 9606.ENSP00000358423; -.
DR iPTMnet; Q9NQL2; -.
DR PhosphoSitePlus; Q9NQL2; -.
DR BioMuta; RRAGD; -.
DR DMDM; 74752904; -.
DR EPD; Q9NQL2; -.
DR MaxQB; Q9NQL2; -.
DR PaxDb; Q9NQL2; -.
DR PeptideAtlas; Q9NQL2; -.
DR PRIDE; Q9NQL2; -.
DR DNASU; 58528; -.
DR Ensembl; ENST00000359203; ENSP00000352131; ENSG00000025039. [Q9NQL2-2]
DR Ensembl; ENST00000369415; ENSP00000358423; ENSG00000025039. [Q9NQL2-1]
DR GeneID; 58528; -.
DR KEGG; hsa:58528; -.
DR UCSC; uc003pnd.5; human. [Q9NQL2-1]
DR CTD; 58528; -.
DR DisGeNET; 58528; -.
DR GeneCards; RRAGD; -.
DR HGNC; HGNC:19903; RRAGD.
DR HPA; HPA068664; -.
DR MIM; 608268; gene.
DR neXtProt; NX_Q9NQL2; -.
DR OpenTargets; ENSG00000025039; -.
DR PharmGKB; PA134957148; -.
DR eggNOG; KOG3887; Eukaryota.
DR eggNOG; ENOG410XQS9; LUCA.
DR GeneTree; ENSGT00550000074708; -.
DR HOGENOM; HOG000203695; -.
DR HOVERGEN; HBG059482; -.
DR InParanoid; Q9NQL2; -.
DR KO; K16186; -.
DR OMA; HPDINFE; -.
DR OrthoDB; EOG091G0AN4; -.
DR PhylomeDB; Q9NQL2; -.
DR TreeFam; TF300659; -.
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 SIGNOR; Q9NQL2; -.
DR ChiTaRS; RRAGD; human.
DR EvolutionaryTrace; Q9NQL2; -.
DR GenomeRNAi; 58528; -.
DR PRO; PR:Q9NQL2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR Bgee; ENSG00000025039; -.
DR CleanEx; HS_RRAGD; -.
DR Genevisible; Q9NQL2; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC.
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; IMP:CAFA.
DR GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
DR GO; GO:0034613; P:cellular protein localization; ISS: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:0016236; P:macroautophagy; TAS:Reactome.
DR GO; GO:0032008; P:positive regulation of TOR signaling; NAS:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:CAFA.
DR InterPro; IPR006762; Gtr1_RagA.
DR InterPro; IPR027417; P-loop_NTPase.
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; Complete proteome; Cytoplasm;
KW GTP-binding; Lysosome; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1 400 Ras-related GTP-binding protein D.
FT /FTId=PRO_0000239953.
FT NP_BIND 69 77 GTP.
FT NP_BIND 117 121 GTP.
FT NP_BIND 179 182 GTP.
FT VAR_SEQ 1 151 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14574404}.
FT /FTId=VSP_052078.
FT MUTAGEN 76 76 S->L: Increased RPTOR-binding.
FT {ECO:0000269|PubMed:18497260}.
FT MUTAGEN 121 121 Q->L: Decreased RPTOR-binding.
FT {ECO:0000269|PubMed:18497260}.
FT STRAND 64 70 {ECO:0000244|PDB:2Q3F}.
FT HELIX 75 84 {ECO:0000244|PDB:2Q3F}.
FT HELIX 88 93 {ECO:0000244|PDB:2Q3F}.
FT STRAND 101 105 {ECO:0000244|PDB:2Q3F}.
FT STRAND 113 117 {ECO:0000244|PDB:2Q3F}.
FT HELIX 131 136 {ECO:0000244|PDB:2Q3F}.
FT STRAND 138 146 {ECO:0000244|PDB:2Q3F}.
FT HELIX 152 168 {ECO:0000244|PDB:2Q3F}.
FT STRAND 173 179 {ECO:0000244|PDB:2Q3F}.
FT HELIX 181 183 {ECO:0000244|PDB:2Q3F}.
FT HELIX 188 206 {ECO:0000244|PDB:2Q3F}.
FT STRAND 214 219 {ECO:0000244|PDB:2Q3F}.
FT HELIX 225 235 {ECO:0000244|PDB:2Q3F}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 64 290 ipfam:Gtr1_RagA [T]
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
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