NPRL3_MOUSE
ID NPRL3_MOUSE Reviewed; 569 AA.
AC Q8VIJ8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=GATOR complex protein NPRL3 {ECO:0000305};
DE AltName: Full=Nitrogen permease regulator 3-like protein {ECO:0000312|MGI:MGI:109258};
GN Name=Nprl3 {ECO:0000312|MGI:MGI:109258};
GN Synonyms=Mare {ECO:0000312|MGI:MGI:109258};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11157800; DOI=10.1093/hmg/10.4.371;
RA Flint J., Tufarelli C., Peden J., Clark K., Daniels R.J., Hardison R.,
RA Miller W., Philipsen S., Tan-Un K.C., McMorrow T., Frampton J., Alter B.P.,
RA Frischauf A.-M., Higgs D.R.;
RT "Comparative genome analysis delimits a chromosomal domain and identifies
RT key regulatory elements in the alpha globin cluster.";
RL Hum. Mol. Genet. 10:371-382(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: As a component of the GATOR1 complex functions as an
CC inhibitor of the amino acid-sensing branch of the TORC1 pathway. The
CC GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB
CC within RRAGC-containing heterodimers, thereby deactivating RRAGs,
CC releasing mTORC1 from lysosomal surface and inhibiting mTORC1
CC signaling. The GATOR1 complex is negatively regulated by GATOR2 the
CC other GATOR subcomplex in this amino acid-sensing branch of the TORC1
CC pathway. {ECO:0000250|UniProtKB:Q12980}.
CC -!- SUBUNIT: Forms a heterodimer with NPRL2 (By similarity). Within the
CC GATOR complex, component of the GATOR1 subcomplex, made of DEPDC5,
CC NPRL2 and NPRL3. GATOR1 mediates the strong interaction of the GATOR
CC complex with RRAGA/RRAGC and RRAGB/RRAGC heterodimers (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q12980}.
CC Note=Localization to lysosomes is amino acid-independent.
CC {ECO:0000250|UniProtKB:Q12980}.
CC -!- SIMILARITY: Belongs to the NPR3 family. {ECO:0000305}.
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DR EMBL; AY016021; AAL32369.1; -; Genomic_DNA.
DR EMBL; AK036405; BAC29415.1; -; mRNA.
DR EMBL; AK081902; BAC38366.1; -; mRNA.
DR EMBL; BC064471; AAH64471.1; -; mRNA.
DR CCDS; CCDS24521.1; -.
DR RefSeq; NP_001271288.1; NM_001284359.1.
DR RefSeq; NP_001271289.1; NM_001284360.1.
DR RefSeq; NP_853547.1; NM_181569.3.
DR AlphaFoldDB; Q8VIJ8; -.
DR SMR; Q8VIJ8; -.
DR STRING; 10090.ENSMUSP00000020530; -.
DR iPTMnet; Q8VIJ8; -.
DR PhosphoSitePlus; Q8VIJ8; -.
DR EPD; Q8VIJ8; -.
DR MaxQB; Q8VIJ8; -.
DR PaxDb; Q8VIJ8; -.
DR PRIDE; Q8VIJ8; -.
DR ProteomicsDB; 295515; -.
DR Antibodypedia; 1565; 86 antibodies from 27 providers.
DR DNASU; 17168; -.
DR Ensembl; ENSMUST00000020530; ENSMUSP00000020530; ENSMUSG00000020289.
DR GeneID; 17168; -.
DR KEGG; mmu:17168; -.
DR UCSC; uc007ijc.2; mouse.
DR CTD; 8131; -.
DR MGI; MGI:109258; Nprl3.
DR VEuPathDB; HostDB:ENSMUSG00000020289; -.
DR eggNOG; KOG3830; Eukaryota.
DR GeneTree; ENSGT00390000015916; -.
DR HOGENOM; CLU_014030_1_0_1; -.
DR InParanoid; Q8VIJ8; -.
DR OMA; CLPQKVH; -.
DR OrthoDB; 628619at2759; -.
DR PhylomeDB; Q8VIJ8; -.
DR TreeFam; TF105965; -.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR BioGRID-ORCS; 17168; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Nprl3; mouse.
DR PRO; PR:Q8VIJ8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VIJ8; protein.
DR Bgee; ENSMUSG00000020289; Expressed in hindlimb stylopod muscle and 156 other tissues.
DR ExpressionAtlas; Q8VIJ8; baseline and differential.
DR Genevisible; Q8VIJ8; MM.
DR GO; GO:1990130; C:GATOR1 complex; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0035909; P:aorta morphogenesis; IMP:MGI.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
DR GO; GO:0032007; P:negative regulation of TOR signaling; ISO:MGI.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0038202; P:TORC1 signaling; IBA:GO_Central.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR005365; Npr3.
DR PANTHER; PTHR13153; PTHR13153; 1.
DR Pfam; PF03666; NPR3; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Lysosome; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..569
FT /note="GATOR complex protein NPRL3"
FT /id="PRO_0000278089"
FT REGION 27..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12980"
SQ SEQUENCE 569 AA; 63618 MW; DEB141AB27539E44 CRC64;
MGDNTSPISV ILVSSGSRGN KLLFRYPFQR SQEHPASQTN KPRSRYAVNN TGEHADDQDG
DSRFSDVILA TILATKSEMC GQKFELKIDN VRFVGHPTLL QHALGQVSKT DPSPKREAPT
MILFNVVFAL RANADPSVIN CLHNLSRRIA TVLQHEERRC QYLTREAKLI LALQDEVSAM
ADANEGPQSP FQHILPKCKL ARDLKEAYDS LCTSGVVRLH INSWLEVSFC LPHKIHYAAS
SLIPPEAIER SLKAIRPYHA LLLLSDEKSL LSELPIDCSP ALVRVIKTTS AVKNLQQLAQ
DADLALLQVF QLAAHLVYWG KAVIIYPLCE NNVYVMSPNA SVCLYSPLAE QFSRQFPSHD
LPSVLAKFSL PVSLSEFRSP LAPPAQETQL IQMVVWMLQR RLLIQLHTYV CLMASPSEEE
PRLREDDVPF TARVGGRSLS TPNALSFGSP TSSDDMTLTS PSMDNSSAEL LPSGDSPLNK
RMTENLLASL SEHERAAILN VPAAQNPEDL RMFARLLHYF RGRHHLEEIM YNENTRRSQL
LMLFDKFRSV LVVTTHEDPV IAVFQALLT
