WDR24_MOUSE
ID WDR24_MOUSE Reviewed; 790 AA.
AC Q8CFJ9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=GATOR complex protein WDR24 {ECO:0000305};
DE AltName: Full=WD repeat-containing protein 24 {ECO:0000312|MGI:MGI:2446285};
GN Name=Wdr24 {ECO:0000312|MGI:MGI:2446285};
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 [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594 AND SER-598, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
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 GATOR subcomplex GATOR2, functions
CC within the amino acid-sensing branch of the TORC1 signaling pathway.
CC Indirectly activates mTORC1 and the TORC1 signaling pathway through the
CC inhibition of the GATOR1 subcomplex. It is negatively regulated by the
CC upstream amino acid sensors SESN2 and CASTOR1. In addition to its role
CC in regulation of the TORC1 complex, promotes the acidification of
CC lysosomes and facilitates autophagic flux.
CC {ECO:0000250|UniProtKB:Q96S15}.
CC -!- SUBUNIT: Within the GATOR complex, component of the GATOR2 subcomplex,
CC made of MIOS, SEC13, SEH1L, WDR24 and WDR59. The GATOR complex strongly
CC interacts with RRAGA/RRAGC and RRAGB/RRAGC heterodimers. The GATOR2
CC complex interacts with CASTOR2 and CASTOR1; the interaction is
CC negatively regulated by arginine. The GATOR2 complex interacts with
CC SESN1, SESN2 and SESN3; the interaction is negatively regulated by
CC amino acids. {ECO:0000250|UniProtKB:Q96S15}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q96S15}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR24 family. {ECO:0000305}.
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DR EMBL; BC037651; AAH37651.1; -; mRNA.
DR CCDS; CCDS28531.1; -.
DR RefSeq; NP_776102.1; NM_173741.3.
DR AlphaFoldDB; Q8CFJ9; -.
DR SMR; Q8CFJ9; -.
DR BioGRID; 234581; 1.
DR STRING; 10090.ENSMUSP00000026833; -.
DR iPTMnet; Q8CFJ9; -.
DR PhosphoSitePlus; Q8CFJ9; -.
DR EPD; Q8CFJ9; -.
DR MaxQB; Q8CFJ9; -.
DR PaxDb; Q8CFJ9; -.
DR PeptideAtlas; Q8CFJ9; -.
DR PRIDE; Q8CFJ9; -.
DR ProteomicsDB; 297940; -.
DR Antibodypedia; 42379; 47 antibodies from 18 providers.
DR Ensembl; ENSMUST00000026833; ENSMUSP00000026833; ENSMUSG00000025737.
DR GeneID; 268933; -.
DR KEGG; mmu:268933; -.
DR UCSC; uc008bcd.2; mouse.
DR CTD; 84219; -.
DR MGI; MGI:2446285; Wdr24.
DR VEuPathDB; HostDB:ENSMUSG00000025737; -.
DR eggNOG; KOG0269; Eukaryota.
DR GeneTree; ENSGT00940000159396; -.
DR HOGENOM; CLU_010233_0_0_1; -.
DR InParanoid; Q8CFJ9; -.
DR OMA; QDGTMKC; -.
DR OrthoDB; 590848at2759; -.
DR PhylomeDB; Q8CFJ9; -.
DR TreeFam; TF314190; -.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR BioGRID-ORCS; 268933; 17 hits in 72 CRISPR screens.
DR PRO; PR:Q8CFJ9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8CFJ9; protein.
DR Bgee; ENSMUSG00000025737; Expressed in spermatocyte and 221 other tissues.
DR Genevisible; Q8CFJ9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0061700; C:GATOR2 complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISO:MGI.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR037590; WDR24.
DR PANTHER; PTHR46200; PTHR46200; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Autophagy; Lysosome; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..790
FT /note="GATOR complex protein WDR24"
FT /id="PRO_0000051376"
FT REPEAT 72..112
FT /note="WD 1"
FT REPEAT 118..158
FT /note="WD 2"
FT REPEAT 161..201
FT /note="WD 3"
FT REPEAT 205..245
FT /note="WD 4"
FT REPEAT 249..291
FT /note="WD 5"
FT REPEAT 295..338
FT /note="WD 6"
FT REGION 516..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S15"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S15"
FT MOD_RES 581
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96S15"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 790 AA; 88184 MW; AF4A5E490357D57D CRC64;
MEKMSRVSTA LSGSALTGRT MHCHLDAPAN AISVCRDAAQ VVVAGRSIFK IYAIEEEQFV
EKLNLRVGRK PSLNLSCADV VWHQMDENLL ATAATNGVVV TWNLGRPSRN KQDQLFTEHK
RTVNKVCFHP TEAHVLLSGS QDGFMKCFDL RRKDSVSTFS GQSESVRDVQ FSIRDYFTFA
STFENGNVQL WDIRRPDRCE RMFTAHNGPV FCCDWHPEDR GWLATGGRDK MVKVWDMTTH
RAKEIHCVQT IASVARVKWR PECRHHLATC SMMVDHNIYV WDVRRPFVPA AMFEEHRDVT
TGIAWRHPHD PSFLLSGSKD STLCQHLFRD ASQPVERANP EGLCYGLFGD LAFAVKESLV
AAESGRKPYA GDRRHPIFFK RKLDPAEPFS GLASSALSVF ETESSGGSMS WFVDTAERYV
LAGRPLAELC DHNAKVAREL GRNQVAQTWT MLRIIYCSPG LVSSANLNHS VGKGSSCGLP
LMNSFNLKDM GPGLGSETRL DRSKGDTRSD AALLDSSATL VTNEDNEETE GSDVPADYLL
GDVEGEDDEL YPLDTEHVHS EEPEYVLPQE AFPLRHEIVD TPSGPEHLQD KADSPHVSGN
EADTASLAPV DSSSSLLSVS HALYDSRLPP DFFSVLVRDM LRFYAEQGDV QMAVSVLIVL
GERVRKDIDE QTQEHWYTSY IDLLQRFCLW NVSNEVVKLS TSRAVSCLNQ ASTTLHVNCS
HCKRPMSSRG WVCDRCHRCA SMCAVCHHVV KGLFVWCQGC SHGGHLQHIM KWLEGSSHCP
AGCGHLCEYS
