KOG1_YEAST
ID KOG1_YEAST Reviewed; 1557 AA.
AC P38873; D3DLD4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Target of rapamycin complex 1 subunit KOG1;
DE Short=TORC1 subunit KOG1;
DE AltName: Full=Kontroller of growth protein 1;
DE AltName: Full=Local anesthetic-sensitive protein 24;
DE AltName: Full=Regulatory-associated protein of TOR {ECO:0000250|UniProtKB:Q8N122};
DE Short=Raptor {ECO:0000305};
GN Name=KOG1; Synonyms=LAS24; OrderedLocusNames=YHR186C; ORFNames=H9998.14;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION IN TORC1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12408816; DOI=10.1016/s1097-2765(02)00636-6;
RA Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L.,
RA Bonenfant D., Oppliger W., Jenoe P., Hall M.N.;
RT "Two TOR complexes, only one of which is rapamycin sensitive, have distinct
RT roles in cell growth control.";
RL Mol. Cell 10:457-468(2002).
RN [4]
RP SUBUNIT, AND INTERACTION WITH TOR1.
RX PubMed=12631735; DOI=10.1091/mbc.e02-09-0609;
RA Wedaman K.P., Reinke A., Anderson S., Yates J.R. III, McCaffery J.M.,
RA Powers T.;
RT "Tor kinases are in distinct membrane-associated protein complexes in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:1204-1220(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16394584; DOI=10.1266/ggs.80.325;
RA Araki T., Uesono Y., Oguchi T., Toh-e A.;
RT "LAS24/KOG1, a component of the TOR complex 1 (TORC1), is needed for
RT resistance to local anesthetic tetracaine and normal distribution of actin
RT cytoskeleton in yeast.";
RL Genes Genet. Syst. 80:325-343(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=28483912; DOI=10.1128/mcb.00075-17;
RA Tanigawa M., Maeda T.;
RT "An In Vitro TORC1 Kinase Assay That Recapitulates the Gtr-Independent
RT Glutamine-Responsive TORC1 Activation Mechanism on Yeast Vacuoles.";
RL Mol. Cell. Biol. 37:e00075-e00075(2017).
RN [10]
RP INTERACTION WITH PIB2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29698392; DOI=10.1371/journal.pgen.1007334;
RA Ukai H., Araki Y., Kira S., Oikawa Y., May A.I., Noda T.;
RT "Gtr/Ego-independent TORC1 activation is achieved through a glutamine-
RT sensitive interaction with Pib2 on the vacuolar membrane.";
RL PLoS Genet. 14:e1007334-e1007334(2018).
CC -!- FUNCTION: Component of TORC1, which regulates multiple cellular
CC processes to control cell growth in response to environmental signals.
CC Nutrient limitation and environmental stress signals cause inactivation
CC of TORC1. Active TORC1 positively controls ribosome biogenesis via
CC control of rRNA, ribosomal protein and tRNA gene expression, and rRNA
CC processing. TORC1 positively controls protein biosynthesis by
CC regulation of mRNA stability, translation initiation factor activity,
CC and high-affinity amino acid permeases that serve to provide amino
CC acids for use by the translation machinery. TORC1 also promotes growth
CC by sequestering a number of nutrient and general stress-responsive
CC transcription factors in the cytoplasm. TORC1 negatively controls
CC macroautophagy, a process to recycle surplus cytoplasmic mass under
CC nutrient starvation conditions. KOG1 may have a role in binding and
CC recruiting substrates of TORC1. {ECO:0000269|PubMed:16394584}.
CC -!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of at
CC least KOG1, LST8, TCO89 and either TOR1 (TORC1-A) or TOR2 (TORC1-B)
CC (PubMed:12408816, PubMed:12631735, PubMed:16394584). Interacts with
CC PIB2; following activation of PIB2 by glutamine or cysteine
CC (PubMed:29698392). TORC1 binds to and is inhibited by FKBP-rapamycin
CC (PubMed:12408816). {ECO:0000269|PubMed:12408816,
CC ECO:0000269|PubMed:12631735, ECO:0000269|PubMed:16394584,
CC ECO:0000269|PubMed:29698392}.
CC -!- INTERACTION:
CC P38873; P38691: KSP1; NbExp=3; IntAct=EBI-24864, EBI-9937;
CC P38873; P41318: LST8; NbExp=3; IntAct=EBI-24864, EBI-28598;
CC P38873; P35169: TOR1; NbExp=7; IntAct=EBI-24864, EBI-19374;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16394584, ECO:0000269|PubMed:28483912}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305|PubMed:28483912}. Note=Also localizes to membranous
CC structures within the cell interior, probably endosomal or Golgi
CC membranes. {ECO:0000269|PubMed:16394584}.
CC -!- SIMILARITY: Belongs to the WD repeat RAPTOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68364.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U00030; AAB68364.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006934; DAA06878.1; -; Genomic_DNA.
DR PIR; S46686; S46686.
DR RefSeq; NP_012056.1; NM_001179317.1.
DR AlphaFoldDB; P38873; -.
DR SMR; P38873; -.
DR BioGRID; 36620; 330.
DR ComplexPortal; CPX-1715; TORC1 serine/threonine-protein kinase complex, TOR1 variant.
DR ComplexPortal; CPX-1716; TORC1 serine/threonine-protein kinase complex, TOR2 variant.
DR DIP; DIP-2639N; -.
DR IntAct; P38873; 47.
DR MINT; P38873; -.
DR STRING; 4932.YHR186C; -.
DR iPTMnet; P38873; -.
DR MaxQB; P38873; -.
DR PaxDb; P38873; -.
DR PRIDE; P38873; -.
DR EnsemblFungi; YHR186C_mRNA; YHR186C; YHR186C.
DR GeneID; 856593; -.
DR KEGG; sce:YHR186C; -.
DR SGD; S000001229; KOG1.
DR VEuPathDB; FungiDB:YHR186C; -.
DR eggNOG; KOG1517; Eukaryota.
DR GeneTree; ENSGT00640000091541; -.
DR HOGENOM; CLU_001136_0_2_1; -.
DR InParanoid; P38873; -.
DR OMA; QWSCLCL; -.
DR BioCyc; YEAST:G3O-31216-MON; -.
DR Reactome; R-SCE-3371571; HSF1-dependent transactivation.
DR Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR PRO; PR:P38873; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38873; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0031931; C:TORC1 complex; IPI:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IMP:SGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IBA:GO_Central.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IC:ComplexPortal.
DR GO; GO:0001558; P:regulation of cell growth; IPI:SGD.
DR GO; GO:0007584; P:response to nutrient; IC:ComplexPortal.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR004083; Raptor.
DR InterPro; IPR029347; Raptor_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR12848; PTHR12848; 1.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF14538; Raptor_N; 1.
DR SMART; SM01302; Raptor_N; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Repeat; Vacuole; WD repeat.
FT CHAIN 1..1557
FT /note="Target of rapamycin complex 1 subunit KOG1"
FT /id="PRO_0000051476"
FT REPEAT 548..586
FT /note="HEAT 1"
FT REPEAT 588..625
FT /note="HEAT 2"
FT REPEAT 777..814
FT /note="HEAT 3"
FT REPEAT 888..925
FT /note="HEAT 4"
FT REPEAT 1207..1248
FT /note="WD 1"
FT REPEAT 1252..1293
FT /note="WD 2"
FT REPEAT 1296..1346
FT /note="WD 3"
FT REPEAT 1350..1390
FT /note="WD 4"
FT REPEAT 1400..1440
FT /note="WD 5"
FT REPEAT 1452..1492
FT /note="WD 6"
FT REPEAT 1517..1557
FT /note="WD 7"
FT REGION 1084..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1557 AA; 177609 MW; B927EE93700176D3 CRC64;
MPEIYGPQPL KPLNTVMRHG FEEQYQSDQL LQSLANDFIF YFDDKRHKTN GNPIPEEDKQ
RDVNRYYQPI TDWKIMKDRQ KTVSAALLLC LNLGVDPPDV MKTHPCARVE AWVDPLNFQD
SKKAIEQIGK NLQAQYETLS LRTRYKQSLD PCVEDVKRFC NSLRRTSKED RILFHYNGHG
VPKPTKSGEI WVFNRGYTQY IPVSLYDLQT WLGAPCIFVY DCNSAENILI NFQKFVQKRI
KDDEEGNHDV AAPSPTSAYQ DCFQLASCTS DELLLMSPEL PADLFSCCLT CPIEISIRIF
LMQSPLKDSK YKIFFENSTS NQPFGDSKNS FKSKIPNVNI PGMLSDRRTP LGELNWIFTA
ITDTIAWTSL PRPLFKKLFR HDLMIAALFR NFLLAKRIMP WYNCHPVSDP ELPDSITTHP
MWKSWDLAMD EVLTKIVIDL KNAPPATALE SQMILQQQET LQNGGSSKSN AQDTKAGSIQ
TQSRFAVANL STMSLVNNPA LQSRKSISLQ SSQQQLQQQQ QQQQQFTGFF EQNLTAFELW
LKYASNVRHP PEQLPIVLQV LLSQVHRIRA LVLLSRFLDL GPWAVYLSLS IGIFPYVLKL
LQSPAPELKP ILVFIWARIM SIDYKNTQSE LIKEKGYMYF VTVLVPDWGV NGMSATNGSA
MINSGNPLTM TASQNINGPS SRYYERQQGN RTSNLGHNNL PFYHSNDTTD EQKAMAVFVL
ASFVRNFPLG QKNCFSLELV NKLCFYIDNS EIPLLRQWCV ILLGLLFADN PLNRFVCMNT
GAVEILLKSL KDPVPEVRTA SIFALKHFIS GFQDAEVILR LQQEFEEQYQ QLHSQLQHLQ
NQSHLQQQQS QQQQQHLEQQ QMKIEKQIRH CQVMQNQLEV IDLRKLKRQE IGNLISILPL
INDGSSLVRK ELVVYFSHIV SRYSNFFIVV VFNDLLEEIK LLEKSDINTR NTSDKYSVSQ
GSIFYTVWKS LLILAEDPFL ENKELSKQVI DYILLELSAH KELGGPFAVM EKFLLKRSSK
AHQTGKFGFN SSQVQFVKSS LRSFSPNERV DNNAFKKEQQ QHDPKISHPM RTSLAKLFQS
LGFSESNSDS DTQSSNTSMK SHTSKKGPSG LYLLNGNNNI YPTAETPRFR KHTEPLQLPL
NSSFLDYSRE YFQEPQMKKQ EADEPGSVEY NARLWRRNRN ETIIQETQGE KKLSIYGNWS
KKLISLNNKS QPKLMKFAQF EDQLITADDR STITVFDWEK GKTLSKFSNG TPFGTKVTDL
KLINEDDSAL LLTGSSDGVI KIYRDYQDVD TFKIVSAWRG LTDMLLTPRS TGLLTEWLQI
RGSLLTTGDV KVIRVWDAHT ETVEVDIPAK TSSLITSLTA DQLAGNIFVA GFADGSLRVY
DRRLDPRDSM IRRWRAGNDK QGVWINNVHL QRGGYRELVS GATNGVVELW DIRSEDPVES
FVDQNVTSQY GSQQKPTTMT CMQVHEHAPI IATGTKQIKI WTTSGDLLNS FKNSHNNGVT
STLAATGIPK SLSYSSTSDA FLSSMAFHPH RMMIAATNSH DSIVNIYKCE DERIDYF
