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   27-MAR-2024, entry version 200.
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;
GN   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   PDB; 7PQH; EM; 3.87 A; A/B/G/J=1-1557.
DR   PDBsum; 7PQH; -.
DR   AlphaFoldDB; P38873; -.
DR   SMR; P38873; -.
DR   BioGRID; 36620; 557.
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; 4932-YHR186C; -.
DR   PeptideAtlas; P38873; -.
DR   EnsemblFungi; YHR186C_mRNA; YHR186C; YHR186C.
DR   GeneID; 856593; -.
DR   KEGG; sce:YHR186C; -.
DR   AGR; SGD:S000001229; -.
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; HHHPLWK; -.
DR   OrthoDB; 103066at2759; -.
DR   BioCyc; YEAST:G3O-31216-MONOMER; -.
DR   Reactome; R-SCE-3371571; HSF1-dependent transactivation.
DR   Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR   BioGRID-ORCS; 856593; 0 hits in 10 CRISPR screens.
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:0010506; P:regulation of autophagy; IBA:GO_Central.
DR   GO; GO:0051726; P:regulation of cell cycle; NAS:ComplexPortal.
DR   GO; GO:0001558; P:regulation of cell growth; IPI:SGD.
DR   GO; GO:0007584; P:response to nutrient; NAS:ComplexPortal.
DR   GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR12848; REGULATORY-ASSOCIATED PROTEIN OF MTOR; 1.
DR   PANTHER; PTHR12848:SF16; REGULATORY-ASSOCIATED PROTEIN OF MTOR; 1.
DR   Pfam; PF02985; HEAT; 1.
DR   Pfam; PF14538; Raptor_N; 1.
DR   PRINTS; PR01547; YEAST176DUF.
DR   SMART; SM01302; Raptor_N; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 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   3D-structure; Cell membrane; Membrane; Reference proteome; Repeat; Vacuole;
KW   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
//