TOR1_YEASX
ID TOR1_YEASX Reviewed; 2470 AA.
AC A0A8H4FAU0;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=Serine/threonine-protein kinase TOR1 {ECO:0000250|UniProtKB:P35169};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P35169};
GN Name=TOR1 {ECO:0000303|PubMed:28993463};
GN ORFNames=GI527_G0003323 {ECO:0000312|EMBL:KAF1905928.1};
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932 {ECO:0000312|Proteomes:UP000470054};
RN [1] {ECO:0000312|Proteomes:UP000470054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INSC1005 {ECO:0000312|Proteomes:UP000470054};
RA Fiddes I.T., Church D.M.;
RT "Inscripta technologies.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:28993463};
RX PubMed=28993463; DOI=10.1242/jcs.207910;
RA Varlakhanova N.V., Mihalevic M.J., Bernstein K.A., Ford M.G.J.;
RT "Pib2 and the EGO complex are both required for activation of TORC1.";
RL J. Cell Sci. 130:3878-3890(2017).
CC -!- FUNCTION: Phosphatidylinositol 3-kinase homolog, component of TORC1,
CC which regulates multiple cellular processes to control cell growth in
CC response to environmental signals (By similarity). Nutrient limitation
CC and environmental stress signals cause inactivation of TORC1
CC (PubMed:28993463). Active TORC1 positively controls ribosome biogenesis
CC via control of rRNA, ribosomal protein and tRNA gene expression, and
CC rRNA 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. TORC1 controls many of these processes
CC via TIP41-TAP42-mediated inhibition of the type 2A-related phosphatases
CC PP2A and SIT4 (By similarity). In nutrient-rich conditions, responsible
CC for the phosphorylation of AGC S6 kinase (S6K) YPK3, activating YPK3
CC kinase activity and promoting phosphorylation of ribosomal protein S6.
CC Phosphorylates kinase SCH9 at 6 amino acids in the C-terminus,
CC activating SCH9 kinase activity to properly regulate ribosome
CC biogenesis, translation initiation, and entry into stationary phase (By
CC similarity). {ECO:0000250|UniProtKB:P35169,
CC ECO:0000269|PubMed:28993463}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P35169};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P35169};
CC -!- ACTIVITY REGULATION: Activated by the glutamine sensor PIB2 in
CC nutrient-rich conditions. {ECO:0000269|PubMed:28993463}.
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) (By
CC similarity). Interacts with PIB2; following activation of PIB2 by
CC glutamine or cysteine (By similarity). TORC1 binds to and is inhibited
CC by FKBP-rapamycin (By similarity). {ECO:0000250|UniProtKB:P35169}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35169};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P35169}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P35169}. Vacuole membrane
CC {ECO:0000269|PubMed:28993463}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P35169}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P35169}. Note=Also localizes to membranous
CC structures both proximal to, yet distinct from, the plasma membrane as
CC well as within the cell interior, probably endosomal or Golgi membranes
CC (By similarity). Localization to the vacuolar membrane is dependent
CC upon PIB2 and GTR1 (PubMed:28993463). {ECO:0000250|UniProtKB:P35169,
CC ECO:0000269|PubMed:28993463}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; JAAEAL010000009; KAF1905928.1; -; Genomic_DNA.
DR Proteomes; UP000470054; Unassembled WGS sequence.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.20.120.150; -; 1.
DR Gene3D; 1.25.10.10; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024585; DUF3385_TOR.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR.
DR PANTHER; PTHR11139:SF9; PTHR11139:SF9; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF47212; SSF47212; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Repeat; Serine/threonine-protein kinase; Transferase;
KW Vacuole.
FT CHAIN 1..2470
FT /note="Serine/threonine-protein kinase TOR1"
FT /id="PRO_0000456202"
FT REPEAT 114..151
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 248..286
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 627..664
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 663..701
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 746..784
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 787..826
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 829..870
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 907..946
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 949..987
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1109..1147
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT DOMAIN 1331..1919
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT REPEAT 1869..1907
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT DOMAIN 2093..2408
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2438..2470
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1775..2157
FT /note="Interaction with FKBP-rapamycin"
FT /evidence="ECO:0000250|UniProtKB:P35169"
FT REGION 2099..2105
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2272..2280
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2292..2317
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 2470 AA; 281205 MW; 0B41A1BEC37CF6DE CRC64;
MEPHEEQIWK SKLLKAANND MDMDRNVPLA PNLNVNMNMK MNASRNGDEF GLTSSRFDGV
VIGSNGDVNF KPILEKIFRE LTSDYKEERK LASISLFDLL VSLEHELSIE EFQAVSNDIN
NKILELVHTK KTSTRVGAVL SIDTLISFYA YTERLPNETS RLAGYLRGLI PSNDVEVMRL
AAKTLGKLAV PGGTYTSDFV EFEIKSCLEW LTASTEKNSF SSSKPDHAKH AALLIITALA
ENCPYLLYQY LNSILDNIWR ALRDPHLVIR IDASITLAKC LSTLRNRDPQ LTSQWVQRLA
TSCEYGFQVN TLECIHASLL VYKEILFLKD PFLNQVFDQM CLNCIAYENH KAKMIREKIY
QIVPLLASFN PQLFAGKYLH QIMDNYLEIL TNAPAKKIPH LKDDKPQILI SIGDIAYEVG
PDIAPYVKQI LDYIEHDLQT KFKFRKKFEN EIFYCIGRLA VPLGPVLGKL LNRNILDLMF
KCPLSDYMQE TFQILTERIP SLGPKINDEL LNLVCSTLSG TPFIQPGSPM EIPSFSRERA
REWRNKSILQ KTGESNDDNN DIKIIIQAFR MLKNIKSRFS LVEFVRIVAL SYIEHTDPRV
RKLAALTSCE IYVKDNICKQ TSLHSLNTVS EVLSKLLAIT IADPLQDIRL EVLKNLNPCF
DPQLAQPDNL RLLFIALHDE SFNIQSVAME LVGRLSSVNP AYVIPSIRKI LLELLTKLKF
STSSREKEET ASLLCTLIRS SKDVAKPYIE PLLNVLLPKF QDTSSTVAST ALRTIGELSV
VGGEDMKIYL KDLFPLIIKT FQDQSNSFKR EAALKALGQL AASSGYVIDP LLDYPELLGI
LVNILKTENS QNIRRQTVTL IGILGAIDPY RQKEREVTST TDISTEQNAP PIDIALLMQG
MSPSNDEYYT TVVIHCLLKI LKDPSLSSYH TAVIQAIMHI FQTLGLKCVS FLDQIIPTIL
DVMRTCSQSL LEFYFQQLCS LIIIVRQHIR PHVDSIFQAI KDFSSVAKLQ ITLVSVIEAI
SKALEGEFKR LVPLTLTLFL VILENDKSSD KVLSRRVLRL LESFGPNLEG YSHLITPKIV
QMAEFTSGNL QRSAIITIGK LAKDVDLFEM SSRIVHSLLR VLSSTTSDEL SKVIMNTLSL
LLIQMGTSFA IFIPVINEVL MKKHIQHTIY DDLTNRILNN DVLPTKILEA NTTDYKPAEQ
MEAADAGVAK LPINQSVLKS AWNSSQQRTK EDWQEWSKRL SIQLLKESPS HALRACSNLA
SMYYPLAKEL FNTAFACVWT ELYSQYQEDL IESLCIALSS PLNPPEIHQT LLNLVEFMEH
DDKALPIPTQ SLGEYAERCH AYAKALHYKE IKFIKEPENS TIESLISINN QLNQTDAAIG
ILKHAQQHHS LQLKETWFEK LERWEDALHA YNEREKAGDT SVSVTLGKMR SLHALGEWEQ
LSQLAARKWK VSKLQTKKLI APLAAGAAWG LGEWDMLEQY ISVMKPKSPD KEFFDAILYL
HKNDYDNASK HILNARDLLV TEISALINES YNRAYSVIVR TQIITEFEEI IKYKQLPPNS
EKKLHYQNLW TKRLLGCQKN VDLWQRVLRI RSLVIKPKQD LQIWIKFANL CRKSGRMRLA
NKALNMLLEG GNDPSLPNTV KAPPPVVYAQ LKYIWATGAY KEALNHLIGF TSRLAHDLGL
DPNNMIAQSV KLSSASTAPY VEEYTKLLAR CFLKQGEWRI ATQPNWRNTN PDAILGSYLL
ATHFDKNWYK AWHNWALANF EVISMVQEET KLNGGKNDDD DDTAVNNDNV RIDGSILGSG
SLTINGNRYP LELIQRHVVP AIKGFFHSIS LLETSCLQDT LRLLTLLFNF GGIKEVSQAM
YEGFNLMKIE NWLEVLPQLI SRIHQPDPTV SNSLLSLLSD LGKAHPQALV YPLTVAIKSE
SVSRQKAALS IIEKIRIHSP VLVNQAELVS HELIRVAVLW HELWYEGLED ASRQFFVEHN
IEKMFSTLEP LHKHLGNEPQ TLSEVSFQKS FGRDLNDAYE WLNNYKKSKD INNLNQAWDI
YYNVFRKITR QIPQLQTLDL QHVSPQLLAT HDLELAVPGT YFPGKPTIRI AKFEPLFSVI
SSKQRPRKFS IKGSDGKDYK YVLKGHEDIR QDSLVMQLFG LVNTLLKNDS ECFKRHLDIQ
QYPAIPLSPK SGLLGWVPNS DTFHVLIREH RDAKKIPLNI EHWVMLQMAP DYENLTLLQK
IEVFTYALDN TKGQDLYKIL WLKSRSSETW LERRTTYTRS LAVMSMTGYI LGLGDRHPSN
LMLDRITGKV IHIDFGDCFE AAILREKYPE KVPFRLTRML TYAMEVSGIE GSFRITCENV
MRVLRDNKES LMAILEAFAL DPLIHWGFDL PPQKLTEQTG IPLPLINPSE LLRKGAITVE
EAANMEAEQQ NETRNARAML VLRRITDKLT GNDIKRFNEL DVPEQVDKLI QQATSIERLC
QHYIGWCPFW
