TOR_ORYSJ
ID TOR_ORYSJ Reviewed; 2465 AA.
AC Q0DJS1; A0A077KAU4; A0A0P0WJP4; B7F5Y4; Q6ATH2;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305|PubMed:28230163};
DE AltName: Full=Protein TARGET OF RAPAMYCIN {ECO:0000303|PubMed:25956502};
DE Short=OsTOR {ECO:0000303|PubMed:25956502};
GN Name=TOR {ECO:0000303|PubMed:25956502};
GN OrderedLocusNames=Os05g0235300 {ECO:0000312|EMBL:BAS92935.1},
GN LOC_Os05g14550 {ECO:0000305};
GN ORFNames=OSJNBa0093E24.9 {ECO:0000312|EMBL:AAT93990.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RX PubMed=25956502; DOI=10.1007/s00438-015-1056-0;
RA Maegawa K., Takii R., Ushimaru T., Kozaki A.;
RT "Evolutionary conservation of TORC1 components, TOR, Raptor, and LST8,
RT between rice and yeast.";
RL Mol. Genet. Genomics 290:2019-2030(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1039-2465.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=28230163; DOI=10.1038/srep42835;
RA Bakshi A., Moin M., Kumar M.U., Reddy A.B., Ren M., Datla R., Siddiq E.A.,
RA Kirti P.B.;
RT "Ectopic expression of Arabidopsis Target of Rapamycin (AtTOR) improves
RT water-use efficiency and yield potential in rice.";
RL Sci. Rep. 7:42835-42835(2017).
CC -!- FUNCTION: Component of TORC1 complex, which is an essential cell growth
CC regulator that controls plant development. Acts through the
CC phosphorylation of downstream effectors that are recruited by the
CC binding partner RAPTOR. Acts by activating transcription, protein
CC synthesis and ribosome biogenesis, and inhibiting mRNA degradation and
CC autophagy. {ECO:0000305|PubMed:25956502}.
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:0000305|PubMed:28230163};
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:0000305|PubMed:28230163};
CC -!- ACTIVITY REGULATION: Insensitive to inhibition by rapamycin.
CC {ECO:0000269|PubMed:28230163}.
CC -!- SUBUNIT: The target of rapamycin complex 1 (TORC1) is composed of at
CC least RAPTOR, LST8 and TOR. {ECO:0000305|PubMed:25956502}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT93990.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF16902.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAH00032.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAS92935.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB982929; BAP28447.1; -; mRNA.
DR EMBL; AC136223; AAT93990.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008211; BAF16902.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; BAS92935.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK120473; BAH00032.1; ALT_INIT; mRNA.
DR RefSeq; XP_015639567.1; XM_015784081.1.
DR AlphaFoldDB; Q0DJS1; -.
DR SMR; Q0DJS1; -.
DR STRING; 4530.OS05T0235300-01; -.
DR PaxDb; Q0DJS1; -.
DR PRIDE; Q0DJS1; -.
DR EnsemblPlants; Os05t0235300-01; Os05t0235300-01; Os05g0235300.
DR GeneID; 4338174; -.
DR Gramene; Os05t0235300-01; Os05t0235300-01; Os05g0235300.
DR KEGG; osa:4338174; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_1_1; -.
DR InParanoid; Q0DJS1; -.
DR OrthoDB; 26975at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q0DJS1; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; IEA:EnsemblPlants.
DR GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR GO; GO:0031932; C:TORC2 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblPlants.
DR GO; GO:0043621; F:protein self-association; IEA:EnsemblPlants.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:EnsemblPlants.
DR GO; GO:0016311; P:dephosphorylation; IEA:EnsemblPlants.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR GO; GO:0009630; P:gravitropism; IEA:EnsemblPlants.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IEA:EnsemblPlants.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:0010116; P:positive regulation of abscisic acid biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0010929; P:positive regulation of auxin mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:1900459; P:positive regulation of brassinosteroid mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:EnsemblPlants.
DR GO; GO:0040019; P:positive regulation of embryonic development; IEA:EnsemblPlants.
DR GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IEA:EnsemblPlants.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:EnsemblPlants.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IEA:EnsemblPlants.
DR GO; GO:1901355; P:response to rapamycin; IEA:EnsemblPlants.
DR GO; GO:0009615; P:response to virus; IEA:EnsemblPlants.
DR GO; GO:0009303; P:rRNA transcription; IEA:EnsemblPlants.
DR GO; GO:0009745; P:sucrose mediated signaling; IEA:EnsemblPlants.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
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:SF112; PTHR11139:SF112; 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 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Growth regulation; Kinase;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2465
FT /note="Serine/threonine-protein kinase TOR"
FT /id="PRO_0000409331"
FT REPEAT 184..221
FT /note="HEAT 1"
FT REPEAT 271..308
FT /note="HEAT 2"
FT REPEAT 348..389
FT /note="HEAT 3"
FT REPEAT 549..587
FT /note="HEAT 4"
FT REPEAT 588..625
FT /note="HEAT 5"
FT REPEAT 717..755
FT /note="HEAT 6"
FT REPEAT 761..799
FT /note="HEAT 7"
FT REPEAT 888..926
FT /note="HEAT 8"
FT REPEAT 981..1018
FT /note="HEAT 9"
FT REPEAT 1022..1059
FT /note="HEAT 10"
FT REPEAT 1061..1098
FT /note="HEAT 11"
FT DOMAIN 1297..1877
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2051..2369
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2433..2465
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 1158..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2057..2063
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2230..2238
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2250..2275
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2401..2431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2401..2422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 153
FT /note="G -> L (in Ref. 1; BAP28447)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..316
FT /note="RDRFVTNYLK -> KDRHIKSYSQ (in Ref. 1; BAP28447)"
FT /evidence="ECO:0000305"
FT CONFLICT 422..425
FT /note="SIPS -> RYYF (in Ref. 1; BAP28447)"
FT /evidence="ECO:0000305"
FT CONFLICT 592..593
FT /note="DI -> EL (in Ref. 1; BAP28447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2465 AA; 276787 MW; 6EFDE316494D11FA CRC64;
MKPSPHFPEI GKKPKDLIAK EHGFNIAAYI SSGADVIAAA LRKHVEEEAR DLSGEAFLRF
MEQLYEQICS LLQSNDVAEN LLALRAIDAL IDMPFGEGAS KVSKFANFLR TVFEVKRDPE
VLVPASAVLG HLAKAGGAMT ADEVERQIKT ALGWLGGDRV EYRRFASVLI LKEMAENAST
VFNVHVPEFV DAIWVALRDP KQAVRERAVE ALRACLHVIE KRETRWRVQW YYRMCEAAQV
GLGKNASVHS IHGSLLAVGE LLRNTGEFMM SRYREVADIV LNYLRHRDQL VRRSITSLLP
RIAHFLRDRF VTNYLKICMD HILFVLRTPD ERASGFVALG EMAGALGAEL VPYLPLITSH
LHDAIAPRRG RPSLEAISCV GSFAKAMGPA MEPHIRGGLL DAMFSAGLSD KLVEALESIS
TSIPSLLPTI QERLLDCISQ ALPKSSVRPG AAVGRGSRSS SLQQFVDSGG PVLVQLALGT
LANFNFKGHE LLEFARESVI LYLEDEDCST RKAAATCCCK LVAHSLSASS SSQFSSNRPN
RMGGAKRRRL VEEIVEKLLM AAVADADVGV RSSVFKALYR NPSFDDFLAQ ADIMTSIFVA
LNDEEYHVRE LAISVAGRLS EKNPAYVLPA LRRYLIQLLT YLDQSMDSKC REESARLLGC
LIRSCARLIL PYIAPIHKAL VARLREGTGP NANNALAAGV LATVGELAKV GGFAMRQYLP
ELMPLVVDAL LDGGAVSKRE VAVATLGQVI QSTGYVISPY NEYPPLLGLL LKLLNGELEW
STRLEVLKVL GIMGALDPHA HKRNQHKLPG QHREVLRPTM ETAQHIVSME ELPTDFWPSF
SASEDYYSTV AISSLMRILH DPSLSSYHQM VVGSLIFIFK SMGLGCVPYL PKVLPELFRA
VRMCEDGGLK EFITWKLGTL VSIVRQHIRK YLQEILSLVS ELWTSSFSLP APNRTVQGPQ
ASPVLHLVEQ LCLALNDEFR MYILHILPSC IQVLGDAERC NDYYYVPDIL HTLEVFGGNL
DEHMHLVAPV LVRLFKVELV DIRRRAIVTL TKLIPTVQVG THVSVLVHHL KLVLDGNNDD
LRKDAAEALC CLAHALGEDF TIFVSSIHKL LVKHHMRYRK WDEIENRLLR REPLISENLS
VQKYTQCPPE VISDPLDDFG GVPSEEADET QRQPRSHQVN DVRLRSAGEA SQRSTREDWA
EWMRHFSIAL LKESPSPALR TCARLAQLQP SVGRELFAAG FASCWAQMNE TSQEQLVRSL
KTAFSSQNIP PEILATLLNL AEFMEHDEKP LPIDTRLLGA LAEKCRAFAK ALHYKEMEFE
AVCSKKMGAN PVTVVESLIH INNQLHQHEA AIGILTYSQQ HLEVQLKESW YEKLHRWDEA
LKAYKAKSSQ ASGPLQNLDA TLGRMRCLAA LARWEDLSAL CREQWTGSEP SARLEMAPMA
ANAAWHMGEW DHMAEYVSRL DDGDENKLRI LGNTTASGDG SSNGAFFRAV LSVRCKKYEE
ARVYVERARR CLATELAALV LESYERAYNN MVRVQQLSEL EEVIDYCTLP MESPIADSRR
ELIRNMWNER IKGTKRNVEV WQALLAVREL VLPPNEDRDT WIKFAKLCWK SGRISQAKST
LVKLLQFDPE SSPELTLYHG HPQVVLAYLK YQYAVGDELK RRDAFCRLQD LSVQLATATN
SYSGTLASQV ATSNAGVPLI ARVYLTLASW KRALSPGLDD DSIQEILVSY KNATLNAKDW
GKAWHLWALF NTEVMSRYTL RGRPDIAGKY VVAAVTGYFY SIACASTTKG VDDSLQDILR
LLTLWFNHGA TSEVQMALQK GFSLVNIEMW LVVLPQIIAR IHSNNKIVRE LIQSLLVRIG
KDHPQALMYP LLVACKSISI LRQRAAQEVV DKIRQHSGGL VDQAQLVSKE LIRVAILWHE
MWHEALEEAS RMYFGEHNIE GMLAVLEPLH AMLERGPETI KENTFIQAYG HELLEAHECC
LKYRATGEDA ELTKAWDLYY HVFRRIDKQL PSLTTLDLHS VSPELLECRK LELAVPGTYS
ADAPLVTIEY FVPQLIVITS KQRPRKLTIH GSDGNDYAFL LKGHEDLRQD ERVMQLFGLV
NTLLENSRKT SEKDLSIQRY AVIPLSPNSG LIGWVPNCDT LHALIREYRD ARKIFLNQEH
RCMLSFAPDY DHLPLIAKVE VFQHALENSE GNDLAKVLWL KSRTSEVWLE RRTNYTRSLA
VMSMVGYLLG LGDRHPSNLM LDRYSGKILH IDFGDCFEAS MNREKFPEKV PFRLTRMLVK
AMEVSGIEGT FRTTCENVMQ VLRTNKDSVM AMMEAFVHDP LINWRLFNFN EVPQVTNYGN
AHSHTVVNSE EAANRELMQP PRGARERELL QAVNQLGDAN EVLNERAVAV MARMSHKLTG
RDFSSGSSLS GAGSSTQHGN EHLASGDTRE VEPGLSVKVQ VQRLILQATS HENLCQNYVG
WCPFW
