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Serine/threonine-protein kinase tor (EC 2.7.11.1) (Target of rapamycin)

 TOR_DICDI               Reviewed;        2380 AA.
Q86C65; Q54TG2;
26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
23-MAY-2018, entry version 117.
RecName: Full=Serine/threonine-protein kinase tor;
EC=2.7.11.1;
AltName: Full=Target of rapamycin;
Name=tor; ORFNames=DDB_G0281569;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12626495; DOI=10.1074/jbc.M212467200;
Otto G.P., Wu M.Y., Kazgan N., Anderson O.R., Kessin R.H.;
"Macroautophagy is required for multicellular development of the
social amoeba Dictyostelium discoideum.";
J. Biol. Chem. 278:17636-17645(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[3]
FUNCTION, IDENTIFICATION IN A TORC1 AND TORC2 COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16079174; DOI=10.1091/mbc.E05-04-0342;
Lee S., Comer F.I., Sasaki A., McLeod I.X., Duong Y., Okumura K.,
Yates J.R. III, Parent C.A., Firtel R.A.;
"TOR complex 2 integrates cell movement during chemotaxis and signal
relay in Dictyostelium.";
Mol. Biol. Cell 16:4572-4583(2005).
[4]
FUNCTION.
Rosel D., Majithia A., Khurana T., Kimmel A.R.;
"TOR, the central controller of cell growth negatively regulates
phagocytosis.";
(In) Abstracts of Annual International Dictyostelium Conference,
pp.18-18, Autrans (2005).
[5]
DISRUPTION PHENOTYPE.
PubMed=18657484; DOI=10.1016/j.arr.2008.04.003;
McMains V.C., Liao X.-H., Kimmel A.R.;
"Oscillatory signaling and network responses during the development of
Dictyostelium discoideum.";
Ageing Res. Rev. 7:234-248(2008).
[6]
FUNCTION.
PubMed=18812082; DOI=10.1016/j.cub.2008.07.051;
King J.S., Insall R.H.;
"Chemotaxis: TorC before you Akt.";
Curr. Biol. 18:R864-R866(2008).
[7]
FUNCTION.
PubMed=18635356; DOI=10.1016/j.cub.2008.06.068;
Kamimura Y., Xiong Y., Iglesias P.A., Hoeller O., Bolourani P.,
Devreotes P.N.;
"PIP3-independent activation of TorC2 and PKB at the cell's leading
edge mediates chemotaxis.";
Curr. Biol. 18:1034-1043(2008).
-!- FUNCTION: Regulates cell growth, chemotaxis, signal relay and the
actin cytoskeleton. Functions as a part of 2 distinct protein
complexes TORC1 and TORC2. TORC1 is a rapamycin-sensitive complex
that controls cell growth in response to nutrients and growth
factors. The second TOR complex, TORC2, is presumed to be
indirectly negatively modulated by rapamycin and regulates actin
polarization. TORC2 but not TORC1 negatively regulates
phagocytosis. TORC2-dependent regulation of the cytoskeleton may
follow differential phosphorylation of pkbA. May have some protein
kinase activity, as it appears to phosphorylate pkgB.
{ECO:0000269|PubMed:16079174, ECO:0000269|PubMed:18635356,
ECO:0000269|PubMed:18812082, ECO:0000269|Ref.4}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Part of a complex, TORC1, consisting of tor, raptor and
lst8. Part of a complex, TORC2, consisting of tor, lst8, piaA and
ripA. Additional proteins, such as 14-3-3 and heat-shock proteins,
may also belong to the TORC2 complex.
{ECO:0000269|PubMed:16079174}.
-!- DISRUPTION PHENOTYPE: Null cells are lethal due to a growth defect
involving TOR protein complex 1, TORC1.
{ECO:0000269|PubMed:18657484}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY204354; AAO43977.1; -; Genomic_DNA.
EMBL; AAFI02000042; EAL66546.1; -; Genomic_DNA.
RefSeq; XP_640629.1; XM_635537.1.
ProteinModelPortal; Q86C65; -.
STRING; 44689.DDB0214908; -.
PaxDb; Q86C65; -.
PRIDE; Q86C65; -.
EnsemblProtists; EAL66546; EAL66546; DDB_G0281569.
GeneID; 8623240; -.
KEGG; ddi:DDB_G0281569; -.
dictyBase; DDB_G0281569; tor.
eggNOG; KOG0891; Eukaryota.
eggNOG; COG5032; LUCA.
InParanoid; Q86C65; -.
KO; K07203; -.
OMA; SSHQGLM; -.
PhylomeDB; Q86C65; -.
Reactome; R-DDI-3371571; HSF1-dependent transactivation.
PRO; PR:Q86C65; -.
Proteomes; UP000002195; Chromosome 3.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005829; C:cytosol; IDA:dictyBase.
GO; GO:0005634; C:nucleus; IDA:dictyBase.
GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
GO; GO:0031932; C:TORC2 complex; IPI:dictyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:1903664; P:regulation of asexual reproduction; IMP:dictyBase.
GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 1.20.120.150; -; 1.
Gene3D; 1.25.10.10; -; 4.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR024585; DUF3385_TOR.
InterPro; IPR003152; FATC_dom.
InterPro; IPR009076; FRB_dom.
InterPro; IPR036738; FRB_sf.
InterPro; IPR021133; HEAT_type_2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR003151; PIK-rel_kinase_FAT.
InterPro; IPR014009; PIK_FAT.
InterPro; IPR026683; TOR.
PANTHER; PTHR11139:SF9; PTHR11139:SF9; 1.
Pfam; PF11865; DUF3385; 1.
Pfam; PF02259; FAT; 1.
Pfam; PF02260; FATC; 1.
Pfam; PF08771; FRB_dom; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
SMART; SM01346; DUF3385; 1.
SMART; SM01343; FATC; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF47212; SSF47212; 1.
SUPFAM; SSF48371; SSF48371; 6.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51189; FAT; 1.
PROSITE; PS51190; FATC; 1.
PROSITE; PS50077; HEAT_REPEAT; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Chemotaxis; Coiled coil; Complete proteome;
Kinase; Nucleotide-binding; Reference proteome; Repeat;
Serine/threonine-protein kinase; TPR repeat; Transferase.
CHAIN 1 2380 Serine/threonine-protein kinase tor.
/FTId=PRO_0000376000.
REPEAT 266 303 HEAT 1.
REPEAT 493 530 HEAT 2.
REPEAT 540 578 HEAT 3.
REPEAT 580 614 HEAT 4.
REPEAT 660 697 HEAT 5.
REPEAT 701 739 HEAT 6.
REPEAT 745 783 HEAT 7.
REPEAT 863 900 HEAT 8.
REPEAT 982 1021 HEAT 9.
REPEAT 1023 1060 HEAT 10.
REPEAT 1210 1249 HEAT 11.
REPEAT 1255 1288 TPR 1.
DOMAIN 1260 1790 FAT. {ECO:0000255|PROSITE-
ProRule:PRU00534}.
REPEAT 1316 1349 TPR 2.
REPEAT 1611 1644 TPR 3.
REPEAT 1672 1706 TPR 4.
REPEAT 1942 1974 TPR 5.
DOMAIN 1990 2380 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 2348 2380 FATC. {ECO:0000255|PROSITE-
ProRule:PRU00534, ECO:0000255|PROSITE-
ProRule:PRU00535}.
COILED 11 38 {ECO:0000255}.
COMPBIAS 1395 1399 Poly-Ala.
SEQUENCE 2380 AA; 268750 MW; 5E2998128B92711E CRC64;
MSQHEQPSIW ADALTKLLND LKSKKEEDRV KASKNLKSYV ISQSREMTNE NFTKFMNELN
NNLIFELVNS SVIPEKIGGI MAIDELIDVD YDENATKITR LANYLRIGLG FNDFTVMLMA
SKALGRLARS SGTLTAEFVE FEVTRALEWL SGDRIEARRH AAVLVLKELA QNAPTLFYVH
ASSFVDLIWV ALKDPKVAIR EGAVEALRAC LELISERESR LRLQWYQKIY DEAQKSFKQN
GSPESIHGSL ITVSELLRNT GDFMLSKFKD ICETVLKYKD HRDKLVKKTV LALFPRLAVF
CSRDFVLNYF NACMNHLLAA LRNQNERPTA FIALGEIAMA VGGSIKPYLD SIVVMIKQGL
MTKGKQFCPE VLTCISMLAS AVGQSMYPHM QVILPQMIVS SGLTVVLTDA LRDLTINLPT
LIPNIQYKLL NLISQVLANK PFSEPGAPSP YRKSATPFQG GSIPQLGQNS DVDPQMIALA
LKTLGSFDFS KHNLLEFVRE CVVNYLDDDN IEIRREAAIT CAQLMVGTEE PTPTRGHSAV
IVGEVLEKLL VVGIADPDPS IRKTVLSSLE ARFDHYLAQA ENLRSLFIAL NDELFEIREL
AITVIGRLTI RNPAYVMPSL RKTLIQLLTE LEFSGDGRNK EESARLLGHL ISASEKLIKP
YVEPILKALL PKLRDSNPRV ASCVLAALGE LSVVGGEEMV QHIDSLLPLI IDTLQDQSST
SKREVALKTL AQLASSTGYV IKPFSKYPML LDTLLNAIKT ERIGSIRREV IKVLGILGSL
DPYKHKMNEL GKRREDPKAN DDKNNNMTNE VITISPSNED YYPTVALTAL MKILRDPSLS
SHHTSVIQAV MYIFKSLSLK SIPFLPQIMP PFLHAMNTGE PLFREFLFQQ LGSLVSIVKQ
HIRDYLVNVF ALIEKYWNSN LLIPIIKLVE EISSALNDEF KVYLPNLIPQ MLNVLHTDRS
PKRSPTTKVL RALEVFGTNL DDYLHLVIPA IVKLFEQVDV TTQVRTLAIQ TIGRLCKKLN
FSDYASRIIH PLARVLDSTE SELREETLNT LCALVYQLGS DYAIFIPMVG KVLARREIQS
TNYELLISKL LKNQQLMLTP GSGDDGGMGA NRFGGDHNGH HLGEDHNNTS TPLDIGVKKL
KANEQHLKNA WETSQRSTKE DWGEWIRRFS VELLRESPSP ALRSCLSLAQ DYHPLVKELF
NAGFVSCWTE LHEQFQEELV RSLETALLSP NIPPEILQTL LNLAEFMELH EKPLPIDIRT
LGALAEKCHA YAKALHYKES EFSQSPSSTI EALISINNQL QQPEAAIGIL IYAQKNHSVE
LKEGWYEKLR RWEDALAAYE KKQKDDPNGG TIENTMGILR CLHALGEWER LSALSSETWK
SDINDHTRAT IAPLAAAAAW NLVNWDKMDE YVCAMNKDTV EGSFYRAILE VHHDNFTLAH
GFIDHARTLV DTELTALLGE SYNRAYKVVV RLQQLSELEE IIEYKKCVDS PERRNMIKNT
WKTRLRGCQH NVDIWQSILA VHSLVISPHE ELDMWLKFVG LCRKGSRLGL AQKTLTMLMG
KDPSTTSQFG SVLPNTHPRI TFAYIKQLWS AGAKQPAFEK LRTFVQALRD TDDLPLQGRA
YLKLGEWQLA LGDTLSEASI PHIISSFKAA TECDPNWYKA WHSWALINFE VVSHYEQNGG
TPEQIGAHLL PAVHSFFKSI SLGPDRSLQD TLRLLTLWFK HGAQKEVEAA LMQGFNTISI
DTWLHVIPQI IARIHAPVLP VRRLLHELID TIGKEHPQAL VYPLTVATKS HSPARLAAAK
SLMDKMRKHS ATLVDQALPV SQELVRTAIL WLEMWYEGLE EASRQYFGDH NPEAMLATLA
PLHQILEKGP ETTSETSFLQ AFGRDLQEAL EWSKKYEKTR KEGDLNQAWD LYYQVFRRIY
KQLPQMSSLE LQYVSPKLLN SNNMELAVPG TYKASENVIR IQSFSQALSV IPSKQRPRKL
TIIGSDGLEY TFLLKGHEDL RQDERVMQLF SLVNNLLSAN HETAKSHLSI RRFSVIPLSP
NSGLIGWVPH SDTLHTLIKD FRDSNKILLS IEHRLMLQMC SDYDNLTLLQ KVEVFQYALE
NSNGLDLHKV LWLKSRNSEV WLDRRTNYTR SLAVMSMVGY ILGLGDRHPS NLMLDRHTGH
ILHIDFGDCF EVAMHRDKYP EKIPFRLTRM LINAMEVSGI EGNFRLTCEA VMNVLRNNKE
SLMAVLEAFV HDPLINWRLL TPNENNTKHK ATNIASNNST SNSTTKIEGD LNTIDNPINK
ESPDHEAVAG SLKSSPVHGR QIARNQRVGV DAEQVEAEIV PEALNERALS VINRVNKKLT
GRDFSSNETL DVPEQVQKLI DQATSHENLC LSYVGWCPFW


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