ID F1NUX4_CHICK Unreviewed; 2521 AA.
AC F1NUX4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN Name=MTOR {ECO:0000313|Ensembl:ENSGALP00010031768.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010031768.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010031768.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010031768.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775,
CC ECO:0000256|RuleBase:RU364109};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
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DR RefSeq; XP_417614.3; XM_417614.5.
DR SMR; F1NUX4; -.
DR STRING; 9031.ENSGALP00000005274; -.
DR PaxDb; 9031-ENSGALP00000005274; -.
DR Ensembl; ENSGALT00010052862.1; ENSGALP00010031768.1; ENSGALG00010021746.1.
DR GeneID; 419455; -.
DR KEGG; gga:419455; -.
DR CTD; 2475; -.
DR VEuPathDB; HostDB:geneid_419455; -.
DR GeneTree; ENSGT00930000151037; -.
DR InParanoid; F1NUX4; -.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR Reactome; R-GGA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-GGA-1632852; Macroautophagy.
DR Reactome; R-GGA-165159; MTOR signalling.
DR Reactome; R-GGA-166208; mTORC1-mediated signalling.
DR Reactome; R-GGA-3371571; HSF1-dependent transactivation.
DR Reactome; R-GGA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-GGA-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-GGA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-GGA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-GGA-6804757; Regulation of TP53 Degradation.
DR Reactome; R-GGA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-GGA-9639288; Amino acids regulate mTORC1.
DR Proteomes; UP000000539; Chromosome 21.
DR Bgee; ENSGALG00000003339; Expressed in testis and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR GO; GO:0001002; F:RNA polymerase III type 1 promoter sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0001003; F:RNA polymerase III type 2 promoter sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0001156; F:TFIIIC-class transcription factor complex binding; IEA:Ensembl.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:Ensembl.
DR GO; GO:0048266; P:behavioral response to pain; IEA:Ensembl.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0071233; P:cellular response to leucine; IEA:Ensembl.
DR GO; GO:1990253; P:cellular response to leucine starvation; IEA:Ensembl.
DR GO; GO:0031670; P:cellular response to nutrient; IEA:Ensembl.
DR GO; GO:0006112; P:energy reserve metabolic process; IEA:Ensembl.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR GO; GO:0003179; P:heart valve morphogenesis; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR GO; GO:0016236; P:macroautophagy; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR GO; GO:0045792; P:negative regulation of cell size; IEA:Ensembl.
DR GO; GO:1905672; P:negative regulation of lysosome organization; IEA:Ensembl.
DR GO; GO:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0051647; P:nucleus localization; IEA:Ensembl.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IEA:Ensembl.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IEA:Ensembl.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IEA:Ensembl.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:Ensembl.
DR GO; GO:1903691; P:positive regulation of wound healing, spreading of epidermal cells; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IEA:Ensembl.
DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IEA:Ensembl.
DR GO; GO:0090559; P:regulation of membrane permeability; IEA:Ensembl.
DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0031529; P:ruffle organization; IEA:Ensembl.
DR GO; GO:0002296; P:T-helper 1 cell lineage commitment; IEA:Ensembl.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR GO; GO:0038202; P:TORC1 signaling; IEA:Ensembl.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; IEA:Ensembl.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
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_cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 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 SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364109};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364109};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364109};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1NUX4};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU364109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
SQ SEQUENCE 2521 AA; 286722 MW; 0057499F8388AB71 CRC64;
MSGTVSILQQ FANGLKSRSE ETRAKAAKDL QHYVTMELRE MSQEESTRFY DQLNHHIFEL
VSSSDANERK GGILAIASLI GVEGGNATRI GRFANYLRNL LPSNDPVVME MASKAIGRLA
MAGDTFTAEY VEFEVKRALE WLGADRNEGR RHAAVLVLRE LAISVPTFFF QQVQPFFDNI
FVAVWDPKQA IREGAVSALR ACLILTTQRE PKEMQKPQWY RHTYEEAEKG FDETLAKEKG
MNRDDRIHGA LLILNELVRI SSMEGERLRE EMEEITQQQL VHDKYCKDLM GFSTKPRHIT
PFTSFQSLQP SQSNALAGLL GYNAHQGIMG FATSPMPAKS TLVESRCCRD LMEEKFDQVC
QWVLKCRTSK NSLIQMTVLN LLPRLAAFRP SAFTADQYLP DTMNHVLSCV KKEKERTAAF
QALGLLSVAV RSEFQAYLPK VLEIIKAALP PKDFAHKRQK SVQVDATVFT CISMLARAMG
PSIQQDIKEL LEPMLAVGLS PALTAVLYDL SRQIPQLKKD IQDGLLKMLS LVLMHKPLRH
PGMPKGLAHQ LASPSLTNIP EASDVGSITL ALRTLGSFEF EGHSLTQFVR HCADHFLNSE
HKEIRMEAAR TCSRLLTPSI HLISGHAHVV SQTAVQVVAD VLSKLLVVGI TDPDPDIRFC
VLASLDERFD AHLAQAENLQ ALFVALNDQV FEIRELAICT VGRLSSMNPA FVMPFLRKML
IQILTELEHS GVGRIKEQSA RMLGHLVSNA PRLIRPYMEP ILKALIVKLK DPDPDPNPGV
INNVLATIGE LAQVSGLEMR KWVDELFIII MDMLQDSSLL AKRQVALWTL GQLVASTGYV
VEPYRKYPTL LEVLLNFLKT EQNQGTRREA IRVLGLLGAL DPYKHKVNIG MIDQSRDASA
VSLSESKSSQ DSSDYSTSEM LVNMGNLPLD EFYPAVSMVA LMRIFRDQSL SQHHTMVVQA
ITFIFKSLGL KCVQFLPQVM PTFLNVIRVC DGAIREFLFQ QLGMLVSFVR SHIRPYMDEI
VTLMRDFWVM NNSIQSTIIL LIEQIVVALG GEFKLYLPQL IPHMLRVFMH DNSQSRIVSV
KLLNAIQLFG ANLDDYLHLL LPPIVKLFDA PDAPVVARKA ALETVDRLTE SLDFTDYASR
IIHPIVRTLD QSPELRTTAM DTLSSLVFQL GKKYQIFIPM VNKVLVRHRI NHQRYDVLIC
RIVKGYTLAD EEEDPLIYQH RMLRSNQGET LASGPVETGP MKKLHVSTIN LQKAWGAARR
VSKDDWLEWL RRLSLELLKD SSSPSLRSCW ALAQAYNPMA RDLFNAAFVS CWSELNEDQQ
DELIRSIELA LTSQDIAEVT QTLLNLAEFM EHSDKGPLPL RDDNGIVLLG ERAAKCRAYA
KALHYKELEF QKGPTPAILE SLISINNKLQ QPEAAAGVLE YAMKHFGELE IQATWYEKLH
EWEDALVAYD KKMDTNKDDP ELMLGRMRCL EALGEWGQLH QQCCEKWTQV NDETQAKMAR
MAAAAAWGLG QWDSMEEYTC MIPRDTHDGA FYRAVLALHQ DLFSLAQQCI DKARDLLDAE
LTAMAGESYS RAYGAMVSCQ MLSELEEVIQ YKLVPERREI IRQIWWERLQ GCQRIVEDWQ
RILMVRSLVV NPHEDMRTWL KYASLCGKSG RLALAHKTLV LLLGVDPSRQ LDHPLPTVHP
QVTYAYMKHM WKSARKIDAF QHMQHFVQTM QQQAQHAIAT EDQQHKQELH KLMARCFLKL
GEWQLNLQGI NESTIPKVLQ YYSAATEHDR NWYKAWHAWA VMNFEAVLHY KHQNQARDEK
KKLRHASGAS ITSANTEGSN SESDAESTEN SPIPSPVQKK VTEDLSKTLL MYTVPAVQGF
FRSISLSRGN NLQDTLRVLT LWFDYGHWPD VNEALVEGVK AIQIDTWLQV IPQLIARIDT
PRPLVGRLIH QLLTDIGRYH PQALIYPLTV ASKSTTTARH NAANKILKNM CEHSNTLVQQ
AMMVSEELIR VAILWHEMWH EGLEEASRLY FGERNVKGMF EVLEPLHAMM ERGPQTLKET
SFNQAYGRDL MEAQEWCRKY MKSGNVKDLT QAWDLYYHVF RRISKQLPQL TSLELQYVSP
KLLMCRDLEL AVPGTYDPNQ PIIRIQSIAP SLQVITSKQR PRKLTLMGSN GHEFVFLLKG
HEDLRQDERV MQLFGLVNTL LANDPTSLRK NLSIQRYAVI PLSTNSGLIG WVPHCDTLHA
LIRDYREKKK ILLNIEHRIM LRMAPDYDHL TLMQKVEVFE HAVNNTAGDD LAKLLWLKSP
SSEVWFDRRT NYTRSLAVMS MVGYILGLGD RHPSNLMLDR LSGKILHIDF GDCFEVAMTR
EKFPEKIPFR LTRMLTNAME VTGLDGNYRI TCHTVMEVLR EHKDSVMAVL EAFVYDPLLN
WRLMDTNTKG NKRSRTRTDS YSASQSVEML DGMELGETAH KKTGTTVPES IHSFIGDGLV
KPEALNKKAI QIINRVRDKL TGRDFSHDET LDVPTQVELL IKQATSHENL CQCYIGWCPF
W
//
