ID A0A3Q7TR17_VULVU Unreviewed; 2550 AA. AC A0A3Q7TR17; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 29-MAY-2024, entry version 25. DE RecName: Full=Serine/threonine-protein kinase mTOR {ECO:0000256|RuleBase:RU364109}; DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109}; GN Name=MTOR {ECO:0000313|RefSeq:XP_025867696.1}; OS Vulpes vulpes (Red fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes. OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025867696.1}; RN [1] RP IDENTIFICATION. RG RefSeq; RL Submitted (JAN-2019) to UniProtKB. RN [2] {ECO:0000313|RefSeq:XP_025867696.1} RP IDENTIFICATION. RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025867696.1}; RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025867696.1}; RG RefSeq; RL Submitted (FEB-2024) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_025867696.1; XM_026011911.1. DR SMR; A0A3Q7TR17; -. DR STRING; 9627.ENSVVUP00000039784; -. DR Ensembl; ENSVVUT00000052175; ENSVVUP00000039882; ENSVVUG00000027154. DR KEGG; vvp:112929738; -. DR OrthoDB; 8448at2759; -. DR Proteomes; UP000286640; Unplaced. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0031931; C:TORC1 complex; IEA:UniProt. DR GO; GO:0031932; C:TORC2 complex; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. 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:0016043; P:cellular component organization; IEA:UniProt. DR GO; GO:0016242; P:negative regulation of macroautophagy; IEA:TreeGrafter. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:UniProt. DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt. DR GO; GO:0031929; P:TOR signaling; IEA:TreeGrafter. 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 3: Inferred from homology; 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 Reference proteome {ECO:0000313|Proteomes:UP000286640}; 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}. FT DOMAIN 1382..1983 FT /note="FAT" FT /evidence="ECO:0000259|PROSITE:PS51189" FT DOMAIN 2157..2470 FT /note="PI3K/PI4K catalytic" FT /evidence="ECO:0000259|PROSITE:PS50290" FT DOMAIN 2518..2550 FT /note="FATC" FT /evidence="ECO:0000259|PROSITE:PS51190" FT REGION 1812..1868 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1821..1868 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 2550 AA; 288929 MW; E940051732AA0744 CRC64; MLGTGPAAAT AATTTSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN ATRIGRFANY LRNLLPSNDP VVMEMASKAI GRLAMAGDTF TAEYVEFEVK RALEWLGADR NEGRRHAAVL VLRELAVSVP TFFFQQVQPF FDNIFVAVWD PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE AEKGFDETLA KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC KDLMGFGTKP RHITPFTSFQ AVQPPQSNAL VGLLGYSSHQ GLMGFGASPS PAKSTLVESR CCRDLMEEKF DQVCQWVLKC RNSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKAMQVDA TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TALPEASDVG SITLALRTLG SFEFEGHSLT QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSVHLISGH AHVVSQTAVQ VVADVLSKLL VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL NDQVFEIREL AICTVGRLSS MNPAFVMPFL RKMLIQILTE LEHSGIGRIK EQSARMLGHL VSNAPRLIRP YMEPILKALI LKLKDPDPDP NPGVINNVLA TIGELAQVSG LEMRKWVDEL FIIIMDMLQD SSLLAKRQVA LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV SMVALMRIFR DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV IRVCDGAIRE FLFQQLGMLV SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS TIILLIEQIV VALGGEFKLY LPQLIPHMLR VFMHDNSPGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEVPLP SRKAALETVD RLTESLDFTD YASRIIHPIV RTLDQSPELR PTAMDTLSSL VFQLGKKYQI FIPMVNKVLV RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSG QGDALASGPV ETGPMKKLHV STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL RSCWALAQAY NPMARDLFNA AFVSCWSELN EDQQDELIRS IELALTSQDI AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI VLLGERAAKC RAYAKALHYK ELEFQKGPTP AILESLISIN NKLQQPEAAA GVLEYAMKHF GELEIQATWY EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL ALHQDLFSLA QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE EVIQYKLVPE RREIIRQIWW ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGVD PSRQLDHPLP TVHPQVTYAY MKNMWKSTRK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK QELHKLMARC FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA VLHYKHQNQA RDEKKKLRHA SGANITSTTT AATTAATATA TATSTEGSNS ESEAESTENS PTPSPLQKKV TEDLSKTLLM YTVPAVQGFF RSISLSRGNN LQDTLRVLTL WFDYGHWPDV NEALVEGVKA IQIDTWLQVI PQLIARIDTP RPLVGRLIHQ LLTDIGRYHP QALIYPLTVA SKSTTTARHN AANKILKNMC EHSNTLVQQA MMVSEELIRV AILWHEMWHE GLEEASRLYF GERNVKGMFE VLEPLHAMME RGPQTLKETS FNQAYGRDLM EAQEWCRKYM KSGNVKDLTQ AWDLYYHVFR RISKQLPQLT SLELQYVSPK LLMCRDLELA VPGTYDPNQP IIRIQSIAPS LQVITSKQRP RKLTLMGSNG HEFVFLLKGH EDLRQDERVM QLFGLVNTLL ANDPTSLRKN LSIQRYAVIP LSTNSGLIGW VPHCDTLHAL IRDYREKKKI LLNIEHRIML RMAPDYDHLT LMQKVEVFEH AVNNTAGDDL AKLLWLKSPS SEVWFDRRTN YTRSLAVMSM VGYILGLGDR HPSNLMLDRL SGKILHIDFG DCFEVAMTRE KFPEKIPFRL TRMLTNAMEV TGLDGNYRIT CHTVMEVLRE HKDSVMAVLE AFVYDPLLNW RLMDTNTKGN KRSRTRTDSY SAGQSVEILD GVELGEPAHK KTGTTVPESI HSFIGDGLVK PEALNKKAIQ IINRVRDKLT GRDFSHDETL DVPTQVELLI KQATSHENLC QCYIGWCPFW //