UniProt: A0A8J1JWG6

Database: UniProt
Entry: A0A8J1JWG6_XENTR

LinkDB:  A0A8J1JWG6_XENTR 
Original site:  A0A8J1JWG6_XENTR

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Ontology (24)   
   GO (24)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   XENBASE (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (31)   
   InterPro (16)   
   Pfam (6)   
   PROSITE (5)   
   SMART (4)   
All databases (61)   

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ID   A0A8J1JWG6_XENTR        Unreviewed;      2532 AA.
AC   A0A8J1JWG6;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   28-JAN-2026, entry version 19.
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|RefSeq:XP_031761369.1,
GN   ECO:0000313|RefSeq:XP_031761370.1,
GN   ECO:0000313|Xenbase:XB-GENE-993118};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Proteomes:UP000008143, ECO:0000313|RefSeq:XP_031761370.1};
RN   [1] {ECO:0000313|RefSeq:XP_031761369.1, ECO:0000313|RefSeq:XP_031761370.1}
RP   IDENTIFICATION.
RC   STRAIN=Nigerian {ECO:0000313|RefSeq:XP_031761369.1,
RC   ECO:0000313|RefSeq:XP_031761370.1};
RC   TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_031761369.1,
RC   ECO:0000313|RefSeq:XP_031761370.1};
RG   RefSeq;
RL   Submitted (APR-2025) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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:ARBA00048679};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00047899,
CC         ECO:0000256|RuleBase:RU364109};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00051942};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597;
CC         Evidence={ECO:0000256|ARBA:ARBA00051942};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
CC       Cytoplasmic vesicle, phagosome {ECO:0000256|ARBA:ARBA00004262}.
CC       Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus
CC       membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004255}. Lysosome membrane
CC       {ECO:0000256|ARBA:ARBA00004630}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004630}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004630}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004524}. Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004570}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004570}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004570}. Nucleus, PML body
CC       {ECO:0000256|ARBA:ARBA00004322}.
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_031761369.1; XM_031905509.1.
DR   RefSeq; XP_031761370.1; XM_031905510.1.
DR   GeneID; 100491970; -.
DR   KEGG; xtr:100491970; -.
DR   AGR; Xenbase:XB-GENE-993118; -.
DR   CTD; 2475; -.
DR   Xenbase; XB-GENE-993118; mtor.
DR   OMA; MRQHSAK; -.
DR   OrthoDB; 2250022at2759; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
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:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
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:0016242; P:negative regulation of macroautophagy; IBA:GO_Central.
DR   GO; GO:0009891; P:positive regulation of biosynthetic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IEA:UniProtKB-ARBA.
DR   GO; GO:0051240; P:positive regulation of multicellular organismal process; IEA:UniProtKB-ARBA.
DR   GO; GO:0008361; P:regulation of cell size; IEA:UniProtKB-ARBA.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0051896; P:regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:UniProtKB-ARBA.
DR   GO; GO:0038202; P:TORC1 signaling; IBA:GO_Central.
DR   CDD; cd05169; PIKKc_TOR; 1.
DR   FunFam; 1.10.1070.11:FF:000074; DJ576K7.1 (FK506 binding protein 12-rapamycin associated protein 1); 1.
DR   FunFam; 1.10.1070.11:FF:000058; MTOR isoform 6; 1.
DR   FunFam; 1.25.10.10:FF:000060; Serine/threonine-protein kinase mTOR; 1.
DR   FunFam; 1.25.10.10:FF:000094; Serine/threonine-protein kinase mTOR; 1.
DR   FunFam; 1.25.10.10:FF:000532; Serine/threonine-protein kinase mTOR; 1.
DR   FunFam; 1.20.120.150:FF:000001; Serine/threonine-protein kinase TOR; 1.
DR   FunFam; 1.25.10.10:FF:000083; Serine/threonine-protein kinase TOR; 1.
DR   FunFam; 3.30.1010.10:FF:000004; Serine/threonine-protein kinase 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; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR050517; DDR_Repair_Kinase.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR009076; FRB_dom.
DR   InterPro; IPR036738; FRB_sf.
DR   InterPro; IPR057564; HEAT_ATR.
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; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF08771; FRB_dom; 1.
DR   Pfam; PF23593; HEAT_ATR; 1.
DR   Pfam; PF11865; mTOR_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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364109};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364109};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364109}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU364109}; TPR repeat {ECO:0000256|ARBA:ARBA00022803};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          1385..1965
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2139..2452
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2500..2532
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
FT   REGION          1810..1851
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2532 AA;  288064 MW;  739648953E6EE2C0 CRC64;
     MNPANMSGIM TMLQQFANGL RSRNEETRIK AAKDLQHYVT TELREVSQEE ATQFYDELNH
     FIFEFVSSSD VSERKGGILA IVSLIGVEGG NATRISRFAN YLRNLLPSSD PGVMEMASKA
     MGRLAMAGDT FTAEYVEFEV KRALEWLGAD RNEGRRHAAV LVLRELAVSA PTFFFQQVQP
     FFDNIFFAVW DPKQAIREGA VAALRACLIL TTQREPKELQ KPLWYRQTYE EAERGFDETL
     SKEKGMNRDD RIHGALLIIN ELVRISSMEG ERLREEMEEI TQQQMVHDKH CKDLMTFGLK
     PRHITPFASF QSVQPQPSNA LLSLLGYTGQ QGILGYGAAP MPDKTTLVES RACRELVEEK
     FDQICRWVLK CRSSKNPLIQ MTILNVLPRL AAFRPSAFTA DLYLPDTMSH LLSCVRKEKE
     RTVAFQALGL ISVAVRSEIR LYLPKILEHV KAALPPKDFA HKRQKSIQVD ATVFTCISML
     ARSMGPSIQQ DIKELLEPML SVGLSPALTA VLYDLSRHIP QLKKDIQDGL LKMLSLVLMH
     KPLRHPGMPK GLAQQLSSPS LTNIPEISDV GSITLALRTL GTFEFEGHSL TQFVRHCADH
     FLNSEHKEIR MEAARTCSRL LTPSIQLLSG HGHVSQTAVQ VVADVLGKLL VVGITDPDPD
     IRYCVLASLD ERFDTHLAQA ENLQALFVAL NDEVFEIREL AICTIGRLSS MNPAFVMPFL
     RKMLIQILTE LEHSGVGRNK EQSARMLGHL VSNAPRLIRP YMEPILKALI LKLRDPDPNP
     GVVTNVLATI GELAQVSGLE MRKWMDELFP IIMDMLQDSS LLAKRQVALW TLGQLVASTG
     YVVEPYRKYP SLLEVLLNFL KTEQNQGIRR EAIRVLGLLG ALDPYKHKVN IGMIDQSRDA
     SALSLSESKA NQDSADYSTS EMLVNMGNLP LDEFYPAVSV VTLMRILRDQ SLSNHHTMVV
     QAITFIFKSL GLKCVQFLPQ VMPTFLSAIR LCDNNMRESH QPSPQKRTSL MSPQFMFQQL
     GMLVGFVRSH IRPYMDEIFA LIKDYWTMNN PIQSTIILLI EQIVLSLGGE FKLYLPQLIP
     HMLRVFMHDS SVGRSVTIKL LNAIQMFGAN LDDYLHLLLP PIVKLFDAPD SPMPARKVAL
     ETVDRLTESL DFTDYASRII HPIVRTLDMS PDLRITAMDT LSSLVFQLGK KYHIFIPMVN
     KVLQKHRILH QRYEVLTCRI LKGYTLADEE EDPLIYQHKA QRGNLSETAS APLDAGPMKK
     LHVSTTNLQK AWGAARRVSK DDWLEWLRRL SVELLKDSSS PALRSCWSLA QAYNPLARDL
     FNAAFLSCWS ELNEDQQDEL IRSIELALTS QDIAEVTQTL LNLAEFMEHS DKGPLPLRDD
     NGVVLLGERA SKCRAYAKAL HYKELEFQKG PSPAILESLI SINNKLQQPE AASGVLEFAM
     KHYGEMEIQA TWYEKLHEWE DALVAYDKKI EVNKDDSELI LGRMRCLEAL GEWGQLHQQC
     CENWTNVNED ARAKMARMAA AAAWGLEQWD SMEEYTCLIP RDTHDGAFYR AVLALHQDLF
     SLAQQCIDKA RDMLDAELTA MAGESYSRAY GAMVTCQMLS ELEEVIQYKL VPERREIIRQ
     TWWDRLQGCQ RIVEDWQKIL MVQSLVVSPH EDMRTWLKYA SLCSKSGRLA LSHKTLVMLL
     GVDPALESDQ PLPTAHPQVT YAYMKYMWKS TRKIEAFQHM QKFVNNMQLQ AQHVADDPQH
     KQELQKLMAR CFLKLGEWQL NLQGINECTI PCVLEYYSAA TEHDHNWYKA WHAWAVMNFE
     AVLHFKHQNH PRDEKKVRHP STASAPPEGS ESESEGESND NSPVSSPVQK KPSEDISHTL
     LLYTVPAVQG FFRSISLSRG NNLQDTLRVL TLWFDYGHWP DVNEALVEGI KTIQIDTWLQ
     VIPQLIARID TPRALVGRLI HQLLTDIGRY HPQALIYPLT VASKSTTTAR HNAANKILKN
     MCEHSNTLVQ QAMMVSEELI RVAILWHEMW HEGLEEASRL YFGERNVKGM FAVLDPLHAM
     MERGPQTLKE TSFNQAYGRD LMEAQDWCRK YMKSGNVKDL TQAWDLYYHV FRRISKQLPQ
     LTSLELQYVS PKLLMCRDLE LAVPGTYDPN QPIIRIQSIA PSLQVITSKQ RPRKLTLMGS
     NGHEFMFLLK GHEDLRQDER VMQLFGLVNT LLANDPASLR KNLSIQRYAV IPLSTNSGLI
     GWVPHCDTLH ALIRDYREKK KILLNIEHRI MLRMAPDYDH LTLMQKVEVF EHAVNNTAGD
     DLAKLLWLKS PSSEVWFDRR TNYTRSLAVM SMVGYILGLG DRHPSNLMLD RLSGKILHID
     FGDCFEVAMT REKFPEKIPF RLTRMLTNAM EVTGLDGNYR ITCHTVMEVL REHKDSVMAV
     LEAFVYDPLL NWRLMDTNIK GNKRSRTRTD SYSAGQSGEI METVELGETA HKKTGSTVPE
     SIHTFIGDGL VQPEALNKKA IQIINRVRDK LTGRDFSHEE TLDVATQVEL LIKQATSHEN
     LCQCYIGWCP FW
//

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