TFE3_BOVIN
ID TFE3_BOVIN Reviewed; 573 AA.
AC Q05B92;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Transcription factor E3 {ECO:0000250|UniProtKB:P19532};
GN Name=TFE3 {ECO:0000250|UniProtKB:P19532};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that acts as a master regulator of
CC lysosomal biogenesis and immune response (By similarity). Specifically
CC recognizes and binds E-box sequences (5'-CANNTG-3'); efficient DNA-
CC binding requires dimerization with itself or with another MiT/TFE
CC family member such as TFEB or MITF (By similarity). Involved in the
CC cellular response to amino acid availability by acting downstream of
CC MTOR: in the presence of nutrients, TFE3 phosphorylation by MTOR
CC promotes its cytosolic retention and subsequent inactivation. Upon
CC starvation or lysosomal stress, inhibition of MTOR induces TFE3
CC dephosphorylation, resulting in nuclear localization and transcription
CC factor activity (By similarity). In association with TFEB, activates
CC the expression of CD40L in T-cells, thereby playing a role in T-cell-
CC dependent antibody responses in activated CD4(+) T-cells and thymus-
CC dependent humoral immunity (By similarity). Specifically recognizes the
CC MUE3 box, a subset of E-boxes, present in the immunoglobulin enhancer.
CC It also binds very well to a USF/MLTF site. May regulate lysosomal
CC positioning in response to nutrient deprivation by promoting the
CC expression of PIP4P1 (By similarity). Acts as a positive regulator of
CC browning of adipose tissue by promoting expression of target genes;
CC mTOR-dependent phosphorylation promotes cytoplasmic retention of TFE3
CC and inhibits browning of adipose tissue. Maintains the pluripotent
CC state of embryonic stem cells by promoting the expression of genes such
CC as ESRRB; mTOR-dependent nuclear exclusion promotes exit from
CC pluripotency (By similarity). Required to maintain the naive
CC pluripotent state of hematopoietic stem cell; mTOR-dependent
CC cytoplasmic retention of TFE3 promotes the exit of hematopoietic stem
CC cell from pluripotency (By similarity). {ECO:0000250|UniProtKB:P19532,
CC ECO:0000250|UniProtKB:Q64092}.
CC -!- SUBUNIT: Homodimer and heterodimer; with TFEB or MITF.
CC {ECO:0000250|UniProtKB:P19532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P19532}. Nucleus {ECO:0000250|UniProtKB:P19532}.
CC Note=When nutrients are present, phosphorylation by MTOR prevents
CC nuclear translocation and activity. Conversely, inhibition of mTORC1,
CC starvation and lysosomal disruption, promotes dephosphorylation and
CC translocation to the nucleus. {ECO:0000250|UniProtKB:P19532}.
CC -!- PTM: Sumoylated; does not affect dimerization with MITF.
CC {ECO:0000250|UniProtKB:P19532}.
CC -!- PTM: Phosphorylation by MTOR regulates its subcellular location and
CC activity. When nutrients are present, phosphorylation by MTOR promotes
CC retention in the cytosol. Inhibition of mTORC1, starvation and
CC lysosomal disruption, promotes dephosphorylation and translocation to
CC the nucleus. {ECO:0000250|UniProtKB:P19532}.
CC -!- SIMILARITY: Belongs to the MiT/TFE family. {ECO:0000305}.
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DR EMBL; BC122581; AAI22582.1; -; mRNA.
DR RefSeq; NP_001069279.2; NM_001075811.2.
DR AlphaFoldDB; Q05B92; -.
DR SMR; Q05B92; -.
DR STRING; 9913.ENSBTAP00000011237; -.
DR PaxDb; Q05B92; -.
DR PRIDE; Q05B92; -.
DR Ensembl; ENSBTAT00000011237; ENSBTAP00000011237; ENSBTAG00000008523.
DR GeneID; 520800; -.
DR KEGG; bta:520800; -.
DR CTD; 7030; -.
DR VEuPathDB; HostDB:ENSBTAG00000008523; -.
DR VGNC; VGNC:35787; TFE3.
DR eggNOG; KOG1318; Eukaryota.
DR GeneTree; ENSGT00940000157503; -.
DR HOGENOM; CLU_031638_1_1_1; -.
DR InParanoid; Q05B92; -.
DR OMA; DEMRWNK; -.
DR OrthoDB; 1211990at2759; -.
DR TreeFam; TF317174; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000008523; Expressed in monocyte and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006959; P:humoral immune response; ISS:UniProtKB.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR021802; MiT/TFE_C.
DR InterPro; IPR031867; MiT/TFE_N.
DR InterPro; IPR024100; TFE3.
DR PANTHER; PTHR45776:SF3; PTHR45776:SF3; 1.
DR Pfam; PF11851; DUF3371; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF15951; MITF_TFEB_C_3_N; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW Activator; Adaptive immunity; Cytoplasm; DNA-binding; Immunity;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..573
FT /note="Transcription factor E3"
FT /id="PRO_0000270142"
FT DOMAIN 344..397
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 91..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..269
FT /note="Strong transcription activation domain"
FT /evidence="ECO:0000255"
FT REGION 407..428
FT /note="Leucine-zipper"
FT REGION 531..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q64092"
FT MOD_RES 319
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000250|UniProtKB:Q64092"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19532"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19532"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64092"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19532"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19532"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19532"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P19532"
SQ SEQUENCE 573 AA; 61498 MW; ECAF75544180277D CRC64;
MSHAAEPAQD GVEASAEGPR AVFLLLEDRR PADSAQLLSL NSLLPESGIV ADIELENVLD
PDSFYELKSP PLSLRSSLPI SLQATPATPA TLSASSSAEG SRTPAMSSSS SSRVLLRQQL
MRAQAQEQER RERREQASSF PSPAPASPAI SVVGVSAGGH TLGRPPPAQV PREVLKVQTH
LENPTRYHLQ QARRQQVKQY LSTTLGPKLA SQALTPPPGG ASVQPLPTPE AAHAPGPTSS
APNSPMALLT IGSSSEKEID DVIDEIISLE SSYNDEMLSY LPGGNTGLQL PSTLPVSGNL
LDVYNNQGVA TPAITVSNSC PAELPNIKRE ISETEAKALL KERQKKDNHN LIERRRRFNI
NDRIKELGTL IPKSSDPEMR WNKGTILKAS VDYIRKLQKE QQRSKDLESR QRSLEQANRS
LQLRIQELEL QAQIHGLPVP PTPGLLSLAA TSASDSLKPE QLDVEEEGRP GTAIFHATGG
LAQSAPHQQP PPPPSDALLD LHFPSDHLGD LGDPFHLGLE DILMEEEEGV VGGLSGGTLS
PLRAASDPLL SSVSPAVSKA SSRRSSFSME EES
