DDIT4_BOVIN
ID DDIT4_BOVIN Reviewed; 229 AA.
AC Q08E62;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA damage-inducible transcript 4 protein;
GN Name=DDIT4;
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=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates cell growth, proliferation and survival via
CC inhibition of the activity of the mammalian target of rapamycin complex
CC 1 (mTORC1). Inhibition of mTORC1 is mediated by a pathway that involves
CC DDIT4/REDD1, AKT1, the TSC1-TSC2 complex and the GTPase RHEB. Plays an
CC important role in responses to cellular energy levels and cellular
CC stress, including responses to hypoxia and DNA damage. Regulates
CC p53/TP53-mediated apoptosis in response to DNA damage via its effect on
CC mTORC1 activity. Its role in the response to hypoxia depends on the
CC cell type; it mediates mTORC1 inhibition in fibroblasts and thymocytes,
CC but not in hepatocytes. Inhibits neuronal differentiation and neurite
CC outgrowth mediated by NGF via its effect on mTORC1 activity. Required
CC for normal neuron migration during embryonic brain development. Plays a
CC role in neuronal cell death. Required for mTORC1-mediated defense
CC against viral protein synthesis and virus replication (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with BTRC. Identified in a complex with
CC CUL4A, DDB1 and BTRC. Interacts with TXNIP; this inhibits the
CC proteasomal degradation of DDIT4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by GSK3B; this promotes proteasomal degradation.
CC {ECO:0000250}.
CC -!- PTM: Polyubiquitinated by a DCX (DDB1-CUL4A-RBX1) E3 ubiquitin-protein
CC ligase complex with BTRC as substrate-recognition component, leading to
CC its proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DDIT4 family. {ECO:0000305}.
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DR EMBL; BC123397; AAI23398.1; -; mRNA.
DR RefSeq; NP_001069390.1; NM_001075922.1.
DR AlphaFoldDB; Q08E62; -.
DR SMR; Q08E62; -.
DR STRING; 9913.ENSBTAP00000000187; -.
DR PaxDb; Q08E62; -.
DR Ensembl; ENSBTAT00000000187; ENSBTAP00000000187; ENSBTAG00000000163.
DR GeneID; 529235; -.
DR KEGG; bta:529235; -.
DR CTD; 54541; -.
DR VEuPathDB; HostDB:ENSBTAG00000000163; -.
DR VGNC; VGNC:27948; DDIT4.
DR eggNOG; ENOG502RB72; Eukaryota.
DR GeneTree; ENSGT00530000063652; -.
DR HOGENOM; CLU_086145_1_0_1; -.
DR InParanoid; Q08E62; -.
DR OMA; EQGKGCH; -.
DR OrthoDB; 1588396at2759; -.
DR TreeFam; TF105007; -.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000000163; Expressed in urethra and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0071889; F:14-3-3 protein binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IEA:Ensembl.
DR GO; GO:1902532; P:negative regulation of intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; ISS:UniProtKB.
DR GO; GO:0032984; P:protein-containing complex disassembly; IEA:Ensembl.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0032006; P:regulation of TOR signaling; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR Gene3D; 3.90.470.40; -; 1.
DR InterPro; IPR012918; RTP801-like.
DR InterPro; IPR038281; RTP801-like_C_sf.
DR PANTHER; PTHR12478; PTHR12478; 1.
DR Pfam; PF07809; RTP801_C; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Apoptosis; Cytoplasm; Mitochondrion; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..229
FT /note="DNA damage-inducible transcript 4 protein"
FT /id="PRO_0000307196"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX09"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX09"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX09"
SQ SEQUENCE 229 AA; 24811 MW; 1AB4CB2849F9AB6B CRC64;
MPSLWDRFSS SSSSSSLSRT PTPNQPPRSA WGSAAREEGL GRCGSLESSD CESLDSSNSG
FGPEEDSAYL DGVSLPDFEL LSDPEDEHLC ASLMQLLQES LAQARLGSRR PARLLMPGQL
VSQVGKELLR LAYSEPCGLR GALLDVCVEQ GKSCHSVGQL ALDPSLVPTF QLTLVLRLDS
RLWPKIQGLF SSANSPFVPG FSQSLTLSTG FRVIKKKLYS SEQLLIEEC
