T22D3_PIG
ID T22D3_PIG Reviewed; 77 AA.
AC P80220;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=TSC22 domain family protein 3;
DE AltName: Full=DSIP-immunoreactive peptide;
DE Short=DIP protein;
DE AltName: Full=Delta sleep-inducing peptide immunoreactor;
DE AltName: Full=Glucocorticoid-induced leucine zipper protein;
GN Name=TSC22D3; Synonyms=DSIPI, GILZ;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Brain;
RX PubMed=8375381; DOI=10.1111/j.1432-1033.1993.tb18160.x;
RA Sillard R., Schulz-Knappe P., Vogel P., Raida M., Bensch K.W.,
RA Forssmann W.-G., Mutt M.;
RT "A novel 77-residue peptide from porcine brain contains a leucine-zipper
RT motif and is recognized by an antiserum to delta-sleep-inducing peptide.";
RL Eur. J. Biochem. 216:429-436(1993).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=9388238; DOI=10.1074/jbc.272.49.30918;
RA Seidel G., Adermann K., Schindler T., Ejchart A., Jaenicke R.,
RA Forssmann W.-G., Roesch P.;
RT "Solution structure of porcine delta sleep-inducing peptide immunoreactive
RT peptide A homolog of the shortsighted gene product.";
RL J. Biol. Chem. 272:30918-30927(1997).
CC -!- FUNCTION: Protects T-cells from IL2 deprivation-induced apoptosis
CC through the inhibition of FOXO3A transcriptional activity that leads to
CC the down-regulation of the pro-apoptotic factor BCL2L11. In
CC macrophages, plays a role in the anti-inflammatory and
CC immunosuppressive effects of glucocorticoids and IL10. In T-cells,
CC inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro,
CC suppresses AP1 and NFKB1 DNA-binding activities. Inhibits myogenic
CC differentiation and mediates anti-myogenic effects of glucocorticoids
CC by binding and regulating MYOD1 and HDAC1 transcriptional activity
CC resulting in reduced expression of MYOG (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Can form homodimers, however it is likely to function as a
CC monomer. Interacts with AP1 and NFKB1. Interacts with MYOD1. Interacts
CC with HDAC1; this interaction affects HDAC1 activity on MYOG promoter
CC and thus inhibits MYOD1 transcriptional activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Localization depends on differentiation status of myoblasts. In
CC undifferentiated myoblasts, localizes to the cytoplasm, but in
CC differentiating myoblasts is localized to the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- INDUCTION: By glucocorticoids in lymphoid cells and upon IL4, IL10,
CC IL13 or glucocorticoid treatment in monocyte/macrophage cells.
CC Transiently induced by IL2 deprivation in T-cells. Expression is up-
CC regulated by synthetic glucocorticoid dexamethasone in differentiating
CC myoblasts (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The leucine-zipper is involved in homodimerization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family. {ECO:0000305}.
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 PIR; S36827; S36827.
DR PDB; 1DIP; NMR; -; A/B=1-77.
DR PDBsum; 1DIP; -.
DR AlphaFoldDB; P80220; -.
DR SMR; P80220; -.
DR STRING; 9823.ENSSSCP00000021368; -.
DR iPTMnet; P80220; -.
DR PaxDb; P80220; -.
DR PeptideAtlas; P80220; -.
DR eggNOG; KOG4797; Eukaryota.
DR HOGENOM; CLU_148757_2_0_1; -.
DR InParanoid; P80220; -.
DR EvolutionaryTrace; P80220; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P80220; SS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR DisProt; DP00759; -.
DR InterPro; IPR000580; TSC-22_Dip_Bun.
DR Pfam; PF01166; TSC22; 1.
DR PROSITE; PS01289; TSC22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..77
FT /note="TSC22 domain family protein 3"
FT /id="PRO_0000219372"
FT REGION 19..40
FT /note="Leucine-zipper"
FT REGION 41..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:8375381"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99576"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:1DIP"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:1DIP"
FT HELIX 17..43
FT /evidence="ECO:0007829|PDB:1DIP"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1DIP"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1DIP"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1DIP"
SQ SEQUENCE 77 AA; 8713 MW; A46C9FC08B72542D CRC64;
MDLVKNHLMY AVREEVEILK EQIRELVEKN SQLERENTLL KTLASPEQLE KFQSRLSPEE
PAPETPEAPE APGGSAV
