ID T22D3_PONAB Reviewed; 134 AA.
AC Q5RED5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 29-MAY-2024, entry version 76.
DE RecName: Full=TSC22 domain family protein 3;
GN Name=TSC22D3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CR857595; CAH89872.1; -; mRNA.
DR RefSeq; NP_001124873.1; NM_001131401.1.
DR AlphaFoldDB; Q5RED5; -.
DR SMR; Q5RED5; -.
DR STRING; 9601.ENSPPYP00000023578; -.
DR Ensembl; ENSPPYT00000024044.2; ENSPPYP00000023074.1; ENSPPYG00000020613.3.
DR GeneID; 100171736; -.
DR KEGG; pon:100171736; -.
DR CTD; 1831; -.
DR eggNOG; KOG4797; Eukaryota.
DR GeneTree; ENSGT00940000156656; -.
DR HOGENOM; CLU_148757_0_0_1; -.
DR InParanoid; Q5RED5; -.
DR OMA; MNAEMYQ; -.
DR OrthoDB; 2965073at2759; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IEA:TreeGrafter.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd21940; ZIP_TSC22D3; 1.
DR Gene3D; 1.20.5.490; Single helix bin; 1.
DR InterPro; IPR000580; TSC22/Bun.
DR InterPro; IPR047862; TSC22/BUN_CS.
DR PANTHER; PTHR12348; TSC22; 1.
DR PANTHER; PTHR12348:SF24; TSC22 DOMAIN FAMILY PROTEIN 3; 1.
DR Pfam; PF01166; TSC22; 1.
DR SUPFAM; SSF58026; Delta-sleep-inducing peptide immunoreactive peptide; 1.
DR PROSITE; PS01289; TSC22; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..134
FT /note="TSC22 domain family protein 3"
FT /id="PRO_0000262586"
FT REGION 1..60
FT /note="AP1-binding"
FT /evidence="ECO:0000250"
FT REGION 76..97
FT /note="Leucine-zipper"
FT REGION 108..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99576"
SQ SEQUENCE 134 AA; 14810 MW; 77B1024969FA8687 CRC64;
MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAI DNKIEQAMDL
VKNHLMYAVR EEVEILKEQI RELVEKNSQL ERENTLLKTL ASPEQLEKFQ SCLSPEEPAP
ESPQVPEAPG GSAV
//