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   25-MAY-2022, entry version 70.
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}.
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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; ENSPPYP00000023074; ENSPPYG00000020613.
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; YQSPMEV; -.
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:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   InterPro; IPR000580; TSC-22_Dip_Bun.
DR   Pfam; PF01166; TSC22; 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