T22D3_RAT
ID T22D3_RAT Reviewed; 134 AA.
AC Q9EQZ1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=TSC22 domain family protein 3;
DE AltName: Full=Glucocorticoid-induced leucine zipper protein;
GN Name=Tsc22d3; Synonyms=Dsipi, Gilz;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Okada T.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; AB025431; BAB18679.1; -; mRNA.
DR EMBL; BC061979; AAH61979.1; -; mRNA.
DR RefSeq; NP_112635.1; NM_031345.1.
DR AlphaFoldDB; Q9EQZ1; -.
DR SMR; Q9EQZ1; -.
DR STRING; 10116.ENSRNOP00000051018; -.
DR iPTMnet; Q9EQZ1; -.
DR PhosphoSitePlus; Q9EQZ1; -.
DR jPOST; Q9EQZ1; -.
DR PaxDb; Q9EQZ1; -.
DR Ensembl; ENSRNOT00000085118; ENSRNOP00000072713; ENSRNOG00000056135.
DR GeneID; 83514; -.
DR KEGG; rno:83514; -.
DR UCSC; RGD:621654; rat.
DR CTD; 1831; -.
DR RGD; 621654; Tsc22d3.
DR eggNOG; KOG4797; Eukaryota.
DR GeneTree; ENSGT00940000156656; -.
DR HOGENOM; CLU_148757_0_0_1; -.
DR InParanoid; Q9EQZ1; -.
DR OMA; YQSPMEV; -.
DR OrthoDB; 1602203at2759; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR PRO; PR:Q9EQZ1; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000056135; Expressed in lung and 19 other tissues.
DR Genevisible; Q9EQZ1; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0043426; F:MRF binding; ISO:RGD.
DR GO; GO:0007589; P:body fluid secretion; IEP:RGD.
DR GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; ISO:RGD.
DR GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006970; P:response to osmotic stress; ISO:RGD.
DR InterPro; IPR000580; TSC-22_Dip_Bun.
DR Pfam; PF01166; TSC22; 1.
DR PROSITE; PS01289; TSC22; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..134
FT /note="TSC22 domain family protein 3"
FT /id="PRO_0000219373"
FT REGION 1..60
FT /note="AP1-binding"
FT /evidence="ECO:0000250"
FT REGION 76..97
FT /note="Leucine-zipper"
FT REGION 101..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 125
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2S7"
SQ SEQUENCE 134 AA; 14836 MW; C3B6CC1266908342 CRC64;
MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAL DNKIEQAMDL
VKNHLMYAVR EEVEVLKEQI RELVEKNSQL ERENTLLKTL ASPEQLEKFQ SRLSPEEPAP
EAPETPEAPG GSAV
