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TSC22 domain family protein 3 (Glucocorticoid-induced leucine zipper protein) (TSC22-related-inducible leucine zipper 3) (Tilz3)

 T22D3_MOUSE             Reviewed;         137 AA.
Q9Z2S7; B1AVF3; C6EX03; Q3UNI6; Q8K160; Q9EQN0; Q9EQN1; Q9EQN2;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
25-OCT-2017, entry version 141.
RecName: Full=TSC22 domain family protein 3;
AltName: Full=Glucocorticoid-induced leucine zipper protein;
AltName: Full=TSC22-related-inducible leucine zipper 3;
Short=Tilz3;
Name=Tsc22d3; Synonyms=Dsip1, Dsipi, Gilz;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INDUCTION.
STRAIN=C3H/HeN; TISSUE=Thymus;
PubMed=9430225; DOI=10.1016/S1074-7613(00)80398-2;
D'Adamio F., Zollo O., Moraca R., Ayroldi E., Bruscoli S., Bartoli A.,
Cannarile L., Migliorati G., Riccardi C.;
"A new dexamethasone-induced gene of the leucine zipper family
protects T lymphocytes from TCR/CD3-activated cell death.";
Immunity 7:803-812(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH
MYOD1 AND HDAC1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND INDUCTION.
STRAIN=DBA/2J; TISSUE=Myoblast;
PubMed=20124407; DOI=10.1074/jbc.M109.070136;
Bruscoli S., Donato V., Velardi E., Di Sante M., Migliorati G.,
Donato R., Riccardi C.;
"Glucocorticoid-induced leucine zipper (GILZ) and long GILZ inhibit
myogenic differentiation and mediate anti-myogenic effects of
glucocorticoids.";
J. Biol. Chem. 285:10385-10396(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
Ershler M.A., Belyavsky A.V., Visser J.W.M.;
"Identification and characterization of a family of leucine zipper
genes related to TSC22.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
TISSUE SPECIFICITY.
PubMed=11468175; DOI=10.1182/blood.V98.3.743;
Ayroldi E., Migliorati G., Bruscoli S., Marchetti C., Zollo O.,
Cannarile L., D'Adamio F., Riccardi C.;
"Modulation of T-cell activation by the glucocorticoid-induced leucine
zipper factor via inhibition of nuclear factor kappa B.";
Blood 98:743-753(2001).
[8]
HOMODIMERIZATION, AND INTERACTION WITH JUN AND FOS.
PubMed=11397794; DOI=10.1074/jbc.M101522200;
Mittelstadt P.R., Ashwell J.D.;
"Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ.";
J. Biol. Chem. 276:29603-29610(2001).
[9]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=12393603; DOI=10.1182/blood-2002-02-0538;
Berrebi D., Bruscoli S., Cohen N., Foussat A., Migliorati G.,
Bouchet-Delbos L., Maillot M.-C., Portier A., Couderc J., Galanaud P.,
Peuchmaur M., Riccardi C., Emilie D.;
"Synthesis of glucocorticoid-induced leucine zipper (GILZ) by
macrophages: an anti-inflammatory and immunosuppressive mechanism
shared by glucocorticoids and IL-10.";
Blood 101:729-738(2003).
[10]
INDUCTION.
PubMed=15031210; DOI=10.1182/blood-2003-12-4295;
Asselin-Labat M.-L., David M., Biola-Vidamment A., Lecoeuche D.,
Zennaro M.-C., Bertoglio J., Pallardy M.;
"GILZ, a new target for the transcription factor FoxO3, protects T
lymphocytes from interleukin-2 withdrawal-induced apoptosis.";
Blood 104:215-223(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125 AND THR-128,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 (ISOFORM 3),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 (ISOFORM 4), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Protects T-cells from IL2 deprivation-induced apoptosis
through the inhibition of FOXO3A transcriptional activity that
leads to the down-regulation of the pro-apoptotic factor BCL2L11.
In macrophages, plays a role in the anti-inflammatory and
immunosuppressive effects of glucocorticoids and IL10. In T-cells,
inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro,
suppresses AP1 and NFKB1 DNA-binding activities (By similarity).
Isoform 1 and isoform 4 inhibit myogenic differentiation and
mediate anti-myogenic effects of glucocorticoids by binding and
regulating MYOD1 and HDAC1 transcriptional activity resulting in
reduced expression of MYOG. {ECO:0000250,
ECO:0000269|PubMed:20124407}.
-!- SUBUNIT: Can form homodimers, however it is likely to function as
a monomer. Interacts with AP1 and NFKB1 (By similarity). Isoform 1
and isoform 4 interact with MYOD1. Isoform 1 interacts with HDAC1;
this interaction affects HDAC1 activity on MYOG promoter and thus
inhibits MYOD1 transcriptional activity. {ECO:0000250,
ECO:0000269|PubMed:11397794, ECO:0000269|PubMed:20124407}.
-!- INTERACTION:
Q8CFI0:Nedd4l; NbExp=2; IntAct=EBI-15771036, EBI-8046183;
Q99N57:Raf1; NbExp=2; IntAct=EBI-15771036, EBI-397757;
Q9WVC6:Sgk1; NbExp=2; IntAct=EBI-15771036, EBI-15591730;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.
Note=Localization depends on differentiation status of myoblasts.
In undifferentiated myoblasts, isoform 1 localizes to the
cytoplasm, but in differentiating myoblasts, isoform 1 is
localized to the nucleus.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Nucleus.
Note=Localization depends on differentiation status of myoblasts.
In undifferentiated myoblasts, isoform 4 localizes to the
cytoplasm, but in differentiating myoblasts, isoform 4 is
localized to the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Tilz3b;
IsoId=Q9Z2S7-1; Sequence=Displayed;
Name=2; Synonyms=Tilz3a;
IsoId=Q9Z2S7-2; Sequence=VSP_012690;
Name=3; Synonyms=Tilz3c;
IsoId=Q9Z2S7-3; Sequence=VSP_012691;
Note=Contains a phosphoserine at position 40.
{ECO:0000244|PubMed:21183079};
Name=4; Synonyms=Long Gilz, L-Gilz;
IsoId=Q9Z2S7-4; Sequence=VSP_055016;
Note=Contains a phosphoserine at position 73.
{ECO:0000244|PubMed:21183079};
-!- TISSUE SPECIFICITY: Constitutively expressed in lung, intestine,
kidney and liver, most probably by resident cells from the
macrophage lineage. Expression inversely correlates with T-cell
activation, being higher in resting cells and lower in cells
activated by TCR/CD3 triggering. Isoform 1 and isoform 4 are
expressed in spleen and skeletal muscle (at protein level).
Isoform 1 is expressed in thymus, lymph nodes, bone marrow,
spleen, lung and skeletal muscle. {ECO:0000269|PubMed:11468175,
ECO:0000269|PubMed:12393603, ECO:0000269|PubMed:20124407}.
-!- DEVELOPMENTAL STAGE: Isoform 1 and isoform 4 are expressed in
differentiating myoblasts at a time of myotube formation.
{ECO:0000269|PubMed:20124407}.
-!- INDUCTION: By glucocorticoids in lymphoid cells and upon IL4,
IL10, IL13 or glucocorticoid treatment in monocyte/macrophage
cells. Transiently induced by IL2 deprivation in T-cells. Isoform
1 and isoform 4 expression is up-regulated by the synthetic
glucocorticoid dexamethasone in differentiating myoblasts.
{ECO:0000269|PubMed:12393603, ECO:0000269|PubMed:15031210,
ECO:0000269|PubMed:20124407, ECO:0000269|PubMed:9430225}.
-!- DOMAIN: The leucine-zipper is involved in homodimerization.
-!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family. {ECO:0000305}.
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EMBL; AF024519; AAD01789.1; -; mRNA.
EMBL; EU818782; ACJ09091.1; -; mRNA.
EMBL; AF201287; AAG41220.1; -; mRNA.
EMBL; AF201288; AAG41221.1; -; mRNA.
EMBL; AF201289; AAG41222.1; -; mRNA.
EMBL; AK083389; BAC38897.1; -; mRNA.
EMBL; AK144196; BAE25761.1; -; mRNA.
EMBL; AL683809; CAM24436.1; -; Genomic_DNA.
EMBL; BC028813; AAH28813.1; -; mRNA.
CCDS; CCDS30440.1; -. [Q9Z2S7-1]
CCDS; CCDS41150.1; -. [Q9Z2S7-3]
RefSeq; NP_001070832.1; NM_001077364.1. [Q9Z2S7-3]
RefSeq; NP_034416.3; NM_010286.4. [Q9Z2S7-1]
RefSeq; XP_006528562.1; XM_006528499.3. [Q9Z2S7-3]
RefSeq; XP_006528563.1; XM_006528500.3. [Q9Z2S7-3]
RefSeq; XP_006528564.1; XM_006528501.3. [Q9Z2S7-1]
RefSeq; XP_006528566.1; XM_006528503.3. [Q9Z2S7-2]
RefSeq; XP_006528567.1; XM_006528504.3. [Q9Z2S7-3]
RefSeq; XP_006528568.1; XM_006528505.3. [Q9Z2S7-3]
UniGene; Mm.22216; -.
ProteinModelPortal; Q9Z2S7; -.
SMR; Q9Z2S7; -.
BioGrid; 199919; 5.
DIP; DIP-48844N; -.
IntAct; Q9Z2S7; 5.
STRING; 10090.ENSMUSP00000108620; -.
iPTMnet; Q9Z2S7; -.
PhosphoSitePlus; Q9Z2S7; -.
REPRODUCTION-2DPAGE; IPI00265379; -.
PaxDb; Q9Z2S7; -.
PeptideAtlas; Q9Z2S7; -.
PRIDE; Q9Z2S7; -.
Ensembl; ENSMUST00000055738; ENSMUSP00000062589; ENSMUSG00000031431. [Q9Z2S7-1]
Ensembl; ENSMUST00000112996; ENSMUSP00000108620; ENSMUSG00000031431. [Q9Z2S7-3]
GeneID; 14605; -.
KEGG; mmu:14605; -.
UCSC; uc009ukz.2; mouse. [Q9Z2S7-1]
UCSC; uc009ulb.1; mouse. [Q9Z2S7-3]
CTD; 1831; -.
MGI; MGI:1196284; Tsc22d3.
eggNOG; ENOG410IRR1; Eukaryota.
eggNOG; ENOG410YAFT; LUCA.
GeneTree; ENSGT00530000063062; -.
HOGENOM; HOG000015349; -.
HOVERGEN; HBG075918; -.
InParanoid; Q9Z2S7; -.
OMA; STEMFAK; -.
OrthoDB; EOG091G06PM; -.
PhylomeDB; Q9Z2S7; -.
TreeFam; TF329224; -.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
PRO; PR:Q9Z2S7; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031431; -.
CleanEx; MM_TSC22D3; -.
ExpressionAtlas; Q9Z2S7; baseline and differential.
Genevisible; Q9Z2S7; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0043426; F:MRF binding; IPI:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro.
GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IDA:MGI.
GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0006970; P:response to osmotic stress; IDA:MGI.
InterPro; IPR000580; TSC-22_Dip_Bun.
PANTHER; PTHR12348; PTHR12348; 1.
Pfam; PF01166; TSC22; 1.
ProDom; PD007152; TSC-22_Dip_Bun; 1.
PROSITE; PS01289; TSC22; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 137 TSC22 domain family protein 3.
/FTId=PRO_0000219371.
REGION 1 60 AP1-binding.
REGION 76 97 Leucine-zipper.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:Q99576}.
MOD_RES 125 125 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 128 128 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 57 Missing (in isoform 2).
{ECO:0000303|PubMed:9430225,
ECO:0000303|Ref.3}.
/FTId=VSP_012690.
VAR_SEQ 1 40 MNTEMYQTPMEVAVYQLHNFSISFFSSLLGGDVVSVKLDN
-> MAQPKTECRSPVGLDCCNCCLDLANRCELQKEKSGESP
GSPFVSNFRQLQEKLVFENLNTDKLNNIMRQDSMEPVVRDP
CYLINEGICNRNIDQTMLSILLFFH (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_012691.
VAR_SEQ 1 40 MNTEMYQTPMEVAVYQLHNFSISFFSSLLGGDVVSVKLDN
-> MESQKASSAGAHLPAAPDLPEQAAAAAASKPEKMAQPK
TECRSPVGLDCCNCCLDLANRCELQKEKSGESPGSPFVSNF
RQLQEKLVFENLNTDKLNNIMRQDSMEPVVRDPCYLINEGI
CNRNIDQTMLSILLFFH (in isoform 4).
{ECO:0000303|PubMed:20124407}.
/FTId=VSP_055016.
CONFLICT 22 22 I -> T (in Ref. 1; AAD01789).
{ECO:0000305}.
CONFLICT 33 33 V -> L (in Ref. 3; AAG41221).
{ECO:0000305}.
SEQUENCE 137 AA; 15177 MW; A11D7B69037F111E CRC64;
MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAL DNKIEQAMDL
VKNHLMYAVR EEVEVLKEQI RELLEKNSQL ERENTLLKTL ASPEQLEKFQ SRLSPEEPAP
EAPETPETPE APGGSAV


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