T22D1_MOUSE
ID T22D1_MOUSE Reviewed; 1077 AA.
AC P62500; Q00992; Q69Z44; Q6PDK1; Q9EQN4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=TSC22 domain family protein 1;
DE AltName: Full=Regulatory protein TSC-22;
DE AltName: Full=TGFB-stimulated clone 22 homolog;
DE AltName: Full=TSC22-related inducible leucine zipper 1b;
DE AltName: Full=Transforming growth factor beta-1-induced transcript 4 protein;
GN Name=Tsc22d1; Synonyms=Kiaa1994, Tgfb1i4, Tilz1b, Tsc22;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Osteoblast;
RX PubMed=1587811; DOI=10.1016/s0021-9258(19)50006-0;
RA Shibanuma M., Kuroki T., Nose K.;
RT "Isolation of a gene encoding a putative leucine zipper structure that is
RT induced by transforming growth factor beta 1 and other growth factors.";
RL J. Biol. Chem. 267:10219-10224(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-1077 (ISOFORM 1).
RA Ershler M.A., Belyavsky A.V., Visser J.W.M.;
RT "Identification and characterization of a family of leucine zipper genes
RT related to TSC22.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcriptional repressor. Acts on the C-type natriuretic
CC peptide (CNP) promoter.
CC -!- SUBUNIT: Homodimer or heterodimer. Can form a heterodimer with TSC22D4
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P62500; Q9EQN3: Tsc22d4; NbExp=2; IntAct=EBI-8296837, EBI-7821198;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P62500-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62500-2; Sequence=VSP_035327, VSP_035329;
CC Name=3;
CC IsoId=P62500-3; Sequence=VSP_035328;
CC -!- INDUCTION: By transforming growth factor beta-1 and other growth
CC factors.
CC -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG41218.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH58660.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD32600.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X62940; CAA44712.1; -; mRNA.
DR EMBL; AK173322; BAD32600.1; ALT_INIT; mRNA.
DR EMBL; BC058660; AAH58660.1; ALT_INIT; mRNA.
DR EMBL; AF201285; AAG41218.1; ALT_INIT; mRNA.
DR CCDS; CCDS27285.2; -. [P62500-1]
DR CCDS; CCDS27286.1; -. [P62500-2]
DR CCDS; CCDS79344.1; -. [P62500-3]
DR PIR; S23255; S23255.
DR RefSeq; NP_033392.1; NM_009366.4. [P62500-2]
DR RefSeq; NP_997535.2; NM_207652.3.
DR AlphaFoldDB; P62500; -.
DR SMR; P62500; -.
DR BioGRID; 204159; 4.
DR IntAct; P62500; 1.
DR MINT; P62500; -.
DR STRING; 10090.ENSMUSP00000044517; -.
DR iPTMnet; P62500; -.
DR PhosphoSitePlus; P62500; -.
DR MaxQB; P62500; -.
DR PaxDb; P62500; -.
DR PeptideAtlas; P62500; -.
DR PRIDE; P62500; -.
DR ProteomicsDB; 254628; -. [P62500-1]
DR ProteomicsDB; 254629; -. [P62500-2]
DR ProteomicsDB; 254630; -. [P62500-3]
DR Antibodypedia; 23553; 476 antibodies from 31 providers.
DR DNASU; 21807; -.
DR Ensembl; ENSMUST00000022587; ENSMUSP00000022587; ENSMUSG00000022010. [P62500-2]
DR GeneID; 21807; -.
DR KEGG; mmu:21807; -.
DR CTD; 8848; -.
DR MGI; MGI:109127; Tsc22d1.
DR VEuPathDB; HostDB:ENSMUSG00000022010; -.
DR eggNOG; KOG4797; Eukaryota.
DR GeneTree; ENSGT00940000159144; -.
DR HOGENOM; CLU_148757_0_0_1; -.
DR InParanoid; P62500; -.
DR BioGRID-ORCS; 21807; 1 hit in 69 CRISPR screens.
DR ChiTaRS; Tsc22d1; mouse.
DR PRO; PR:P62500; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P62500; protein.
DR Bgee; ENSMUSG00000022010; Expressed in indifferent gonad and 309 other tissues.
DR ExpressionAtlas; P62500; baseline and differential.
DR Genevisible; P62500; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR InterPro; IPR000580; TSC-22_Dip_Bun.
DR Pfam; PF01166; TSC22; 1.
DR PROSITE; PS01289; TSC22; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1077
FT /note="TSC22 domain family protein 1"
FT /id="PRO_0000219366"
FT REGION 22..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1031
FT /note="Leucine-zipper"
FT REGION 1042..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..240
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15714"
FT VAR_SEQ 1..934
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1587811"
FT /id="VSP_035327"
FT VAR_SEQ 303..384
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_035328"
FT VAR_SEQ 935..975
FT /note="GDSGGMSAVSDGSSSSLAAPASLFPLKVLPLTTPLVDGEDE -> MKSQWCR
FT PVAMDLGVYQLRHFSISFLSSLLGTENASVRLDN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1587811"
FT /id="VSP_035329"
FT CONFLICT 395
FT /note="S -> SQ (in Ref. 4; AAG41218)"
FT /evidence="ECO:0000305"
FT CONFLICT 396..398
FT /note="Missing (in Ref. 2; BAD32600)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="I -> V (in Ref. 4; AAG41218 and 3; AAH58660)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="V -> L (in Ref. 4; AAG41218)"
FT /evidence="ECO:0000305"
FT CONFLICT 591
FT /note="V -> I (in Ref. 4; AAG41218 and 3; AAH58660)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="V -> VQQ (in Ref. 2; BAD32600)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="A -> P (in Ref. 2; BAD32600)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="Q -> P (in Ref. 4; AAG41218)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="I -> T (in Ref. 4; AAG41218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1077 AA; 109811 MW; 35749C0C1CA1E1B6 CRC64;
MHQPPESTAA AAAAADISAR KMAHPAMFPR RGSGGGSASA LNAAGTGVSG AAPSSEDFPP
PSLLQPPPPA ASSTQGPQPP PPQSLNLLSQ AQLQGQPLAP GGTQMKKKSG FQITSVTPAQ
ISASISSNNS IAEDTESYDD LDESHTEDLS SSEILDVSLS RATDLGEPER SSSEETLNNF
QEAETPGAVS PNQPHLPQPH LPHLPQQNVV INGNAHPHHL HHHHHPHHGH HLHHGHHHSS
HAAVAGPSIP GGPPSSPVSR KLSTTGSSDG GVPVAPPPAV PSSGLPASVM TNIRTPSTTG
SLGINSVTGT SATNNVNIAA VGSFSPSVTN SVHGNANINT SNIPNAASIS GGPGVTSVVN
SSILSGMGNG TVSSSPVANS VLNAAAGITV GVVSSQQQQQ QQQQPTVNTS RFRVVKLDST
SEPFKKGRWT CTEFYEKENA VPATEGVAIN KVVETVKQTP TEASSSERES TSGSSVSSSV
STLSHYTESV GSGEMMGAPA VVAPQQPPLP PAPPGLQGVA LQQLEFSSPA PQSIAAVSMP
QSISQSQMSQ VQLQPQELSF QQKQTLQPVP LQATMSAATG IQPSPVSVVG VTAAVGQQPS
VSSLAQPQLP YSQTAPPVQT PLPGAPPQQL QYGQQQPMVP AQIAPGHGQP VTQNPTSEYV
QQQQQPIFQA ALSSGQSSST GTGAGISVIP VAQAQGIQLP GQPTAVQTQP AGAAGQPIGQ
AQTAVSTVPT GGQIASIGQQ ANIPTAVQQP STQVTPSVIQ QGAPPSSQVV LPAPTGIIHQ
GVQTRASSLP QQLVIAPQST LVTVPPQPQG VETVAQGVVS QQLPTGSPLP SASTISVTNQ
VSSAAPSGMP SVPTNLVPPQ NIAQPPATQN GSLVQSVSQS PLIATNINLP LAQQIPLSST
QFSTQSLAQA IGSQMEDARR PAEPSLGGLP QTMSGDSGGM SAVSDGSSSS LAAPASLFPL
KVLPLTTPLV DGEDESSGAS VVAIDNKIEQ AMDLVKSHLM YAVREEVEVL KEQIKELIEK
NSQLEQENNL LKTLASPEQL AQFQAQLQTG SPPATTQPQG TTQPPAQPAS QGSGSTA
