TGIF2_MOUSE
ID TGIF2_MOUSE Reviewed; 237 AA.
AC Q8C0Y1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Homeobox protein TGIF2;
DE AltName: Full=5'-TG-3'-interacting factor 2;
DE AltName: Full=TGF-beta-induced transcription factor 2;
DE Short=TGFB-induced factor 2;
GN Name=Tgif2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Transcriptional repressor, which probably repress
CC transcription by binding directly the 5'-CTGTCAA-3' DNA sequence or by
CC interacting with TGF-beta activated SMAD proteins. Probably represses
CC transcription via the recruitment of histone deacetylase proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the transcriptional modulator SMAD3 and the
CC histone deacetylase HDAC1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
CC Note=Excluded from nucleoli. {ECO:0000250}.
CC -!- PTM: The C-terminal part is phosphorylated in response to EGF signaling
CC by the Ras/MAPK pathway. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TALE/TGIF homeobox family. {ECO:0000305}.
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DR EMBL; AK029490; BAC26473.1; -; mRNA.
DR CCDS; CCDS16969.1; -.
DR RefSeq; NP_001278053.1; NM_001291124.1.
DR RefSeq; NP_775572.1; NM_173396.3.
DR RefSeq; XP_006499414.1; XM_006499351.3.
DR RefSeq; XP_006499415.1; XM_006499352.3.
DR RefSeq; XP_006499416.1; XM_006499353.3.
DR RefSeq; XP_006499417.1; XM_006499354.3.
DR AlphaFoldDB; Q8C0Y1; -.
DR SMR; Q8C0Y1; -.
DR BioGRID; 230781; 1.
DR STRING; 10090.ENSMUSP00000096745; -.
DR PhosphoSitePlus; Q8C0Y1; -.
DR MaxQB; Q8C0Y1; -.
DR PaxDb; Q8C0Y1; -.
DR PRIDE; Q8C0Y1; -.
DR ProteomicsDB; 262900; -.
DR Antibodypedia; 26532; 351 antibodies from 33 providers.
DR DNASU; 228839; -.
DR Ensembl; ENSMUST00000081335; ENSMUSP00000096745; ENSMUSG00000062175.
DR GeneID; 228839; -.
DR KEGG; mmu:228839; -.
DR UCSC; uc008nny.2; mouse.
DR CTD; 60436; -.
DR MGI; MGI:1915299; Tgif2.
DR VEuPathDB; HostDB:ENSMUSG00000062175; -.
DR eggNOG; KOG0773; Eukaryota.
DR GeneTree; ENSGT00940000159849; -.
DR InParanoid; Q8C0Y1; -.
DR OMA; VICHSTS; -.
DR OrthoDB; 1573375at2759; -.
DR PhylomeDB; Q8C0Y1; -.
DR TreeFam; TF318093; -.
DR Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR BioGRID-ORCS; 228839; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q8C0Y1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C0Y1; protein.
DR Bgee; ENSMUSG00000062175; Expressed in ventricular zone and 169 other tissues.
DR ExpressionAtlas; Q8C0Y1; baseline and differential.
DR Genevisible; Q8C0Y1; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0035881; P:amacrine cell differentiation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IDA:MGI.
DR GO; GO:0038092; P:nodal signaling pathway; IGI:MGI.
DR GO; GO:1902871; P:positive regulation of amacrine cell differentiation; IDA:MGI.
DR GO; GO:0010470; P:regulation of gastrulation; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IDA:MGI.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR008422; Homeobox_KN_domain.
DR Pfam; PF05920; Homeobox_KN; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Homeobox; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..237
FT /note="Homeobox protein TGIF2"
FT /id="PRO_0000049322"
FT DNA_BIND 16..79
FT /note="Homeobox; TALE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..237
FT /note="Repressive function"
FT REGION 171..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZN2"
FT MOD_RES 186
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZN2"
SQ SEQUENCE 237 AA; 25933 MW; DB22FC96FD45DC59 CRC64;
MSDSDLGEDE GLLSLTGKRK RRGNLPKESV KILRDWLYLH RYNAYPSEQE KLSLSGQTNL
SVLQICNWFI NARRRLLPDM LRKDGKDPNQ FTISRRGGKA SDVALPRGSS PSLLAVSVPA
PTNMLSLSVC SMPLHSGQGE KPAAPFPQVE LESPKALVTP ASTLTLLTRA EAGSPTGGLF
NTPPPTPPEQ DKDDFSSFQL LVEVALQRAA EMELQKQQEP APPLLHTPLP FVSENAK
