SRTD2_MOUSE
ID SRTD2_MOUSE Reviewed; 309 AA.
AC Q9JJG5; Q8C609; Q91WL3; Q925E5;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=SERTA domain-containing protein 2;
DE AltName: Full=Transcriptional regulator interacting with the PHD-bromodomain 2;
DE Short=TRIP-Br2;
GN Name=Sertad2; Synonyms=Kiaa0127; ORFNames=MNCb-1504;
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=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 129-309.
RX PubMed=11331592; DOI=10.1093/emboj/20.9.2273;
RA Hsu S.-I., Yang C.M., Sim K.G., Hentschel D.M., O'Leary E., Bonventre J.V.;
RT "TRIP-Br: a novel family of PHD zinc finger- and bromodomain-interacting
RT proteins that regulate the transcriptional activity of E2F-1/DP-1.";
RL EMBO J. 20:2273-2285(2001).
RN [5]
RP FUNCTION IN ADIPOGENESIS, INDUCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=23291629; DOI=10.1038/nm.3056;
RA Liew C.W., Boucher J., Cheong J.K., Vernochet C., Koh H.J., Mallol C.,
RA Townsend K., Langin D., Kawamori D., Hu J., Tseng Y.H., Hellerstein M.K.,
RA Farmer S.R., Goodyear L., Doria A., Blueher M., Hsu S.I., Kulkarni R.N.;
RT "Ablation of TRIP-Br2, a regulator of fat lipolysis, thermogenesis and
RT oxidative metabolism, prevents diet-induced obesity and insulin
RT resistance.";
RL Nat. Med. 19:217-226(2013).
CC -!- FUNCTION: Acts at E2F-responsive promoters as coregulator to integrate
CC signals provided by PHD- and/or bromodomain-containing transcription
CC factors. May act as coactivator as well as corepressor of E2F1-TFDP1
CC and E2F4-TFDP1 complexes on E2F consensus binding sites, which would
CC activate or inhibit E2F-target genes expression. Modulates fat storage
CC by down-regulating the expression of key genes involved in adipocyte
CC lipolysis, thermogenesis and oxidative metabolism.
CC {ECO:0000269|PubMed:23291629}.
CC -!- SUBUNIT: Interacts with XPO1; which mediates nuclear export. Interacts
CC with TFDP1; modulates transactivation activity of TFDP1/E2F complexes
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Exported out of the nucleus via its NES in a XPO1-dependent
CC manner. Once in the cytoplasm, is degraded by the proteasome (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in white and brown adipose tissue.
CC {ECO:0000269|PubMed:23291629}.
CC -!- INDUCTION: Up-regulated by high fat diet in adipose tissue.
CC {ECO:0000269|PubMed:23291629}.
CC -!- PTM: Polyubiquitinated, which promotes proteasomal degradation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Resist development of obesity because of enhanced
CC lipolysis and thermogenesis due, in part, to an increase in brown
CC adipocytes number. On high fat diet (HFD), show reduced white adipose
CC tissue (WAT) weight with smaller adipocyte size, improved glucose
CC tolerance and insulin sensitivity with lower fasting glucose and
CC insulin concentrations. Animals on HFD have higher and lower
CC concentrations of adiponectin and leptin, respectively, compared to
CC wild-type. They don't develop liver steatosis and have 57% less adipose
CC tissue macrophage infiltration. {ECO:0000269|PubMed:23291629}.
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DR EMBL; AB041541; BAA95026.1; -; mRNA.
DR EMBL; AK076787; BAC36480.1; -; mRNA.
DR EMBL; BC014726; AAH14726.1; -; mRNA.
DR EMBL; AF366403; AAK52832.1; -; mRNA.
DR CCDS; CCDS24458.1; -.
DR RefSeq; NP_001033714.1; NM_001038625.1.
DR RefSeq; NP_067347.2; NM_021372.2.
DR RefSeq; XP_006514829.1; XM_006514766.3.
DR AlphaFoldDB; Q9JJG5; -.
DR BioGRID; 208368; 2.
DR CORUM; Q9JJG5; -.
DR IntAct; Q9JJG5; 1.
DR STRING; 10090.ENSMUSP00000090981; -.
DR PhosphoSitePlus; Q9JJG5; -.
DR PaxDb; Q9JJG5; -.
DR PRIDE; Q9JJG5; -.
DR Antibodypedia; 16073; 140 antibodies from 18 providers.
DR Ensembl; ENSMUST00000093292; ENSMUSP00000090981; ENSMUSG00000049800.
DR Ensembl; ENSMUST00000109585; ENSMUSP00000105214; ENSMUSG00000049800.
DR Ensembl; ENSMUST00000109586; ENSMUSP00000105215; ENSMUSG00000049800.
DR GeneID; 58172; -.
DR KEGG; mmu:58172; -.
DR UCSC; uc007idc.1; mouse.
DR CTD; 9792; -.
DR MGI; MGI:1931026; Sertad2.
DR VEuPathDB; HostDB:ENSMUSG00000049800; -.
DR eggNOG; ENOG502QUG8; Eukaryota.
DR GeneTree; ENSGT00530000063867; -.
DR HOGENOM; CLU_065586_0_0_1; -.
DR InParanoid; Q9JJG5; -.
DR OMA; FCAVSPP; -.
DR PhylomeDB; Q9JJG5; -.
DR TreeFam; TF331620; -.
DR BioGRID-ORCS; 58172; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Sertad2; mouse.
DR PRO; PR:Q9JJG5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JJG5; protein.
DR Bgee; ENSMUSG00000049800; Expressed in humerus cartilage element and 252 other tissues.
DR ExpressionAtlas; Q9JJG5; baseline and differential.
DR Genevisible; Q9JJG5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR InterPro; IPR009263; SERTA_dom.
DR Pfam; PF06031; SERTA; 1.
DR PROSITE; PS51053; SERTA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..309
FT /note="SERTA domain-containing protein 2"
FT /id="PRO_0000191614"
FT DOMAIN 33..80
FT /note="SERTA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00396"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..306
FT /note="Required for transactivation activity"
FT /evidence="ECO:0000250"
FT MOTIF 233..238
FT /note="Nuclear export signal (NES)"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 138..140
FT /note="CTL -> FTF (in Ref. 4; AAK52832)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="A -> S (in Ref. 3; AAH14726)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="P -> S (in Ref. 4; AAK52832)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="T -> A (in Ref. 1; BAA95026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 33312 MW; D4178688F0DF8F00 CRC64;
MLGKGGKRKF DEHEDGLEGK IVSPSDGPSR VSYTLQRQTI FNISLMKLYN HRPLTEPSLQ
KTVLINNMLR RIQEELKQEG SLRPAFTPSS QPSNSLSDSY QEAPPPAPHP CDLGSTTPLE
ACLTPASLLE DDNDDTFCTL QAVHPAAPTR LSSAALPAEK DSFSSALDEI EELCPTSTST
EAAHTAAPEG PKGTSSESSV QKPEGPEEGR TDDSRFMDSL PGNFEITTST GFLTDLTLDD
ILFADIDTSM YDFDPCTSAS GTASKMAPVS ADDLLKTLAP YSNQPVAPSQ PFKMDLTELD
HIMEVLVGS
