PRD16_MOUSE
ID PRD16_MOUSE Reviewed; 1275 AA.
AC A2A935; Q69ZD6; Q6PB79; Q7TPF4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Histone-lysine N-methyltransferase PRDM16 {ECO:0000305};
DE EC=2.1.1.367 {ECO:0000269|PubMed:22939622};
DE AltName: Full=PR domain zinc finger protein 16 {ECO:0000305};
DE AltName: Full=PR domain-containing protein 16 {ECO:0000305};
DE AltName: Full=Transcription factor MEL1 {ECO:0000305};
DE Short=MDS1/EVI1-like gene 1 {ECO:0000303|PubMed:12816872};
GN Name=Prdm16 {ECO:0000312|MGI:MGI:1917923};
GN Synonyms=Kiaa1675 {ECO:0000305}, Mel1 {ECO:0000303|PubMed:12816872};
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 1).
RC TISSUE=Placenta;
RX PubMed=12816872; DOI=10.1182/blood-2002-12-3944;
RA Nishikata I., Sasaki H., Iga M., Tateno Y., Imayoshi S., Asou N.,
RA Nakamura T., Morishita K.;
RT "A novel EVI1 gene family, MEL1, lacking a PR domain (MEL1S) is expressed
RT mainly in t(1;3)(p36;q21)-positive AML and blocks G-CSF-induced myeloid
RT differentiation.";
RL Blood 102:3323-3332(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [LARGE SCALE MRNA] OF 570-1275 (ISOFORM 3).
RC TISSUE=Pancreatic islet;
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 [5]
RP INTERACTION WITH SMAD3, AND DEVELOPMENTAL STAGE.
RX PubMed=17467076; DOI=10.1016/j.bbamcr.2007.03.016;
RA Warner D.R., Horn K.H., Mudd L., Webb C.L., Greene R.M., Pisano M.M.;
RT "PRDM16/MEL1: a novel Smad binding protein expressed in murine embryonic
RT orofacial tissue.";
RL Biochim. Biophys. Acta 1773:814-820(2007).
RN [6]
RP FUNCTION, INTERACTION WITH PPARGC1A AND PPARGC1B, MUTAGENESIS OF ARG-996,
RP AND TISSUE SPECIFICITY.
RX PubMed=17618855; DOI=10.1016/j.cmet.2007.06.001;
RA Seale P., Kajimura S., Yang W., Chin S., Rohas L.M., Uldry M.,
RA Tavernier G., Langin D., Spiegelman B.M.;
RT "Transcriptional control of brown fat determination by PRDM16.";
RL Cell Metab. 6:38-54(2007).
RN [7]
RP FUNCTION, INTERACTION WITH CTBP1; CTBP2; PPARGC1A AND PPARGC1B, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF 805-ASP-LEU-806, AND REGION.
RX PubMed=18483224; DOI=10.1101/gad.1666108;
RA Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P.,
RA Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.;
RT "Regulation of the brown and white fat gene programs through a PRDM16/CtBP
RT transcriptional complex.";
RL Genes Dev. 22:1397-1409(2008).
RN [8]
RP FUNCTION, INTERACTION WITH PPARA AND PPARG, AND DISRUPTION PHENOTYPE.
RX PubMed=18719582; DOI=10.1038/nature07182;
RA Seale P., Bjork B., Yang W., Kajimura S., Chin S., Kuang S., Scime A.,
RA Devarakonda S., Conroe H.M., Erdjument-Bromage H., Tempst P.,
RA Rudnicki M.A., Beier D.R., Spiegelman B.M.;
RT "PRDM16 controls a brown fat/skeletal muscle switch.";
RL Nature 454:961-967(2008).
RN [9]
RP FUNCTION, AND INTERACTION WITH CEBPA; CEBPB AND CEBPD.
RX PubMed=19641492; DOI=10.1038/nature08262;
RA Kajimura S., Seale P., Kubota K., Lunsford E., Frangioni J.V., Gygi S.P.,
RA Spiegelman B.M.;
RT "Initiation of myoblast to brown fat switch by a PRDM16-C/EBP-beta
RT transcriptional complex.";
RL Nature 460:1154-1158(2009).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22939622; DOI=10.1016/j.cell.2012.06.048;
RA Pinheiro I., Margueron R., Shukeir N., Eisold M., Fritzsch C.,
RA Richter F.M., Mittler G., Genoud C., Goyama S., Kurokawa M., Son J.,
RA Reinberg D., Lachner M., Jenuwein T.;
RT "Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian
RT heterochromatin integrity.";
RL Cell 150:948-960(2012).
RN [11]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=23768516; DOI=10.1016/j.ajhg.2013.05.015;
RA Arndt A.K., Schafer S., Drenckhahn J.D., Sabeh M.K., Plovie E.R.,
RA Caliebe A., Klopocki E., Musso G., Werdich A.A., Kalwa H., Heinig M.,
RA Padera R.F., Wassilew K., Bluhm J., Harnack C., Martitz J., Barton P.J.,
RA Greutmann M., Berger F., Hubner N., Siebert R., Kramer H.H., Cook S.A.,
RA MacRae C.A., Klaassen S.;
RT "Fine mapping of the 1p36 deletion syndrome identifies mutation of PRDM16
RT as a cause of cardiomyopathy.";
RL Am. J. Hum. Genet. 93:67-77(2013).
RN [12]
RP INTERACTION WITH ZNF516, AND REGION.
RX PubMed=25578880; DOI=10.1016/j.molcel.2014.12.005;
RA Dempersmier J., Sambeat A., Gulyaeva O., Paul S.M., Hudak C.S.,
RA Raposo H.F., Kwan H.Y., Kang C., Wong R.H., Sul H.S.;
RT "Cold-inducible Zfp516 activates UCP1 transcription to promote browning of
RT white fat and development of brown fat.";
RL Mol. Cell 57:235-246(2015).
CC -!- FUNCTION: Binds DNA and functions as a transcriptional regulator
CC (PubMed:18483224). Displays histone methyltransferase activity and
CC monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro
CC (PubMed:22939622). Probably catalyzes the monomethylation of free
CC histone H3 in the cytoplasm which is then transported to the nucleus
CC and incorporated into nucleosomes where SUV39H methyltransferases use
CC it as a substrate to catalyze histone H3 'Lys-9' trimethylation
CC (PubMed:22939622). Likely to be one of the primary histone
CC methyltransferases along with MECOM/PRDM3 that direct cytoplasmic
CC H3K9me1 methylation (PubMed:22939622). Functions in the differentiation
CC of brown adipose tissue (BAT) which is specialized in dissipating
CC chemical energy in the form of heat in response to cold or excess
CC feeding while white adipose tissue (WAT) is specialized in the storage
CC of excess energy and the control of systemic metabolism
CC (PubMed:17618855, PubMed:18483224). Together with CEBPB, regulates the
CC differentiation of myoblastic precursors into brown adipose cells
CC (PubMed:18719582, PubMed:19641492). Functions as a repressor of TGF-
CC beta signaling. {ECO:0000269|PubMed:17618855,
CC ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:18719582,
CC ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:22939622}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367;
CC Evidence={ECO:0000269|PubMed:22939622};
CC -!- SUBUNIT: Interacts with CEBPA, CEBPB and CEBPD; the interaction is
CC direct (PubMed:19641492). Interacts with PPARG and PPARA; controls
CC brown adipocytes (PubMed:18719582). Interacts with CTBP1 and CTBP2;
CC represses the expression of WAT-specific genes (PubMed:18483224).
CC Interacts with PPARGC1A and PPARGC1B; interaction with PPARGC1A or
CC PPARGC1B activates the transcription of BAT-specific gene
CC (PubMed:18483224, PubMed:17618855). Interacts with HDAC1, SKI and
CC SMAD2; the interaction with SKI promotes the recruitment of SMAD3-HDAC1
CC complex on the promoter of TGF-beta target genes (Probable). Interacts
CC with ZNF516; the interaction is direct and may play a role in the
CC transcription of brown adipose tissue-specific gene (PubMed:25578880).
CC {ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:18483224,
CC ECO:0000269|PubMed:18719582, ECO:0000269|PubMed:19641492,
CC ECO:0000269|PubMed:25578880, ECO:0000305|PubMed:17467076}.
CC -!- INTERACTION:
CC A2A935-3; Q5DW34-1: Ehmt1; NbExp=2; IntAct=EBI-16080455, EBI-16080518;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18483224}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9HAZ2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2A935-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A935-2; Sequence=VSP_038066, VSP_038067, VSP_038068,
CC VSP_038069;
CC Name=3;
CC IsoId=A2A935-3; Sequence=VSP_038067;
CC -!- TISSUE SPECIFICITY: Enriched in BAT compared to WAT. Detected in heart,
CC lung, kidney and brain. Expressed in nuclei of cardiomyocytes.
CC {ECO:0000269|PubMed:17618855, ECO:0000269|PubMed:23768516}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 12.5 dpc, 13.5 dpc and 14.5 dpc.
CC Expressed in orofacial tissues, heart, liver, brain and limb bud. At
CC 13.5 dpc, expressed throughout the ventricular myocardium, including
CC endocardium and epicardium. {ECO:0000269|PubMed:17467076,
CC ECO:0000269|PubMed:23768516}.
CC -!- DISRUPTION PHENOTYPE: Mice die at birth but embryos display altered
CC brown adipose tissue differentiation. {ECO:0000269|PubMed:18719582}.
CC -!- SIMILARITY: Belongs to the PRDM16 family. {ECO:0000305}.
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DR EMBL; AB078338; BAC79382.1; -; mRNA.
DR EMBL; AL611950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059838; AAH59838.1; -; mRNA.
DR EMBL; AK173230; BAD32508.1; -; mRNA.
DR CCDS; CCDS38989.1; -. [A2A935-1]
DR CCDS; CCDS71532.1; -. [A2A935-2]
DR RefSeq; NP_001277955.1; NM_001291026.1.
DR RefSeq; NP_001277958.1; NM_001291029.1. [A2A935-2]
DR RefSeq; NP_081780.3; NM_027504.3. [A2A935-1]
DR RefSeq; XP_006539236.1; XM_006539173.3. [A2A935-3]
DR AlphaFoldDB; A2A935; -.
DR SMR; A2A935; -.
DR BioGRID; 214194; 5.
DR DIP; DIP-60593N; -.
DR IntAct; A2A935; 991.
DR MINT; A2A935; -.
DR STRING; 10090.ENSMUSP00000030902; -.
DR iPTMnet; A2A935; -.
DR PhosphoSitePlus; A2A935; -.
DR jPOST; A2A935; -.
DR MaxQB; A2A935; -.
DR PaxDb; A2A935; -.
DR PRIDE; A2A935; -.
DR ProteomicsDB; 291862; -. [A2A935-1]
DR ProteomicsDB; 291863; -. [A2A935-2]
DR ProteomicsDB; 291864; -. [A2A935-3]
DR Antibodypedia; 26849; 234 antibodies from 30 providers.
DR DNASU; 70673; -.
DR Ensembl; ENSMUST00000030902; ENSMUSP00000030902; ENSMUSG00000039410. [A2A935-1]
DR Ensembl; ENSMUST00000070313; ENSMUSP00000064546; ENSMUSG00000039410. [A2A935-2]
DR GeneID; 70673; -.
DR KEGG; mmu:70673; -.
DR UCSC; uc008wbu.1; mouse. [A2A935-1]
DR UCSC; uc008wbx.1; mouse. [A2A935-2]
DR CTD; 63976; -.
DR MGI; MGI:1917923; Prdm16.
DR VEuPathDB; HostDB:ENSMUSG00000039410; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160951; -.
DR HOGENOM; CLU_006627_0_0_1; -.
DR InParanoid; A2A935; -.
DR OMA; EGCIKKQ; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF315309; -.
DR BRENDA; 2.1.1.367; 3474.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR BioGRID-ORCS; 70673; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Prdm16; mouse.
DR PRO; PR:A2A935; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A935; protein.
DR Bgee; ENSMUSG00000039410; Expressed in manus and 233 other tissues.
DR ExpressionAtlas; A2A935; baseline and differential.
DR Genevisible; A2A935; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IC:MGI.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; IPI:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:UniProtKB.
DR GO; GO:0048468; P:cell development; IC:GOC-OWL.
DR GO; GO:0070828; P:heterochromatin organization; IMP:UniProtKB.
DR GO; GO:0030853; P:negative regulation of granulocyte differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; IDA:MGI.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043457; P:regulation of cellular respiration; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IDA:MGI.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR GO; GO:0043586; P:tongue development; IMP:MGI.
DR GO; GO:0050872; P:white fat cell differentiation; IDA:UniProtKB.
DR CDD; cd19213; PR-SET_PRDM16; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044410; PRDM16_PR-SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 9.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 5.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Differentiation; DNA-binding;
KW Metal-binding; Methyltransferase; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1275
FT /note="Histone-lysine N-methyltransferase PRDM16"
FT /id="PRO_0000384377"
FT DOMAIN 82..211
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 230..255
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..304
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..332
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 338..361
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 367..389
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 395..417
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 424..446
FT /note="C2H2-type 7; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 951..973
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 979..1002
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1008..1030
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..1038
FT /note="Interaction with CTBP1, CTBP2 and ZNF516"
FT /evidence="ECO:0000269|PubMed:18483224"
FT REGION 740..1275
FT /note="Mediates interaction with SKI and regulation of TGF-
FT beta signaling"
FT /evidence="ECO:0000250|UniProtKB:Q9HAZ2"
FT REGION 789..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 129
FT /note="E -> EQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038066"
FT VAR_SEQ 868
FT /note="Y -> YS (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_038067"
FT VAR_SEQ 1174..1176
FT /note="CVE -> HMQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038068"
FT VAR_SEQ 1177..1275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038069"
FT MUTAGEN 805..806
FT /note="DL->AS: Loss of interaction with CTBP1 and CTBP2 and
FT loss of repression of WAT-specific genes."
FT /evidence="ECO:0000269|PubMed:18483224"
FT MUTAGEN 996
FT /note="R->Q: Loss of DNA-binding activity but no effect on
FT PRDM16-mediated BAT gene transcription activation."
FT /evidence="ECO:0000269|PubMed:17618855"
FT CONFLICT 8
FT /note="R -> K (in Ref. 1; BAC79382)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="A -> T (in Ref. 1; BAC79382)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="G -> D (in Ref. 1; BAC79382)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="P -> L (in Ref. 1; BAC79382)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="R -> Q (in Ref. 1; BAC79382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1275 AA; 140858 MW; 2F1F6B6C3EBFEC10 CRC64;
MRSKARARKL AKSDGDVVNN MYEPDPDLLA GQSAEEETED GILSPIPMGP PSPFPTSEDF
TPKEGSPYEA PVYIPEDIPI PPDFELRESS IPGAGLGIWA KRKMEIGERF GPYVVTPRAA
LKEADFGWEM LTDTEVSSQE SCIKKQISED LGSEKFCVDA NQAGSGSWLK YIRVACSCDD
QNLAMCQINE QIYYKVIKDI EPGEELLVHV KEGAYSLGVM APSLDEDPTF RCDECDELFQ
CRLDLRRHKK YACSSAGAQL YEGLGEELKP EGLGVGSDGQ AHECKDCERM FPNKYSLEQH
MIVHTEEREY KCDQCPKAFN WKSNLIRHQM SHDSGKRFEC ENCVKVFTDP SNLQRHIRSQ
HVGARAHACP DCGKTFATSS GLKQHKHIHS TVKPFICEVC HKSYTQFSNL CRHKRMHADC
RTQIKCKDCG QMFSTTSSLN KHRRFCEGKN HYTPGSIFTP GLPLTPSPMM DKTKPSPTLN
HGGLGFSEYF PSRPHPGSLP FSAAPPAFPA LTPGFPGIFP PSLYPRPPLL PPTPLLKSPL
NHAQDAKLPS PLGNPALPLV SAVSNSSQGA TAATGSEEKF DGRLEDAYAE KVKNRSPDMS
DGSDFEDINT TTGTDLDTTT GTGSDLDSDL DSDRDKGKDK GKPVESKPEF GGASVPPGAM
NSVAEVPAFY SQHSFFPPPE EQLLTASGAA GDSIKAIASI AEKYFGPGFM SMQEKKLGSL
PYHSVFPFQF LPNFPHSLYP FTDRALAHNL LVKAEPKSPR DALKVGGPSA ECPFDLTTKP
KEAKPALLAP KVPLIPSSGE EQPLDLSIGS RARASQNGGG REPRKNHVYG ERKPGVSEGL
PKVCPAQLPQ QPSLHYAKPS PFFMDPIYRV EKRKVADPVG VLKEKYLRPS PLLFHPQMSA
IETMTEKLES FAAMKADSGS SLQPLPHHPF NFRSPPPTLS DPILRKGKER YTCRYCGKIF
PRSANLTRHL RTHTGEQPYR CKYCDRSFSI SSNLQRHVRN IHNKEKPFKC HLCNRCFGQQ
TNLDRHLKKH EHEGAPVSQH SGVLTNHLGT SASSPTSESD NHALLDEKED SYFSEIRNFI
ANSEMNQAST RMDKRPEIQD LDSNPPCPGS ASAKPEDVEE EEEEELEEED DDSLAGKSQE
DTVSPTPEPQ GVYEDEEDEE PPSLTMGFDH TRRCVEERGG GLLALEPTPT FGKGLDLRRA
AEEAFEVKDV LNSTLDSEVL KQTLYRQAKN QAYAMMLSLS EDTPLHAPSQ SSLDAWLNIT
GPSSESGAFN PINHL
