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Mothers against decapentaplegic homolog 6 (MAD homolog 6) (Mothers against DPP homolog 6) (Mad homolog 7) (SMAD family member 6) (SMAD 6) (Smad6)

 SMAD6_MOUSE             Reviewed;         495 AA.
O35182; Q9CW62;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
12-SEP-2018, entry version 159.
RecName: Full=Mothers against decapentaplegic homolog 6;
Short=MAD homolog 6;
Short=Mothers against DPP homolog 6;
AltName: Full=Mad homolog 7;
AltName: Full=SMAD family member 6;
Short=SMAD 6;
Short=Smad6;
Name=Smad6; Synonyms=Madh6, Madh7, Msmad6;
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].
TISSUE=Lung;
PubMed=9335505; DOI=10.1038/39355;
Imamura T., Takase M., Nishihara A., Oeda E., Hanai J., Kawabata M.,
Miyazono K.;
"Smad6 inhibits signalling by the TGF-beta superfamily.";
Nature 389:622-626(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-495.
STRAIN=C57BL/6J; TISSUE=Lung;
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).
[3]
INTERACTION WITH RNF111.
PubMed=14657019; DOI=10.1093/emboj/cdg632;
Koinuma D., Shinozaki M., Komuro A., Goto K., Saitoh M., Hanyu A.,
Ebina M., Nukiwa T., Miyazawa K., Imamura T., Miyazono K.;
"Arkadia amplifies TGF-beta superfamily signaling through degradation
of Smad7.";
EMBO J. 22:6458-6470(2003).
[4]
INTERACTION WITH WWP1, AND UBIQUITINATION.
PubMed=15221015; DOI=10.1038/sj.onc.1207885;
Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K.,
Miyazawa K.;
"Negative regulation of transforming growth factor-beta (TGF-beta)
signaling by WW domain-containing protein 1 (WWP1).";
Oncogene 23:6914-6923(2004).
[5]
INTERACTION WITH NEDD4L.
PubMed=15496141; DOI=10.1042/BJ20040738;
Kuratomi G., Komuro A., Goto K., Shinozaki M., Miyazawa K.,
Miyazono K., Imamura T.;
"NEDD4-2 (neural precursor cell expressed, developmentally down-
regulated 4-2) negatively regulates TGF-beta (transforming growth
factor-beta) signalling by inducing ubiquitin-mediated degradation of
Smad2 and TGF-beta type I receptor.";
Biochem. J. 386:461-470(2005).
[6]
FUNCTION, INTERACTION WITH PELI1, AND INDUCTION.
PubMed=16951688; DOI=10.1038/ni1383;
Choi K.C., Lee Y.S., Lim S., Choi H.K., Lee C.H., Lee E.K., Hong S.,
Kim I.H., Kim S.J., Park S.H.;
"Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor
signaling through direct interaction with the adaptor Pellino-1.";
Nat. Immunol. 7:1057-1065(2006).
[7]
METHYLATION AT ARG-74 AND ARG-81, AND MUTAGENESIS OF ARG-74.
PubMed=23747011; DOI=10.1016/j.molcel.2013.05.004;
Xu J., Wang A.H., Oses-Prieto J., Makhijani K., Katsuno Y., Pei M.,
Yan L., Zheng Y.G., Burlingame A., Bruckner K., Derynck R.;
"Arginine Methylation Initiates BMP-Induced Smad Signaling.";
Mol. Cell 51:5-19(2013).
[8]
UBIQUITINATION.
PubMed=23610558; DOI=10.1371/journal.pbio.1001538;
Kelly C.E., Thymiakou E., Dixon J.E., Tanaka S., Godwin J.,
Episkopou V.;
"Rnf165/Ark2C enhances BMP-Smad signaling to mediate motor axon
extension.";
PLoS Biol. 11:E1001538-E1001538(2013).
-!- FUNCTION: Binds to regulatory elements in target promoter regions
(By similarity). May block the BMP-SMAD1 signaling pathway by
competing with SMAD4 for receptor-activated SMAD1-binding (By
similarity). Acts as a mediator of TGF-beta and BMP antiflammatory
activity. Suppresses IL1R-TLR signaling through its direct
interaction with PEL1, preventing NF-kappa-B activation, nuclear
transport and NF-kappa-B-mediated expression of proinflammatory
genes. {ECO:0000250, ECO:0000269|PubMed:16951688}.
-!- SUBUNIT: Interacts with NEDD4L. Interacts with WWP1. Interacts
with STAMBP and PRKX (By similarity). Interacts with RNF111 and
AXIN1. Interacts with TGF-beta type I receptor superfamily
members, including ACVR1B, BMPR1B and TGFBR1. In response to BMP2
treatment, interacts with SMAD1; this interaction may inhibit
SMAD1-binding to SMAD4. Interacts with HOXC8 and HOXC9 (By
similarity). Interacts with PELI1; this interaction interferes
with PELI1 complex formation with TRAF6, IRAK1, IRAK4 and MYD88 in
response to IL1B and hence negatively regulates IL1R-TLR
signaling. {ECO:0000250, ECO:0000269|PubMed:14657019,
ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:15496141,
ECO:0000269|PubMed:16951688}.
-!- INTERACTION:
O35625:Axin1; NbExp=2; IntAct=EBI-4321242, EBI-2365912;
P36898:Bmpr1b; NbExp=2; IntAct=EBI-4321242, EBI-7107883;
Q9JIF0:Prmt1; NbExp=3; IntAct=EBI-4321242, EBI-519055;
Q9C0C9:UBE2O (xeno); NbExp=4; IntAct=EBI-4321242, EBI-2339946;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitous in various organs, with higher
levels in lung.
-!- INDUCTION: By TGF-beta and BMP4. {ECO:0000269|PubMed:16951688}.
-!- PTM: Monoubiquitinated at Lys-174 by the E2/E3 hybrid ubiquitin-
protein ligase UBE2O, leading to reduced binding affinity for the
activated BMP type I receptor ACVR1/ALK2, thereby enhancing BMP7
and regulating adipocyte differentiation (By similarity).
Ubiquitinated by WWP1 (PubMed:15221015). Ubiquitinated by RNF165,
promoting proteasomal degradation, leading to enhance the BMP-Smad
signaling (PubMed:23610558). {ECO:0000250|UniProtKB:O43541,
ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:23610558}.
-!- PTM: Arginine methylation by PRMT1, which is recruited by BMPR2,
initiates BMP-Induced signaling and induces dissociation from the
BMPR1B receptor at the cell surface leading to derepress
downstream Smad1/Smad5 signaling. {ECO:0000269|PubMed:23747011}.
-!- PTM: Phosphorylated by BMP type 1 receptor kinase and by PRKX.
{ECO:0000250|UniProtKB:O43541}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; AF010133; AAB81351.1; -; mRNA.
EMBL; AK004671; BAB23460.1; -; mRNA.
CCDS; CCDS23273.1; -.
RefSeq; NP_032568.3; NM_008542.3.
RefSeq; XP_006510885.1; XM_006510822.2.
UniGene; Mm.325757; -.
ProteinModelPortal; O35182; -.
SMR; O35182; -.
BioGrid; 201279; 11.
IntAct; O35182; 189.
MINT; O35182; -.
STRING; 10090.ENSMUSP00000036285; -.
iPTMnet; O35182; -.
PhosphoSitePlus; O35182; -.
PaxDb; O35182; -.
PRIDE; O35182; -.
Ensembl; ENSMUST00000041029; ENSMUSP00000036285; ENSMUSG00000036867.
GeneID; 17130; -.
KEGG; mmu:17130; -.
UCSC; uc009qbk.2; mouse.
CTD; 4091; -.
MGI; MGI:1336883; Smad6.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOGENOM; HOG000060106; -.
HOVERGEN; HBG053021; -.
InParanoid; O35182; -.
KO; K04677; -.
OMA; CRTVTCC; -.
OrthoDB; EOG091G0XBN; -.
PhylomeDB; O35182; -.
TreeFam; TF314923; -.
Reactome; R-MMU-201451; Signaling by BMP.
PRO; PR:O35182; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000036867; Expressed in 213 organ(s), highest expression level in lung.
CleanEx; MM_SMAD6; -.
ExpressionAtlas; O35182; baseline and differential.
Genevisible; O35182; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0070410; F:co-SMAD binding; ISO:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
GO; GO:0070411; F:I-SMAD binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0030617; F:transforming growth factor beta receptor, inhibitory cytoplasmic mediator activity; ISO:MGI.
GO; GO:0070698; F:type I activin receptor binding; ISO:MGI.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0035904; P:aorta development; IMP:MGI.
GO; GO:0003180; P:aortic valve morphogenesis; ISO:MGI.
GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
GO; GO:0060948; P:cardiac vascular smooth muscle cell development; TAS:DFLAT.
GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
GO; GO:0060977; P:coronary vasculature morphogenesis; TAS:DFLAT.
GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
GO; GO:0003170; P:heart valve development; IMP:MGI.
GO; GO:0006955; P:immune response; ISO:MGI.
GO; GO:0003183; P:mitral valve morphogenesis; IMP:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0097756; P:negative regulation of blood vessel diameter; TAS:DFLAT.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0030279; P:negative regulation of ossification; IMP:BHF-UCL.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI.
GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
GO; GO:0010991; P:negative regulation of SMAD protein complex assembly; ISO:MGI.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:BHF-UCL.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045907; P:positive regulation of vasoconstriction; TAS:DFLAT.
GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:BHF-UCL.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:InterPro.
GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
GO; GO:0007352; P:zygotic specification of dorsal/ventral axis; ISO:MGI.
Gene3D; 2.60.200.10; -; 1.
Gene3D; 3.90.520.10; -; 1.
InterPro; IPR013790; Dwarfin.
InterPro; IPR003619; MAD_homology1_Dwarfin-type.
InterPro; IPR013019; MAD_homology_MH1.
InterPro; IPR017855; SMAD-like_dom_sf.
InterPro; IPR001132; SMAD_dom_Dwarfin-type.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR036578; SMAD_MH1_sf.
PANTHER; PTHR13703; PTHR13703; 1.
Pfam; PF03165; MH1; 1.
Pfam; PF03166; MH2; 1.
SMART; SM00523; DWA; 1.
SMART; SM00524; DWB; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF56366; SSF56366; 1.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
1: Evidence at protein level;
Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
Methylation; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 495 Mothers against decapentaplegic homolog
6.
/FTId=PRO_0000090870.
DOMAIN 149 276 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 332 495 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
COMPBIAS 25 31 Poly-Gly.
COMPBIAS 81 84 Poly-Arg.
COMPBIAS 166 169 Poly-Leu.
COMPBIAS 276 279 Poly-Pro.
METAL 206 206 Zinc. {ECO:0000250}.
METAL 248 248 Zinc. {ECO:0000250}.
METAL 261 261 Zinc. {ECO:0000250}.
METAL 266 266 Zinc. {ECO:0000250}.
MOD_RES 74 74 Dimethylated arginine; alternate.
{ECO:0000269|PubMed:23747011}.
MOD_RES 74 74 Omega-N-methylarginine; alternate.
{ECO:0000269|PubMed:23747011}.
MOD_RES 81 81 Dimethylated arginine; alternate.
{ECO:0000269|PubMed:23747011}.
MOD_RES 81 81 Omega-N-methylarginine; alternate.
{ECO:0000269|PubMed:23747011}.
MOD_RES 436 436 Phosphoserine; by PRKX; in vitro.
{ECO:0000250|UniProtKB:O43541,
ECO:0000255|PROSITE-ProRule:PRU00439}.
CROSSLNK 174 174 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O43541}.
MUTAGEN 74 74 R->A: Strongly decreased methylation.
{ECO:0000269|PubMed:23747011}.
CONFLICT 176 177 VT -> AQ (in Ref. 2; BAB23460).
{ECO:0000305}.
SEQUENCE 495 AA; 53714 MW; D9282D42B120C507 CRC64;
MFRSKRSGLV RRLWRSRVVP DREEGSGGGG GVDEDGSLGS RAEPAPRARE GGGCSRSEVR
SVAPRRPRDA VGPRGAAIAG RRRRTGGLPR PVSESGAGAG GSPLDVAEPG GPGWLPESDC
ETVTCCLFSE RDAAGAPRDS GDPQARQSPE PEEGGGPRSR EARSRLLLLE QELKTVTYSL
LKRLKERSLD TLLEAVESRG GVPGGCVLVP RADLRLGGQP APPQLLLGRL FRWPDLQHAV
ELKPLCGCHS FTAAADGPTV CCNPYHFSRL CGPESPPPPY SRLSPPDQYK PLDLSDSTLS
YTETEATNSL ITAPGEFSDA SMSPDATKPS HWCSVAYWEH RTRVGRLYAV YDQAVSIFYD
LPQGSGFCLG QLNLEQRSES VRRTRSKIGF GILLSKEPDG VWAYNRGEHP IFVNSPTLDA
PGGRALVVRK VPPGYSIKVF DFERSGLLQH ADAAHGPYDP HSVRISFAKG WGPCYSRQFI
TSCPCWLEIL LNNHR


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U2184h CLIA hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,Smad2,S 96T
E2185h ELISA kit hMAD-3,Homo sapiens,hSMAD3,Human,JV15-2,MAD homolog 3,Mad3,MADH3,Mothers against decapentaplegic homolog 3,Mothers against DPP homolog 3,SMAD 3,SMAD family member 3,Smad3,SMAD3 96T


 

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