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Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (mMad3) (SMAD family member 3) (SMAD 3) (Smad3)

 SMAD3_MOUSE             Reviewed;         425 AA.
Q8BUN5; O09064; O09144; O14510; O35273; Q8BX84; Q92940; Q93002;
Q9GKR4;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 2.
30-AUG-2017, entry version 151.
RecName: Full=Mothers against decapentaplegic homolog 3;
Short=MAD homolog 3;
Short=Mad3;
Short=Mothers against DPP homolog 3;
Short=mMad3;
AltName: Full=SMAD family member 3;
Short=SMAD 3;
Short=Smad3;
Name=Smad3; Synonyms=Madh3;
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], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=10331191; DOI=10.1292/jvms.61.213;
Kano K., Notani A., Nam S.-Y., Fujisawa M., Kurohmaru M., Hayashi Y.;
"Cloning and studies of the mouse cDNA encoding Smad3.";
J. Vet. Med. Sci. 61:213-219(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
Yang X., Xu X., Shen S., Deng C.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Head, and Hippocampus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION AT SER-422; SER-423 AND SER-425.
PubMed=9380693; DOI=10.1073/pnas.94.20.10669;
Liu X., Sun Y., Constantinescu S.N., Karam E., Weinberg R.A.,
Lodish H.F.;
"Transforming growth factor beta-induced phosphorylation of Smad3 is
required for growth inhibition and transcriptional induction in
epithelial cells.";
Proc. Natl. Acad. Sci. U.S.A. 94:10669-10674(1997).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10559937; DOI=10.1038/12971;
Ashcroft G.S., Yang X., Glick A.B., Weinstein M., Letterio J.L.,
Mizel D.E., Anzano M., Greenwell-Wild T., Wahl S.M., Deng C.,
Roberts A.B.;
"Mice lacking Smad3 show accelerated wound healing and an impaired
local inflammatory response.";
Nat. Cell Biol. 1:260-266(1999).
[7]
INTERACTION WITH AIP1, AND IDENTIFICATION IN A COMPLEX WITH AIP1;
ACVR2A AND ACVR1B.
PubMed=10681527; DOI=10.1074/jbc.275.8.5485;
Shoji H., Tsuchida K., Kishi H., Yamakawa N., Matsuzaki T., Liu Z.,
Nakamura T., Sugino H.;
"Identification and characterization of a PDZ protein that interacts
with activin types II receptors.";
J. Biol. Chem. 275:5485-5492(2000).
[8]
INTERACTION WITH HGS.
PubMed=11094085; DOI=10.1128/MCB.20.24.9346-9355.2000;
Miura S., Takeshita T., Asao H., Kimura Y., Murata K., Sasaki Y.,
Hanai J., Beppu H., Tsukazaki T., Wrana J.L., Miyazono K.,
Sugamura K.;
"Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling
through cooperation with SARA.";
Mol. Cell. Biol. 20:9346-9355(2000).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=11585338; DOI=10.1359/jbmr.2001.16.10.1754;
Borton A.J., Frederick J.P., Datto M.B., Wang X.F., Weinstein R.S.;
"The loss of Smad3 results in a lower rate of bone formation and
osteopenia through dysregulation of osteoblast differentiation and
apoptosis.";
J. Bone Miner. Res. 16:1754-1764(2001).
[10]
INTERACTION WITH ZNF8.
PubMed=12370310; DOI=10.1128/MCB.22.21.7633-7644.2002;
Jiao K., Zhou Y., Hogan B.L.M.;
"Identification of mZnf8, a mouse Kruppel-like transcriptional
repressor, as a novel nuclear interaction partner of Smad1.";
Mol. Cell. Biol. 22:7633-7644(2002).
[11]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=14617288; DOI=10.1046/j.1524-475X.2003.11614.x;
Ashcroft G.S., Mills S.J., Flanders K.C., Lyakh L.A., Anzano M.A.,
Gilliver S.C., Roberts A.B.;
"Role of Smad3 in the hormonal modulation of in vivo wound healing
responses.";
Wound Repair Regen. 11:468-473(2003).
[12]
INTERACTION WITH TGFB1I1.
PubMed=14755691; DOI=10.1002/jcb.10754;
Shibanuma M., Kim-Kaneyama J.-R., Sato S., Nose K.;
"A LIM protein, Hic-5, functions as a potential coactivator for Sp1.";
J. Cell. Biochem. 91:633-645(2004).
[13]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
PML AND ZFYVE9/SARA.
PubMed=15356634; DOI=10.1038/nature02783;
Lin H.K., Bergmann S., Pandolfi P.P.;
"Cytoplasmic PML function in TGF-beta signalling.";
Nature 431:205-211(2004).
[14]
INTERACTION WITH WWP1.
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).
[15]
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).
[16]
INTERACTION WITH ZC3H3.
PubMed=16115198; DOI=10.1111/j.1365-2443.2005.00887.x;
Collart C., Remacle J.E., Barabino S., van Grunsven L.A., Nelles L.,
Schellens A., Van de Putte T., Pype S., Huylebroeck D.,
Verschueren K.;
"Smicl is a novel Smad interacting protein and cleavage and
polyadenylation specificity factor associated protein.";
Genes Cells 10:897-906(2005).
[17]
INTERACTION WITH PRDM16.
PubMed=17467076; DOI=10.1016/j.bbamcr.2007.03.016;
Warner D.R., Horn K.H., Mudd L., Webb C.L., Greene R.M., Pisano M.M.;
"PRDM16/MEL1: a novel Smad binding protein expressed in murine
embryonic orofacial tissue.";
Biochim. Biophys. Acta 1773:814-820(2007).
[18]
INTERACTION WITH TTRAP.
PubMed=18039968; DOI=10.1242/dev.000026;
Esguerra C.V., Nelles L., Vermeire L., Ibrahimi A., Crawford A.D.,
Derua R., Janssens E., Waelkens E., Carmeliet P., Collen D.,
Huylebroeck D.;
"Ttrap is an essential modulator of Smad3-dependent Nodal signaling
during zebrafish gastrulation and left-right axis determination.";
Development 134:4381-4393(2007).
[19]
INTERACTION WITH FOXL2.
PubMed=19106105; DOI=10.1074/jbc.M806676200;
Blount A.L., Schmidt K., Justice N.J., Vale W.W., Fischer W.H.,
Bilezikjian L.M.;
"FoxL2 and Smad3 coordinately regulate follistatin gene
transcription.";
J. Biol. Chem. 284:7631-7645(2009).
[20]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=21035443; DOI=10.1016/j.yexmp.2010.10.011;
Kawakatsu M., Kanno S., Gui T., Gai Z., Itoh S., Tanishima H.,
Oikawa K., Muragaki Y.;
"Loss of Smad3 gives rise to poor soft callus formation and
accelerates early fracture healing.";
Exp. Mol. Pathol. 90:107-115(2011).
[21]
INTERACTION WITH PPP5C, AND SUBCELLULAR LOCATION.
PubMed=22781750; DOI=10.1016/j.cellsig.2012.07.003;
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.;
"Protein phosphatase 5 modulates SMAD3 function in the transforming
growth factor-beta pathway.";
Cell. Signal. 24:1999-2006(2012).
[22]
INTERACTION WITH RNF111, AND UBIQUITINATION.
PubMed=17341133; DOI=10.1371/journal.pbio.0050067;
Mavrakis K.J., Andrew R.L., Lee K.L., Petropoulou C., Dixon J.E.,
Navaratnam N., Norris D.P., Episkopou V.;
"Arkadia enhances Nodal/TGF-beta signaling by coupling phospho-Smad2/3
activity and turnover.";
PLoS Biol. 5:E67-E67(2007).
-!- FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an
intracellular signal transducer and transcriptional modulator
activated by TGF-beta (transforming growth factor) and activin
type 1 receptor kinases. Binds the TRE element in the promoter
region of many genes that are regulated by TGF-beta and, on
formation of the SMAD3/SMAD4 complex, activates transcription.
Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site
to regulate TGF-beta-mediated transcription. Has an inhibitory
effect on wound healing probably by modulating both growth and
migration of primary keratinocytes and by altering the TGF-
mediated chemotaxis of monocytes. This effect on wound healing
appears to be hormone-sensitive. Regulator of chondrogenesis and
osteogenesis and inhibits early healing of bone fractures.
Positively regulates PDPK1 kinase activity by stimulating its
dissociation from the 14-3-3 protein YWHAQ which acts as a
negative regulator (By similarity). {ECO:0000250|UniProtKB:P84022,
ECO:0000269|PubMed:10559937, ECO:0000269|PubMed:11585338,
ECO:0000269|PubMed:14617288, ECO:0000269|PubMed:15356634,
ECO:0000269|PubMed:21035443}.
-!- SUBUNIT: Monomer; in the absence of TGF-beta. Homooligomer; in the
presence of TGF-beta. Heterotrimer; forms a heterotrimer in the
presence of TGF-beta consisting of two molecules of C-terminally
phosphorylated SMAD2 or SMAD3 and one of SMAD4 to form the
transcriptionally active SMAD2/SMAD3-SMAD4 complex. Interacts with
TGFBR1. Interacts (via MH2 domain) with CITED2 (via C-terminus).
Interacts (via the MH2 domain) with ZFYVE9. Interacts with HDAC1,
VDR, TGIF and TGIF2, RUNX3, CREBBP, SKOR1, SKOR2, SNON, ATF2,
SMURF2 and SNW1. Interacts with DACH1; the interaction inhibits
the TGF-beta signaling. Part of a complex consisting of AIP1,
ACVR2A, ACVR1B and SMAD3. Forms a complex with SMAD2 and TRIM33
upon addition of TGF-beta. Found in a complex with SMAD3, RAN and
XPO4. Interacts in the complex directly with XPO4. Interacts (via
the MH2 domain) with LEMD3; the interaction represses SMAD3
transcriptional activity through preventing the formation of the
heteromeric complex with SMAD4 and translocation to the nucleus.
Interacts with RBPMS. Interacts (via MH2 domain) with MECOM.
Interacts with WWTR1 (via its coiled-coil domain). Interacts (via
the linker region) with EP300 (C-terminal); the interaction
promotes SMAD3 acetylation and is enhanced by TGF-beta
phosphorylation in the C-terminal of SMAD3. This interaction can
be blocked by competitive binding of adenovirus oncoprotein E1A to
the same C-terminal site on EP300, which then results in partially
inhibited SMAD3/SMAD4 transcriptional activity. Interacts with
SKI; the interaction represses SMAD3 transcriptional activity.
Component of the multimeric complex SMAD3/SMAD4/JUN/FOS which
forms at the AP1 promoter site; required for synergistic
transcriptional activity in response to TGF-beta. Interacts (via
an N-terminal domain) with JUN (via its basic DNA binding and
leucine zipper domains); this interaction is essential for DNA
binding and cooperative transcriptional activity in response to
TGF-beta. Interacts with PPM1A; the interaction dephosphorylates
SMAD3 in the C-terminal SXS motif leading to disruption of the
SMAD2/3-SMAD4 complex, nuclear export and termination of TGF-beta
signaling. Interacts (dephosphorylated form via the MH1 and MH2
domains) with RANBP3 (via its C-terminal R domain); the
interaction results in the export of dephosphorylated SMAD3 out of
the nucleus and termination of the TGF-beta signaling. Interacts
with AIP1, TGFB1I1, TTRAP, FOXL2, PRDM16, HGS and WWP1. Interacts
with NEDD4L; the interaction requires TGF-beta stimulation.
Interacts with PML. Interacts with MEN1. Interaction with CSNK1G2.
Interacts with PDPK1 (via PH domain). Interacts with DAB2; the
interactions are enhanced upon TGF-beta stimulation. Interacts
with USP15. Interacts with PPP5C; the interaction decreases SMAD3
phosphorylation and protein levels. Interacts with LDLRAD4 (via
the SMAD interaction motif). Interacts with PMEPA1. Interacts with
ZC3H3 (PubMed:16115198). Interacts with ZFHX3 (By similarity).
Interacts with ZNF451. Identified in a complex that contains at
least ZNF451, SMAD2, SMAD3 and SMAD4 (By similarity). Interacts
weakly with ZNF8 (PubMed:12370310). Interacts (when
phosphorylated) with RNF111; RNF111 acts as an enhancer of the
transcriptional responses by mediating ubiquitination and
degradation of SMAD3 inhibitors (PubMed:17341133). Interacts with
STUB1, HSPA1A, HSPA1B, HSP90AA1 and HSP90AB1 (By similarity).
{ECO:0000250|UniProtKB:P84022, ECO:0000269|PubMed:10681527,
ECO:0000269|PubMed:11094085, ECO:0000269|PubMed:12370310,
ECO:0000269|PubMed:14755691, ECO:0000269|PubMed:15221015,
ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:15496141,
ECO:0000269|PubMed:16115198, ECO:0000269|PubMed:17341133,
ECO:0000269|PubMed:17467076, ECO:0000269|PubMed:18039968,
ECO:0000269|PubMed:19106105, ECO:0000269|PubMed:22781750}.
-!- INTERACTION:
O35625:Axin1; NbExp=2; IntAct=EBI-2337983, EBI-2365912;
P20263:Pou5f1; NbExp=13; IntAct=EBI-2337983, EBI-1606219;
P97471:Smad4; NbExp=5; IntAct=EBI-2337983, EBI-5259270;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15356634,
ECO:0000269|PubMed:22781750}. Nucleus
{ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:22781750}.
Note=Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-
beta stimulation, migrates to the nucleus when complexed with
SMAD4. Through the action of the phosphatase PPM1A, released from
the SMAD2/SMAD4 complex, and exported out of the nucleus by
interaction with RANBP1. Co-localizes with LEMD3 at the nucleus
inner membrane. MAPK-mediated phosphorylation appears to have no
effect on nuclear import. PDPK1 prevents its nuclear translocation
in response to TGF-beta. {ECO:0000250|UniProtKB:P84022}.
-!- TISSUE SPECIFICITY: Highly expressed in the brain and ovary.
Detected in the pyramidal cells of the hippocampus, granule cells
of the dentate gyrus, granular cells of the cerebral cortex and
the granulosa cells of the ovary. {ECO:0000269|PubMed:10331191}.
-!- DOMAIN: The MH1 domain is required for DNA binding (By
similarity). Also binds zinc ions which are necessary for the DNA
binding. {ECO:0000250}.
-!- DOMAIN: The MH2 domain is required for both homomeric and
heteromeric interactions and for transcriptional regulation.
Sufficient for nuclear import (By similarity). {ECO:0000250}.
-!- DOMAIN: The linker region is required for the TGFbeta-mediated
transcriptional activity and acts synergistically with the MH2
domain. {ECO:0000250}.
-!- PTM: Phosphorylated on serine and threonine residues. Enhanced
phosphorylation in the linker region on Thr-179, Ser-204 and Ser-
208 on EGF and TGF-beta treatment. Ser-208 is the main site of
MAPK-mediated phosphorylation. CDK-mediated phosphorylation occurs
in a cell-cycle dependent manner and inhibits both the
transcriptional activity and antiproliferative functions of SMAD3.
This phosphorylation is inhibited by flavopiridol. Maximum
phosphorylation at the G(1)/S junction. Also phosphorylated on
serine residues in the C-terminal SXS motif by TGFBR1 and ACVR1.
TGFBR1-mediated phosphorylation at these C-terminal sites is
required for interaction with SMAD4, nuclear location and
transactivational activity, and appears to be a prerequisite for
the TGF-beta mediated phosphorylation in the linker region.
Dephosphorylated in the C-terminal SXS motif by PPM1A. This
dephosphorylation disrupts the interaction with SMAD4, promotes
nuclear export and terminates TGF-beta-mediated signaling.
Phosphorylation at Ser-418 by CSNK1G2/CK1 promotes ligand-
dependent ubiquitination and subsequent proteasome degradation,
thus inhibiting SMAD3-mediated TGF-beta responses (By similarity).
Phosphorylated by PDPK1 (By similarity).
{ECO:0000250|UniProtKB:P84022}.
-!- PTM: Acetylation in the nucleus by EP300 in the MH2 domain
regulates positively its transcriptional activity and is enhanced
by TGF-beta. {ECO:0000250|UniProtKB:P84022}.
-!- PTM: Ubiquitinated. Monoubiquitinated, leading to prevent DNA-
binding. Deubiquitination by USP15 alleviates inhibition and
promotes activation of TGF-beta target genes (By similarity).
Ubiquitinated by RNF111, leading to its degradation: only SMAD3
proteins that are 'in use' are targeted by RNF111, RNF111 playing
a key role in activating SMAD3 and regulating its turnover
(PubMed:17341133). Undergoes STUB1-mediated ubiquitination and
degradation (By similarity). {ECO:0000250|UniProtKB:P84022,
ECO:0000269|PubMed:17341133}.
-!- PTM: Poly-ADP-ribosylated by PARP1 and PARP2. ADP-ribosylation
negatively regulates SMAD3 transcriptional responses during the
course of TGF-beta signaling. {ECO:0000250|UniProtKB:P84022}.
-!- DISRUPTION PHENOTYPE: SMAD3 null mice exhibit inhibition of
proliferation of mammary gland epithelial cells. Fibrobasts are
only partially growth inhibited. Defects in osteoblast
differentiation are observed. Animals are osteopenic with less
cortical and cancellous bone. Facture healing is accelerated.
Decreased bone mineral density (BMD) reflects the inability of
osteoblasts to balance osteoclast activity. Wound healing is
accelerated to about two and a half times that of normal animals.
Wound areas are significantly reduced with less quantities of
granulation tissue. There is reduced local infiltration of
moncytes and keratinocytes show altered patterns of growth and
migration. Accelerated wound healing is observed on castration of
null male mice, while null female mice exhibited delayed healing
following ovariectomy. {ECO:0000269|PubMed:10559937,
ECO:0000269|PubMed:11585338, ECO:0000269|PubMed:14617288,
ECO:0000269|PubMed:21035443}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; AB008192; BAA76956.1; -; mRNA.
EMBL; AF016189; AAB81755.1; -; mRNA.
EMBL; AK048626; BAC33398.1; -; mRNA.
EMBL; AK083158; BAC38789.1; -; mRNA.
EMBL; BC066850; AAH66850.1; -; mRNA.
CCDS; CCDS23272.1; -.
RefSeq; NP_058049.3; NM_016769.4.
UniGene; Mm.7320; -.
ProteinModelPortal; Q8BUN5; -.
SMR; Q8BUN5; -.
BioGrid; 201276; 68.
DIP; DIP-29717N; -.
IntAct; Q8BUN5; 45.
MINT; MINT-262056; -.
STRING; 10090.ENSMUSP00000034973; -.
iPTMnet; Q8BUN5; -.
PhosphoSitePlus; Q8BUN5; -.
MaxQB; Q8BUN5; -.
PaxDb; Q8BUN5; -.
PeptideAtlas; Q8BUN5; -.
PRIDE; Q8BUN5; -.
Ensembl; ENSMUST00000034973; ENSMUSP00000034973; ENSMUSG00000032402.
GeneID; 17127; -.
KEGG; mmu:17127; -.
UCSC; uc009qbi.1; mouse.
CTD; 4088; -.
MGI; MGI:1201674; Smad3.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOVERGEN; HBG053353; -.
InParanoid; Q8BUN5; -.
KO; K04500; -.
OMA; SDHQMTH; -.
OrthoDB; EOG091G082C; -.
PhylomeDB; Q8BUN5; -.
TreeFam; TF314923; -.
Reactome; R-MMU-1181150; Signaling by NODAL.
Reactome; R-MMU-1502540; Signaling by Activin.
Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-8941855; RUNX3 regulates CDKN1A transcription.
PRO; PR:Q8BUN5; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032402; -.
CleanEx; MM_SMAD3; -.
ExpressionAtlas; Q8BUN5; baseline and differential.
Genevisible; Q8BUN5; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0071141; C:SMAD protein complex; ISS:UniProtKB.
GO; GO:0071144; C:SMAD2-SMAD3 protein complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
GO; GO:0043425; F:bHLH transcription factor binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:BHF-UCL.
GO; GO:0070410; F:co-SMAD binding; ISO:MGI.
GO; GO:0005518; F:collagen binding; IPI:MGI.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:MGI.
GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
GO; GO:0035259; F:glucocorticoid receptor binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0031962; F:mineralocorticoid receptor binding; ISO:MGI.
GO; GO:0019902; F:phosphatase binding; ISO:MGI.
GO; GO:0070878; F:primary miRNA binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0000988; F:transcription factor activity, protein binding; IEA:Ensembl.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:MGI.
GO; GO:0030618; F:transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity; ISO:MGI.
GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0032924; P:activin receptor signaling pathway; ISO:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
GO; GO:0045216; P:cell-cell junction organization; ISO:MGI.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
GO; GO:0048589; P:developmental growth; IGI:MGI.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IGI:MGI.
GO; GO:0048617; P:embryonic foregut morphogenesis; IGI:MGI.
GO; GO:0009880; P:embryonic pattern specification; IGI:MGI.
GO; GO:0007492; P:endoderm development; IGI:MGI.
GO; GO:0019049; P:evasion or tolerance of host defenses by virus; ISO:MGI.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0007369; P:gastrulation; IGI:MGI.
GO; GO:0001947; P:heart looping; IGI:MGI.
GO; GO:0006955; P:immune response; ISO:MGI.
GO; GO:0002520; P:immune system development; IGI:MGI.
GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0070306; P:lens fiber cell differentiation; IMP:MGI.
GO; GO:0001889; P:liver development; IGI:MGI.
GO; GO:0001707; P:mesoderm formation; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:MGI.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
GO; GO:0061767; P:negative regulation of lung blood pressure; IEA:Ensembl.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IGI:MGI.
GO; GO:0033689; P:negative regulation of osteoblast proliferation; IMP:UniProtKB.
GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0061045; P:negative regulation of wound healing; IMP:UniProtKB.
GO; GO:0038092; P:nodal signaling pathway; ISO:MGI.
GO; GO:0002076; P:osteoblast development; IGI:MGI.
GO; GO:0001649; P:osteoblast differentiation; IMP:UniProtKB.
GO; GO:0048340; P:paraxial mesoderm morphogenesis; IMP:MGI.
GO; GO:0060039; P:pericardium development; IGI:MGI.
GO; GO:0010694; P:positive regulation of alkaline phosphatase activity; IEA:Ensembl.
GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
GO; GO:0035413; P:positive regulation of catenin import into nucleus; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:1901203; P:positive regulation of extracellular matrix assembly; ISO:MGI.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IEA:Ensembl.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0032916; P:positive regulation of transforming growth factor beta3 production; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
GO; GO:0051098; P:regulation of binding; IDA:MGI.
GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
GO; GO:0016202; P:regulation of striated muscle tissue development; IDA:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; ISO:MGI.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
GO; GO:0001501; P:skeletal system development; IGI:MGI.
GO; GO:0007183; P:SMAD protein complex assembly; ISO:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; IGI:MGI.
GO; GO:0001756; P:somitogenesis; IMP:MGI.
GO; GO:0042110; P:T cell activation; IMP:UniProtKB.
GO; GO:0030878; P:thyroid gland development; IGI:MGI.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0060290; P:transdifferentiation; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:0006810; P:transport; ISO:MGI.
GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
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_dom-like.
InterPro; IPR001132; SMAD_dom_Dwarfin-type.
InterPro; IPR008984; SMAD_FHA_domain.
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;
Acetylation; ADP-ribosylation; Complete proteome; Cytoplasm;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P84022}.
CHAIN 2 425 Mothers against decapentaplegic homolog
3.
/FTId=PRO_0000090857.
DOMAIN 10 136 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 232 425 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
REGION 137 231 Linker.
REGION 271 324 Sufficient for interaction with XPO4.
{ECO:0000250}.
METAL 64 64 Zinc. {ECO:0000250}.
METAL 109 109 Zinc. {ECO:0000250}.
METAL 121 121 Zinc. {ECO:0000250}.
METAL 126 126 Zinc. {ECO:0000250}.
SITE 40 40 Required for trimerization.
{ECO:0000250}.
SITE 41 41 Required for interaction with DNA and JUN
and for functional cooperation with JUN.
{ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P84022}.
MOD_RES 8 8 Phosphothreonine; by CDK2 and CDK4.
{ECO:0000250|UniProtKB:P84022}.
MOD_RES 179 179 Phosphothreonine; by CDK2, CDK4 and MAPK.
{ECO:0000250|UniProtKB:P84022}.
MOD_RES 204 204 Phosphoserine; by GSK3 and MAPK.
{ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 208 208 Phosphoserine; by MAPK.
{ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 213 213 Phosphoserine; by CDK2 and CDK4.
{ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 378 378 N6-acetyllysine.
{ECO:0000250|UniProtKB:P84022}.
MOD_RES 416 416 Phosphoserine.
{ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 418 418 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:P84022,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 422 422 Phosphoserine; by TGFBR1.
{ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:9380693}.
MOD_RES 423 423 Phosphoserine; by TGFBR1.
{ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:9380693}.
MOD_RES 425 425 Phosphoserine; by TGFBR1.
{ECO:0000255|PROSITE-ProRule:PRU00439,
ECO:0000269|PubMed:9380693}.
CONFLICT 26 26 Q -> E (in Ref. 3; BAC38789).
{ECO:0000305}.
CONFLICT 269 269 F -> L (in Ref. 2; AAB81755).
{ECO:0000305}.
CONFLICT 408 408 D -> V (in Ref. 3; BAC33398).
{ECO:0000305}.
SEQUENCE 425 AA; 48081 MW; 46DF5E8B371321AC CRC64;
MSSILPFTPP IVKRLLGWKK GEQNGQEEKW CEKAVKSLVK KLKKTGQLDE LEKAITTQNV
NTKCITIPRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELRAMELCE FAFNMKKDEV
CVNPYHYQRV ETPVLPPVLV PRHTEIPAEF PPLDDYSHSI PENTNFPAGI EPQSNIPETP
PPGYLSEDGE TSDHQMNHSM DAGSPNLSPN PMSPAHNNLD LQPVTYCEPA FWCSISYYEL
NQRVGETFHA SQPSMTVDGF TDPSNSERFC LGLLSNVNRN AAVELTRRHI GRGVRLYYIG
GEVFAECLSD SAIFVQSPNC NQRYGWHPAT VCKIPPGCNL KIFNNQEFAA LLAQSVNQGF
EAVYQLTRMC TIRMSFVKGW GAEYRRQTVT STPCWIELHL NGPLQWLDKV LTQMGSPSIR
CSSVS


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