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Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (Deletion target in pancreatic carcinoma 4 homolog) (SMAD family member 4) (SMAD 4) (Smad4)

 SMAD4_MOUSE             Reviewed;         551 AA.
P97471; Q6GTP6; Q9CW56;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-OCT-2017, entry version 170.
RecName: Full=Mothers against decapentaplegic homolog 4;
Short=MAD homolog 4;
Short=Mothers against DPP homolog 4;
AltName: Full=Deletion target in pancreatic carcinoma 4 homolog;
AltName: Full=SMAD family member 4;
Short=SMAD 4;
Short=Smad4;
Name=Smad4; Synonyms=Dpc4, Madh4;
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].
STRAIN=A/J; TISSUE=Lung;
PubMed=9166592; DOI=10.1007/s003359900465;
Anna C.H., Devereux T.R.;
"Sequence and chromosomal mapping of the mouse homolog (Madh4) of the
human DPC4/MADH4 gene.";
Mamm. Genome 8:443-444(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Olfactory epithelium;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-551.
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).
[5]
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).
[6]
FUNCTION, DNA-BINDING, AND IDENTIFICATION IN A COMPLEX WITH SMAD1 AND
YY1.
PubMed=15329343; DOI=10.1242/dev.01344;
Lee K.H., Evans S., Ruan T.Y., Lassar A.B.;
"SMAD-mediated modulation of YY1 activity regulates the BMP response
and cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5
enhancer.";
Development 131:4709-4723(2004).
[7]
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24076600; DOI=10.1038/ng.2772;
Sartori R., Schirwis E., Blaauw B., Bortolanza S., Zhao J., Enzo E.,
Stantzou A., Mouisel E., Toniolo L., Ferry A., Stricker S.,
Goldberg A.L., Dupont S., Piccolo S., Amthor H., Sandri M.;
"BMP signaling controls muscle mass.";
Nat. Genet. 45:1309-1318(2013).
[10]
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 9-140 IN COMPLEX WITH DNA,
ZINC_BINDING SITES, AND SUBUNIT.
PubMed=20147459; DOI=10.1093/nar/gkq046;
Baburajendran N., Palasingam P., Narasimhan K., Sun W., Prabhakar S.,
Jauch R., Kolatkar P.R.;
"Structure of Smad1 MH1/DNA complex reveals distinctive rearrangements
of BMP and TGF-beta effectors.";
Nucleic Acids Res. 38:3477-3488(2010).
-!- FUNCTION: Common SMAD (co-SMAD) is the coactivator and mediator of
signal transduction by TGF-beta (transforming growth factor).
Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that
forms in the nucleus and is required for the TGF-mediated
signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to
DNA and provides an activation function required for SMAD1 or
SMAD2 to stimulate transcription. Component of the multimeric
SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site;
required for synergistic transcriptional activity in response to
TGF-beta. May act as a tumor suppressor. Positively regulates
PDPK1 kinase activity by stimulating its dissociation from the 14-
3-3 protein YWHAQ which acts as a negative regulator (By
similarity). Acts synergistically with SMAD1 and YY1 in bone
morphogenetic protein (BMP)-mediated cardiac-specific gene
expression (PubMed:15329343). Binds to SMAD binding elements
(SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of
cardiac activating regions (PubMed:15329343). In muscle
physiology, plays a central role in the balance between atrophy
and hypertrophy. When recruited by MSTN, promotes atrophy response
via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and
subsequent recruitment by the BMP pathway to promote hypertrophy
via phosphorylated SMAD1/5/8. {ECO:0000250,
ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:24076600}.
-!- SUBUNIT: Monomer (By similarity). Heterotrimer; with a C-
terminally phosphorylated R-SMAD molecule and to form the
transcriptionally active SMAD2/3-SMAD4 complex (By similarity).
Found in a ternary complex composed of SMAD4, STK11/LKB1 and
STK11IP. Interacts with ATF2, COPS5, DACH1, MSG1, SKI, STK11/LKB1,
STK11IP and TRIM33. Associates with ZNF423 or ZNF521 in response
to BMP2 leading to activate transcription of BMP target genes.
Interacts with USP9X. Interacts with RBPMS. Interacts with WWTR1
(via coiled-coil domain). Interacts with CITED1 and CITED2 (By
similarity). Interacts with PDPK1 (via PH domain) (By similarity).
Interacts with VPS39; this interaction affects heterodimer
formation with SMAD3, but not with SMAD2, and leads to inhibition
of SMAD3-dependent transcription activation (By similarity).
Interactions with VPS39 and SMAD2 may be mutually exclusive (By
similarity). Interacts (via MH2 domain) with ZNF451 (via N-
terminal zinc-finger domains) (By similarity). Identified in a
complex that contains at least ZNF451, SMAD2, SMAD3 and SMAD4 (By
similarity). Found in a complex with SMAD1 and YY1
(PubMed:15329343). Interacts with ZC3H3 (PubMed:16115198).
Interacts weakly with ZNF8 (PubMed:12370310). Interacts with NUP93
and IPO7; translocates SMAD4 to the nucleus through the NPC upon
BMP7 stimulation resulting in activation of SMAD4 signaling (By
similarity). Interacts with CREB3L1, the interaction takes place
upon TGFB1 induction and SMAD4 acts as CREB3L1 coactivator to
induce the expression of genes involved in the assembly of
collagen extracellular matrix (By similarity). Interacts with DLX1
(By similarity). {ECO:0000250|UniProtKB:O70437,
ECO:0000250|UniProtKB:Q13485, ECO:0000269|PubMed:12370310,
ECO:0000269|PubMed:15329343, ECO:0000269|PubMed:16115198,
ECO:0000269|PubMed:20147459}.
-!- INTERACTION:
Q8R1H0:Hopx; NbExp=2; IntAct=EBI-5259270, EBI-6913924;
Q62432:Smad2; NbExp=3; IntAct=EBI-5259270, EBI-2337932;
Q8BUN5:Smad3; NbExp=6; IntAct=EBI-5259270, EBI-2337983;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13485}.
Nucleus {ECO:0000250|UniProtKB:Q13485}. Note=In the cytoplasm in
the absence of ligand. Migration to the nucleus when complexed
with R-SMAD. PDPK1 prevents its nuclear translocation.
{ECO:0000250|UniProtKB:Q13485}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The MH1 domain is required for DNA binding.
-!- DOMAIN: The MH2 domain is required for both homomeric and
heteromeric interactions and for transcriptional regulation.
Sufficient for nuclear import (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated by PDPK1. {ECO:0000250}.
-!- PTM: Monoubiquitinated on Lys-518 by E3 ubiquitin-protein ligase
TRIM33. Monoubiquitination hampers its ability to form a stable
complex with activated SMAD2/3 resulting in inhibition of TGF-
beta/BMP signaling cascade. Deubiquitination by USP9X restores its
competence to mediate TGF-beta signaling (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Conditional knockout in muscle leads to
muscle atrophy and weakness. Mutant mice loose significantly more
muscle mass after denervation as compared to wild-type animals and
show excessive proteolysis in denervated muscle. The loss of
maximal absolute force after fasting is greater in mutant mice
than in controls. {ECO:0000269|PubMed:24076600}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; U79748; AAB57905.1; -; mRNA.
EMBL; CH466528; EDL09560.1; -; Genomic_DNA.
EMBL; BC046584; AAH46584.1; -; mRNA.
EMBL; AK004804; BAB23576.1; -; mRNA.
CCDS; CCDS29337.1; -.
RefSeq; NP_032566.2; NM_008540.2.
UniGene; Mm.100399; -.
PDB; 3QSV; X-ray; 2.71 A; A/B/C/D=9-140.
PDBsum; 3QSV; -.
ProteinModelPortal; P97471; -.
SMR; P97471; -.
BioGrid; 201277; 29.
CORUM; P97471; -.
DIP; DIP-29718N; -.
IntAct; P97471; 6.
MINT; MINT-261841; -.
STRING; 10090.ENSMUSP00000025393; -.
iPTMnet; P97471; -.
PhosphoSitePlus; P97471; -.
EPD; P97471; -.
MaxQB; P97471; -.
PaxDb; P97471; -.
PRIDE; P97471; -.
Ensembl; ENSMUST00000025393; ENSMUSP00000025393; ENSMUSG00000024515.
Ensembl; ENSMUST00000114939; ENSMUSP00000110589; ENSMUSG00000024515.
GeneID; 17128; -.
KEGG; mmu:17128; -.
UCSC; uc008fou.1; mouse.
CTD; 4089; -.
MGI; MGI:894293; Smad4.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOGENOM; HOG000286019; -.
HOVERGEN; HBG053353; -.
InParanoid; P97471; -.
KO; K04501; -.
OMA; DIGTIQH; -.
OrthoDB; EOG091G05Z9; -.
TreeFam; TF314923; -.
Reactome; R-MMU-1181150; Signaling by NODAL.
Reactome; R-MMU-1502540; Signaling by Activin.
Reactome; R-MMU-201451; Signaling by BMP.
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.
ChiTaRS; Smad4; mouse.
EvolutionaryTrace; P97471; -.
PRO; PR:P97471; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024515; -.
CleanEx; MM_SMAD4; -.
Genevisible; P97471; MM.
GO; GO:0032444; C:activin responsive factor complex; ISO:MGI.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0071141; C:SMAD protein complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0005518; F:collagen binding; IPI:MGI.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
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:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
GO; GO:0070412; F:R-SMAD 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:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:BHF-UCL.
GO; GO:0043199; F:sulfate binding; ISO:MGI.
GO; GO:0001076; F:transcription factor activity, RNA polymerase II transcription factor binding; IDA:BHF-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0030616; F:transforming growth factor beta receptor, common-partner cytoplasmic mediator activity; ISO:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0036302; P:atrioventricular canal development; IGI:BHF-UCL.
GO; GO:0003190; P:atrioventricular valve formation; IGI:BHF-UCL.
GO; GO:0007411; P:axon guidance; IMP:MGI.
GO; GO:0030509; P:BMP signaling pathway; IMP:BHF-UCL.
GO; GO:0003360; P:brainstem development; IMP:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
GO; GO:0003279; P:cardiac septum development; IGI:BHF-UCL.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:BHF-UCL.
GO; GO:0048589; P:developmental growth; IMP:MGI.
GO; GO:0042733; P:embryonic digit morphogenesis; IMP:CACAO.
GO; GO:0060956; P:endocardial cell differentiation; IMP:BHF-UCL.
GO; GO:0007492; P:endoderm development; IMP:MGI.
GO; GO:0042118; P:endothelial cell activation; IMP:BHF-UCL.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
GO; GO:0008585; P:female gonad development; IGI:MGI.
GO; GO:0061040; P:female gonad morphogenesis; IMP:MGI.
GO; GO:0048859; P:formation of anatomical boundary; IMP:MGI.
GO; GO:0007369; P:gastrulation; IMP:MGI.
GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0003220; P:left ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
GO; GO:0008584; P:male gonad development; IMP:MGI.
GO; GO:0007498; P:mesoderm development; IMP:MGI.
GO; GO:0072133; P:metanephric mesenchyme morphogenesis; IMP:UniProtKB.
GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
GO; GO:1905305; P:negative regulation of cardiac myofibril assembly; IMP:BHF-UCL.
GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0072134; P:nephrogenic mesenchyme morphogenesis; IMP:UniProtKB.
GO; GO:0014033; P:neural crest cell differentiation; IMP:MGI.
GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
GO; GO:0003148; P:outflow tract septum morphogenesis; IGI:BHF-UCL.
GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
GO; GO:0060021; P:palate development; IMP:BHF-UCL.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:MGI.
GO; GO:0003251; P:positive regulation of cell proliferation involved in heart valve morphogenesis; IMP:BHF-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0046881; P:positive regulation of follicle-stimulating hormone secretion; IMP:MGI.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:BHF-UCL.
GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IMP:BHF-UCL.
GO; GO:0033686; P:positive regulation of luteinizing hormone secretion; IMP:MGI.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0070207; P:protein homotrimerization; ISO:MGI.
GO; GO:0051098; P:regulation of binding; IDA:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0051797; P:regulation of hair follicle development; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO: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:0071559; P:response to transforming growth factor beta; ISO:MGI.
GO; GO:0048733; P:sebaceous gland development; IMP:MGI.
GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
GO; GO:0007338; P:single fertilization; IGI:MGI.
GO; GO:0007183; P:SMAD protein complex assembly; ISO:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI.
GO; GO:0032525; P:somite rostral/caudal axis specification; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0048729; P:tissue morphogenesis; IMP:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0060065; P:uterus development; IGI:MGI.
GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
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.
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;
3D-structure; Acetylation; Complete proteome; Cytoplasm; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 551 Mothers against decapentaplegic homolog
4.
/FTId=PRO_0000090862.
DOMAIN 18 142 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 322 551 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
REGION 274 319 SAD.
COMPBIAS 450 465 Poly-Ala.
METAL 71 71 Zinc. {ECO:0000250}.
METAL 115 115 Zinc. {ECO:0000250}.
METAL 127 127 Zinc. {ECO:0000250}.
METAL 132 132 Zinc. {ECO:0000250}.
SITE 514 514 Necessary for heterotrimerization.
{ECO:0000250}.
MOD_RES 37 37 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13485}.
MOD_RES 427 427 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13485}.
MOD_RES 506 506 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13485}.
CROSSLNK 113 113 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13485}.
CROSSLNK 518 518 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q13485}.
CONFLICT 257 257 A -> S (in Ref. 1; AAB57905).
{ECO:0000305}.
CONFLICT 292 292 P -> R (in Ref. 1; AAB57905).
{ECO:0000305}.
HELIX 16 24 {ECO:0000244|PDB:3QSV}.
HELIX 33 47 {ECO:0000244|PDB:3QSV}.
HELIX 51 62 {ECO:0000244|PDB:3QSV}.
TURN 63 65 {ECO:0000244|PDB:3QSV}.
STRAND 73 75 {ECO:0000244|PDB:3QSV}.
STRAND 82 84 {ECO:0000244|PDB:3QSV}.
STRAND 87 89 {ECO:0000244|PDB:3QSV}.
HELIX 91 99 {ECO:0000244|PDB:3QSV}.
STRAND 109 111 {ECO:0000244|PDB:3QSV}.
HELIX 119 121 {ECO:0000244|PDB:3QSV}.
STRAND 124 127 {ECO:0000244|PDB:3QSV}.
HELIX 130 132 {ECO:0000244|PDB:3QSV}.
STRAND 133 135 {ECO:0000244|PDB:3QSV}.
SEQUENCE 551 AA; 60342 MW; 4FBDF5DED4442F86 CRC64;
MDNMSITNTP TSNDACLSIV HSLMCHRQGG ESETFAKRAI ESLVKKLKEK KDELDSLITA
ITTNGAHPSK CVTIQRTLDG RLQVAGRKGF PHVIYARLWR WPDLHKNELK HVKYCQYAFD
LKCDSVCVNP YHYERVVSPG IDLSGLTLQS NAPSMLVKDE YVHDFEGQPS LPTEGHSIQT
IQHPPSNRAS TETYSAPALL APAESNATST TNFPNIPVAS TSQPASILAG SHSEGLLQIA
SGPQPGQQQN GFTAQPATYH HNSTTTWTGS RTAPYTPNLP HHQNGHLQHH PPMPPHPGHY
WPVHNELAFQ PPISNHPAPE YWCSIAYFEM DVQVGETFKV PSSCPVVTVD GYVDPSGGDR
FCLGQLSNVH RTEAIERARL HIGKGVQLEC KGEGDVWVRC LSDHAVFVQS YYLDREAGRA
PGDAVHKIYP SAYIKVFDLR QCHRQMQQQA ATAQAAAAAQ AAAVAGNIPG PGSVGGIAPA
ISLSAAAGIG VDDLRRLCIL RMSFVKGWGP DYPRQSIKET PCWIEIHLHR ALQLLDEVLH
TMPIADPQPL D


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