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Mothers against decapentaplegic homolog 4 (MAD homolog 4) (Mothers against DPP homolog 4) (SMAD family member 4) (SMAD 4) (Smad4)

 SMAD4_RAT               Reviewed;         552 AA.
O70437;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
10-OCT-2018, entry version 141.
RecName: Full=Mothers against decapentaplegic homolog 4;
Short=MAD homolog 4;
Short=Mothers against DPP homolog 4;
AltName: Full=SMAD family member 4;
Short=SMAD 4;
Short=Smad4;
Name=Smad4; Synonyms=Madh4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
Miyakita A., Okuno S., Watanabe T.K., Oga K., Tsuji A., Hishigaki H.,
Suto T., Nakagawa K., Nakahara Y., Higashi K.;
"Molecular cloning of rat Smad4 gene.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10670756; DOI=10.1507/endocrj.46.695;
Osaki M., Tsukazaki T., Ono N., Yonekura A., Hirota Y., Miyazaki Y.,
Shindo H., Sonta S., Yamashita S.;
"cDNA cloning and chromosomal mapping of rat Smad2 and Smad4 and their
expression in cultured rat articular chondrocytes.";
Endocr. J. 46:695-701(1999).
[3]
INTERACTION WITH CITED2.
PubMed=16619037; DOI=10.1038/sj.onc.1209552;
Chou Y.T., Wang H., Chen Y., Danielpour D., Yang Y.C.;
"Cited2 modulates TGF-beta-mediated upregulation of MMP9.";
Oncogene 25:5547-5560(2006).
-!- 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. Acts synergistically with SMAD1 and YY1 in bone
morphogenetic protein (BMP)-mediated cardiac-specific gene
expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-
3') within BMP response element (BMPRE) of cardiac activating
regions. 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. 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer. Heterotrimer; with a C-terminally phosphorylated
R-SMAD molecule and to form the transcriptionally active SMAD2/3-
SMAD4 complex. Found in a ternary complex composed of SMAD4,
STK11/LKB1 and STK11IP. Interacts with ATF2, COPS5, DACH1, MSG1,
SKI, STK11/LKB1, STK11IP and TRIM33. Found in a complex with SMAD1
and YY1. 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 PDPK1 (via PH domain).
Interacts with VPS39; this interaction affects heterodimer
formation with SMAD3, but not with SMAD2, and leads to inhibition
of SMAD3-dependent transcription activation. Interactions with
VPS39 and SMAD2 may be mutually exclusive (By similarity).
Interacts with CITED1 and CITED2. Interacts with ZC3H3 (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). Interacts weakly with ZNF8 (By similarity). 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). Interacts with ZBTB7A; the
interaction is direct and stimulated by TGFB1 (By similarity).
Interacts with CREBBP; the recruitment of this transcriptional
coactivator is negatively regulated by ZBTB7A (By similarity).
Interacts with EP300; the interaction with this transcriptional
coactivator is negatively regulated by ZBTB7A (By similarity).
Interacts with HDAC1 (By similarity).
{ECO:0000250|UniProtKB:P97471, ECO:0000250|UniProtKB:Q13485,
ECO:0000269|PubMed:16619037}.
-!- 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}.
-!- DOMAIN: The MH1 domain is required for 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}.
-!- PTM: Phosphorylated by PDPK1. {ECO:0000250}.
-!- PTM: Monoubiquitinated on Lys-519 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}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB010954; BAA83092.1; -; mRNA.
EMBL; AF056002; AAC12781.1; -; mRNA.
RefSeq; NP_062148.1; NM_019275.3.
UniGene; Rn.9774; -.
ProteinModelPortal; O70437; -.
SMR; O70437; -.
IntAct; O70437; 1.
MINT; O70437; -.
iPTMnet; O70437; -.
PhosphoSitePlus; O70437; -.
PRIDE; O70437; -.
GeneID; 50554; -.
KEGG; rno:50554; -.
CTD; 4089; -.
RGD; 3033; Smad4.
HOGENOM; HOG000286019; -.
HOVERGEN; HBG053353; -.
InParanoid; O70437; -.
KO; K04501; -.
PhylomeDB; O70437; -.
PRO; PR:O70437; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IDA:RGD.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
GO; GO:0031005; F:filamin binding; IPI:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046332; F:SMAD binding; IPI:RGD.
GO; GO:0030325; P:adrenal gland development; IEP:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IDA:RGD.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:RGD.
GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:BHF-UCL.
GO; GO:0001649; P:osteoblast differentiation; IMP:RGD.
GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:RGD.
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:0042060; P:wound healing; IMP:RGD.
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;
Acetylation; Complete proteome; Cytoplasm; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 552 Mothers against decapentaplegic homolog
4.
/FTId=PRO_0000090864.
DOMAIN 18 142 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 323 552 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
REGION 1 322 Mediates interaction with ZBTB7A.
{ECO:0000250|UniProtKB:Q13485}.
REGION 275 320 SAD.
COMPBIAS 451 466 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 515 515 Necessary for heterotrimerization.
{ECO:0000250}.
MOD_RES 37 37 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13485}.
MOD_RES 428 428 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13485}.
MOD_RES 507 507 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 519 519 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q13485}.
SEQUENCE 552 AA; 60469 MW; 7AE0540AB4DF0E77 CRC64;
MDNMSITNTP TSNDACLSIV HSLMCHRQGG ESETFAKRAI ESLVKKLKEK KDELDSLITA
ITTNGAHPSK CVTIQRTLDG RLQVAGRKGF PHVIYARLWR WPDLHKNELK HVKYCQYAFD
LKCDSVCVNP YHYERVVSPG IDLSGLTLQS NAPPSMLVKD EYVHDFEGQP SLPTEGHSIQ
TIQHPPSNRA STETYSAPAL LAPSESNATS TTNFPNIPVA STSQPASILA GSHSEGLLQI
ASGPQPGQQQ NGFTAQPATY HHNSTTTWTG SRTAPYTPNL PHHQNGHLQH HPPMPPHPGH
YWPVHNELAF QPPISNHPAP EYWCSIAYFE MDVQVGETFK VPSSCPIVTV DGYVDPSGGD
RFCLGQLSNV HRTEAIERAR LHIGKGVQLE CKGEGDVWVR CLSDHAVFVQ SYYLDREAGR
APGDAVHKIY PSAYIKVFDL RQCHRQMQQQ AATAQAAAAA QAAAVAGNIP GPGSVGGIAP
AISLSAAAGI GVDDLRRLCI LRMSFVKGWG PDYPRQSIKE TPCWIEIHLH RALQLLDEVL
HTMPIADPQP LD


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