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Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7)

 SMAD7_MOUSE             Reviewed;         426 AA.
O35253; O88709;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
23-MAY-2018, entry version 171.
RecName: Full=Mothers against decapentaplegic homolog 7;
Short=MAD homolog 7;
Short=Mothers against DPP homolog 7;
AltName: Full=Mothers against decapentaplegic homolog 8;
Short=MAD homolog 8;
Short=Mothers against DPP homolog 8;
AltName: Full=SMAD family member 7;
Short=SMAD 7;
Short=Smad7;
Name=Smad7; Synonyms=Madh7, Madh8;
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] (ISOFORM A).
TISSUE=Placenta;
PubMed=9335507; DOI=10.1038/39369;
Nakao A., Afrakhte M., Moren A., Nakayama T., Christian J.L.,
Heuchel R., Itoh S., Kawabata M., Heldin N.-E., Heldin C.-H.,
ten Dijke P.;
"Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta
signalling.";
Nature 389:631-635(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Embryo;
Kitamura K., Okazaki K.;
"Characterization of a novel mouse homologue of Mad, Smad7, that can
mediate TGF-beta family signalling.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
TISSUE=Embryo;
Kitamura K., Okazaki K.;
"Isolation of cDNAs encoding mouse homologues of Mad (Smad7 and
Smad7B) that can mediate TGF-beta family signalling.";
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
PubMed=10828018;
Kitamura K., Aota S., Sakamoto R., Yoshikawa S.I., Okazaki K.;
"Smad7 selectively interferes with different pathways of activin
signaling and inhibits erythroid leukemia cell differentiation.";
Blood 95:3371-3379(2000).
[5]
PHOSPHORYLATION AT SER-249, MUTAGENESIS OF SER-249, AND SUBCELLULAR
LOCATION.
PubMed=11278814; DOI=10.1074/jbc.M011019200;
Pulaski L., Landstrom M., Heldin C.-H., Souchelnytskyi S.;
"Phosphorylation of Smad7 at Ser-249 does not interfere with its
inhibitory role in transforming growth factor-beta-dependent signaling
but affects Smad7-dependent transcriptional activation.";
J. Biol. Chem. 276:14344-14349(2001).
[6]
INTERACTION WITH RNF111, AND UBIQUITINATION.
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).
[7]
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).
[8]
INTERACTION WITH NEDD4L, AND SUBCELLULAR LOCATION.
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).
[9]
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: Antagonist of signaling by TGF-beta (transforming growth
factor) type 1 receptor superfamily members; has been shown to
inhibit TGF-beta (Transforming growth factor) and activin
signaling by associating with their receptors thus preventing
SMAD2 access. Functions as an adapter to recruit SMURF2 to the
TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-
PP1 complex to TGFBR1, which promotes its dephosphorylation.
Positively regulates PDPK1 kinase activity by stimulating its
dissociation from the 14-3-3 protein YWHAQ which acts as a
negative regulator. {ECO:0000250|UniProtKB:O15105}.
-!- SUBUNIT: Interacts with COPS5. Interacts with STAMBP. Interacts
with PPP1R15A (By similarity). Interacts with NEDD4L. Interacts
with RNF111, AXIN1 and AXIN2. Interacts with ACVR1B, SMURF1,
SMURF2 and TGFBR1; SMAD7 recruits SMURF1 and SMURF2 to the TGF-
beta receptor and regulates its degradation (By similarity).
Interacts with WWP1. Interacts with PDPK1 (via PH domain) (By
similarity). Ubiquitinated by WWP1. {ECO:0000250,
ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:15221015,
ECO:0000269|PubMed:15496141}.
-!- INTERACTION:
O35625:Axin1; NbExp=2; IntAct=EBI-5274835, EBI-2365912;
Q923E4:Sirt1; NbExp=6; IntAct=EBI-5274835, EBI-1802585;
Q9C0C9:UBE2O (xeno); NbExp=2; IntAct=EBI-5274835, EBI-2339946;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11278814,
ECO:0000269|PubMed:15496141}. Cytoplasm
{ECO:0000269|PubMed:11278814, ECO:0000269|PubMed:15496141}.
Note=Interaction with NEDD4L or RNF111 induces translocation from
the nucleus to the cytoplasm (PubMed:15496141). TGF-beta
stimulates its translocation from the nucleus to the cytoplasm.
PDPK1 inhibits its translocation from the nucleus to the cytoplasm
in response to TGF-beta (By similarity).
{ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:15496141}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=O35253-1; Sequence=Displayed;
Name=B;
IsoId=O35253-2; Sequence=VSP_006181;
-!- TISSUE SPECIFICITY: Ubiquitous in various organs, with higher
levels in brain and kidney.
-!- PTM: Phosphorylation on Ser-249 does not affect its stability,
nuclear localization or inhibitory function in TGFB signaling;
however it affects its ability to regulate transcription
(PubMed:11278814). Phosphorylated by PDPK1 (By similarity).
{ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:11278814}.
-!- PTM: Ubiquitinated by WWP1 (PubMed:15221015). Polyubiquitinated by
RNF111, which is enhanced by AXIN1 and promotes proteasomal
degradation (PubMed:14657019). In response to TGF-beta,
ubiquitinated by SMURF1; which promotes its degradation (By
similarity). Ubiquitinated by RNF165, promoting proteasomal
degradation, leading to enhance the BMP-Smad signaling
(PubMed:23610558). {ECO:0000250|UniProtKB:O15105,
ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:15221015,
ECO:0000269|PubMed:23610558}.
-!- PTM: Acetylation prevents ubiquitination and degradation mediated
by SMURF1. {ECO:0000250|UniProtKB:O15105}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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EMBL; AF015260; AAB81353.1; -; mRNA.
EMBL; AJ000550; CAA04182.1; -; mRNA.
EMBL; AJ000551; CAA04183.1; -; mRNA.
CCDS; CCDS37860.1; -. [O35253-1]
RefSeq; NP_001036125.1; NM_001042660.1. [O35253-1]
RefSeq; XP_006525766.1; XM_006525703.2. [O35253-2]
UniGene; Mm.34407; -.
ProteinModelPortal; O35253; -.
SMR; O35253; -.
BioGrid; 201280; 26.
IntAct; O35253; 8.
MINT; O35253; -.
STRING; 10090.ENSMUSP00000026999; -.
iPTMnet; O35253; -.
PhosphoSitePlus; O35253; -.
PaxDb; O35253; -.
PRIDE; O35253; -.
Ensembl; ENSMUST00000026999; ENSMUSP00000026999; ENSMUSG00000025880. [O35253-1]
Ensembl; ENSMUST00000168918; ENSMUSP00000129322; ENSMUSG00000025880. [O35253-1]
GeneID; 17131; -.
KEGG; mmu:17131; -.
UCSC; uc008fqd.1; mouse. [O35253-1]
UCSC; uc008fqe.2; mouse. [O35253-2]
CTD; 4092; -.
MGI; MGI:1100518; Smad7.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOGENOM; HOG000060106; -.
HOVERGEN; HBG053021; -.
InParanoid; O35253; -.
KO; K19631; -.
OMA; GQLCSEN; -.
OrthoDB; EOG091G0XBN; -.
PhylomeDB; O35253; -.
TreeFam; TF314923; -.
Reactome; R-MMU-201451; Signaling by BMP.
Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
ChiTaRS; Smad7; mouse.
PRO; PR:O35253; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000025880; -.
CleanEx; MM_SMAD7; -.
ExpressionAtlas; O35253; baseline and differential.
Genevisible; O35253; MM.
GO; GO:0016342; C:catenin complex; IEA:Ensembl.
GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0048185; F:activin binding; ISO:MGI.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0005518; F:collagen binding; IPI:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; IEA:InterPro.
GO; GO:0070411; F:I-SMAD binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0030617; F:transforming growth factor beta receptor, inhibitory cytoplasmic mediator activity; 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:0034333; P:adherens junction assembly; ISO:MGI.
GO; GO:0048844; P:artery morphogenesis; IMP:BHF-UCL.
GO; GO:0034629; P:cellular protein-containing complex localization; ISO:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:BHF-UCL.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI.
GO; GO:0043433; P:negative regulation of DNA binding transcription factor activity; ISO:MGI.
GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:BHF-UCL.
GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
GO; GO:0002725; P:negative regulation of T cell cytokine production; IMP:BHF-UCL.
GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IMP:BHF-UCL.
GO; GO:2000317; P:negative regulation of T-helper 17 type immune response; IMP:BHF-UCL.
GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IMP:BHF-UCL.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:BHF-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0032925; P:regulation of activin receptor signaling pathway; ISO:MGI.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IC:BHF-UCL.
GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IC:BHF-UCL.
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; IDA:MGI.
GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
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-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; 2.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc.
CHAIN 1 426 Mothers against decapentaplegic homolog
7.
/FTId=PRO_0000090873.
DOMAIN 64 207 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 261 426 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
REGION 208 217 Important for interaction with SMURF2.
{ECO:0000250}.
MOTIF 208 211 PY-motif. {ECO:0000250}.
COMPBIAS 27 35 Poly-Gly.
COMPBIAS 49 56 Poly-Gly.
COMPBIAS 207 210 Poly-Pro.
METAL 125 125 Zinc. {ECO:0000250}.
METAL 180 180 Zinc. {ECO:0000250}.
METAL 192 192 Zinc. {ECO:0000250}.
METAL 197 197 Zinc. {ECO:0000250}.
MOD_RES 64 64 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O15105}.
MOD_RES 70 70 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O15105}.
MOD_RES 249 249 Phosphoserine. {ECO:0000255|PROSITE-
ProRule:PRU00439,
ECO:0000269|PubMed:11278814}.
CROSSLNK 64 64 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:O15105}.
CROSSLNK 70 70 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:O15105}.
VAR_SEQ 223 223 Missing (in isoform B).
{ECO:0000303|PubMed:10828018,
ECO:0000303|Ref.3}.
/FTId=VSP_006181.
MUTAGEN 249 249 S->A: No effect on stability, nuclear
localization or inhibitory function in
TGFB signaling. Abolishes transcriptional
activity. {ECO:0000269|PubMed:11278814}.
MUTAGEN 249 249 S->D: No effect.
{ECO:0000269|PubMed:11278814}.
CONFLICT 233 233 A -> V (in Ref. 3 and 4). {ECO:0000305}.
SEQUENCE 426 AA; 46442 MW; BEEE751371C0E0CF CRC64;
MFRTKRSALV RRLWRSRAPG GEDEEEGVGG GGGGGELRGE GATDGRAYGA GGGGAGRAGC
CLGKAVRGAK GHHHPHPPTS GAGAAGGAEA DLKALTHSVL KKLKERQLEL LLQAVESRGG
TRTACLLLPG RLDCRLGPGA PASAQPAQPP SSYSLPLLLC KVFRWPDLRH SSEVKRLCCC
ESYGKINPEL VCCNPHHLSR LCELESPPPP YSRYPMDFLK PTAGCPDAVP SSAETGGTNY
LAPGGLSDSQ LLLEPGDRSH WCVVAYWEEK TRVGRLYCVQ EPSLDIFYDL PQGNGFCLGQ
LNSDNKSQLV QKVRSKIGCG IQLTREVDGV WVYNRSSYPI FIKSATLDNP DSRTLLVHKV
FPGFSIKAFD YEKAYSLQRP NDHEFMQQPW TGFTVQISFV KGWGQCYTRQ FISSCPCWLE
VIFNSR


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