SMAD9_MOUSE
ID SMAD9_MOUSE Reviewed; 430 AA.
AC Q9JIW5; Q8CFF9;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Mothers against decapentaplegic homolog 9;
DE Short=MAD homolog 9;
DE Short=Mothers against DPP homolog 9;
DE AltName: Full=SMAD family member 9;
DE Short=SMAD 9;
DE Short=Smad9;
DE AltName: Full=Smad8;
GN Name=Smad9; Synonyms=Madh8, Madh9, Smad8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND VARIANT 214-SER-GLU-215
RP DEL.
RC TISSUE=Embryo;
RX PubMed=10814522; DOI=10.1006/bbrc.2000.2704;
RA Kawai S., Faucheu C., Gallea S., Spinella-Jaegle S., Atfi A., Baron R.,
RA Roman-Roman S.;
RT "Mouse Smad8 phosphorylation downstream of BMP receptors ALK-2, ALK-3, and
RT ALK-6 induces its association with Smad4 and transcriptional activity.";
RL Biochem. Biophys. Res. Commun. 271:682-687(2000).
RN [2]
RP SEQUENCE REVISION TO 115 AND 135.
RA Kawai S., Roman-Roman S.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RA Kawai S., Roman-Roman S.;
RT "Mouse Smad8 protein mRNA alternative form (6-bp insert in linker
RT region).";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional modulator activated by BMP (bone
CC morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-
CC regulated SMAD (R-SMAD). Has been shown to be activated by activin type
CC I receptor-like kinases (ALK-2, ALK-3, ALK-6) which stimulate
CC heteromerization between SMAD9 and SMAD4. May play a role in osteoblast
CC differentiation and maturation.
CC -!- SUBUNIT: Interaction with the co-SMAD SMAD4. Interacts with PEBP2-alpha
CC subunit (By similarity). Interacts with RANBP3L (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:O15198}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in the
CC absence of ligand. Migrates to the nucleus when complexed with SMAD4.
CC -!- PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type
CC 1 receptor kinase and activin type I receptor-like kinases (ALK-2, ALK-
CC 3 and ALK-6).
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR EMBL; AF175408; AAF77079.2; -; mRNA.
DR EMBL; AY145520; AAN85445.1; -; mRNA.
DR CCDS; CCDS17354.1; -.
DR RefSeq; NP_062356.3; NM_019483.5.
DR RefSeq; XP_006501791.1; XM_006501728.3.
DR AlphaFoldDB; Q9JIW5; -.
DR SMR; Q9JIW5; -.
DR BioGRID; 207765; 9.
DR IntAct; Q9JIW5; 1.
DR MINT; Q9JIW5; -.
DR STRING; 10090.ENSMUSP00000029371; -.
DR ChEMBL; CHEMBL3883282; -.
DR iPTMnet; Q9JIW5; -.
DR PhosphoSitePlus; Q9JIW5; -.
DR MaxQB; Q9JIW5; -.
DR PaxDb; Q9JIW5; -.
DR PRIDE; Q9JIW5; -.
DR ProteomicsDB; 261377; -.
DR DNASU; 55994; -.
DR Ensembl; ENSMUST00000029371; ENSMUSP00000029371; ENSMUSG00000027796.
DR GeneID; 55994; -.
DR KEGG; mmu:55994; -.
DR UCSC; uc008pfv.2; mouse.
DR CTD; 4093; -.
DR MGI; MGI:1859993; Smad9.
DR VEuPathDB; HostDB:ENSMUSG00000027796; -.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000154391; -.
DR HOGENOM; CLU_026736_0_2_1; -.
DR InParanoid; Q9JIW5; -.
DR OMA; YHATETP; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; Q9JIW5; -.
DR TreeFam; TF314923; -.
DR Reactome; R-MMU-201451; Signaling by BMP.
DR BioGRID-ORCS; 55994; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9JIW5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JIW5; protein.
DR Bgee; ENSMUSG00000027796; Expressed in female urethra and 70 other tissues.
DR ExpressionAtlas; Q9JIW5; baseline and differential.
DR Genevisible; Q9JIW5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0060348; P:bone development; IGI:MGI.
DR GO; GO:0051216; P:cartilage development; IGI:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR GO; GO:0030901; P:midbrain development; IMP:MGI.
DR GO; GO:0001880; P:Mullerian duct regression; ISO:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; IGI:BHF-UCL.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
DR Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; -; 1.
DR InterPro; IPR013790; Dwarfin.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR InterPro; IPR013019; MAD_homology_MH1.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR001132; SMAD_dom_Dwarfin-type.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036578; SMAD_MH1_sf.
DR PANTHER; PTHR13703; PTHR13703; 2.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56366; SSF56366; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..430
FT /note="Mothers against decapentaplegic homolog 9"
FT /id="PRO_0000090876"
FT DOMAIN 16..140
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 236..430
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT REGION 186..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VARIANT 214..215
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:10814522"
SQ SEQUENCE 430 AA; 48636 MW; 3B15EC51D6A594E5 CRC64;
MHPSTPISSL FSFTSPAVKR LLGWKQGDEE EKWAEKAVDS LVKKLKKKKG AMDELERALS
CPGQPSKCVT IPRSLDGRLQ VSHRKGLPHV IYCRVWRWPD LQSHHELKPL ECCEFPFGSK
QKEVCINPYH YRRVETPVLP PVLVPRHSEY NPQLSLLAKF RSASLHSEPL MPHNATYPDS
FQQSLCPAPP SSPGHVFPQS PCPTSYPHSP GSPSESDSPY QHSDFRPVCY EEPQHWCSVA
YYELNNRVGE TFQASSRSVL IDGFTDPSNN RNRFCLGLLS NVNRNSTIEN TRRHIGKGVH
LYYVGGEVYA ECVSDSSIFV QSRNCNYQHG FHPATVCKIP SGCSLKVFNN QLFAQLLAQS
VHHGFEVVYE LTKMCTIRMS FVKGWGAEYH RQDVTSTPCW IEIHLHGPLQ WLDKVLTQMG
SPHNPISSVS
