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   24-JAN-2024, entry version 171.
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; 10090-ENSMUSP00000029371; -.
DR   ProteomicsDB; 261377; -.
DR   DNASU; 55994; -.
DR   Ensembl; ENSMUST00000029371.3; ENSMUSP00000029371.3; ENSMUSG00000027796.3.
DR   GeneID; 55994; -.
DR   KEGG; mmu:55994; -.
DR   UCSC; uc008pfv.2; mouse.
DR   AGR; MGI:1859993; -.
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; CSASYPH; -.
DR   OrthoDB; 2891561at2759; -.
DR   PhylomeDB; Q9JIW5; -.
DR   TreeFam; TF314923; -.
DR   Reactome; R-MMU-201451; Signaling by BMP.
DR   BioGRID-ORCS; 55994; 2 hits in 78 CRISPR screens.
DR   PRO; PR:Q9JIW5; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9JIW5; Protein.
DR   Bgee; ENSMUSG00000027796; Expressed in female urethra and 72 other cell types or tissues.
DR   ExpressionAtlas; Q9JIW5; baseline and differential.
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 DNA-templated transcription; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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   CDD; cd10490; MH1_SMAD_1_5_9; 1.
DR   Gene3D; 2.60.200.10; -; 1.
DR   Gene3D; 3.90.520.10; SMAD MH1 domain; 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:SF41; MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG 9; 1.
DR   PANTHER; PTHR13703; SMAD; 1.
DR   Pfam; PF03165; MH1; 1.
DR   Pfam; PF03166; MH2; 1.
DR   SMART; SM00523; DWA; 1.
DR   SMART; SM00524; DWB; 1.
DR   SUPFAM; SSF56366; SMAD MH1 domain; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS51075; MH1; 1.
DR   PROSITE; PS51076; MH2; 1.
DR   Genevisible; Q9JIW5; MM.
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
//