SMAD9_RAT
ID SMAD9_RAT Reviewed; 434 AA.
AC O54835;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=9371779; DOI=10.1073/pnas.94.24.12938;
RA Chen Y., Bhushan A., Vale W.W.;
RT "Smad8 mediates the signaling of the ALK-2 receptor serine kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12938-12943(1997).
CC -!- FUNCTION: Transcriptional modulator activated by BMP (bone
CC morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-
CC regulated SMAD (R-SMAD) (By similarity). Has been shown to be activated
CC by activin type I receptor-like kinase-2 (ALK-2) which stimulates
CC heteromerization between SMAD9 and SMAD4. ALK-2 binds TGF-beta, activin
CC and BMP. {ECO:0000250}.
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 {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=In the cytoplasm in the absence of ligand. Migration to the
CC nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type
CC 1 receptor kinase (By similarity). Phosphorylated by activin type I
CC receptor-like kinase-2 (ALK-2). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR EMBL; AF012347; AAC53515.1; -; mRNA.
DR RefSeq; NP_620227.1; NM_138872.1.
DR AlphaFoldDB; O54835; -.
DR SMR; O54835; -.
DR BioGRID; 250104; 1.
DR STRING; 10116.ENSRNOP00000000102; -.
DR iPTMnet; O54835; -.
DR PhosphoSitePlus; O54835; -.
DR jPOST; O54835; -.
DR PaxDb; O54835; -.
DR GeneID; 85435; -.
DR KEGG; rno:85435; -.
DR UCSC; RGD:71004; rat.
DR CTD; 4093; -.
DR RGD; 71004; Smad9.
DR eggNOG; KOG3701; Eukaryota.
DR InParanoid; O54835; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; O54835; -.
DR Reactome; R-RNO-201451; Signaling by BMP.
DR PRO; PR:O54835; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0030902; P:hindbrain development; ISO:RGD.
DR GO; GO:0030901; P:midbrain development; ISO:RGD.
DR GO; GO:0001880; P:Mullerian duct regression; IMP:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IDA:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001657; P:ureteric bud development; ISO:RGD.
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..434
FT /note="Mothers against decapentaplegic homolog 9"
FT /id="PRO_0000090877"
FT DOMAIN 16..140
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 236..434
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT REGION 171..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"
SQ SEQUENCE 434 AA; 48992 MW; DF6D7D31046D2575 CRC64;
MHPSTPISSL FSFTSPAVKR LLGWKQGDEE EKWAEKAVDS LVKKLKKKKG AMDELERALS
CPGQPSKCVT IPRSLDGRLQ VSHRKGLPHV IYCRVWRWPD LQSHHELKPL ECCEFPFGSK
QKEVCINPYH YRRVETPVLP PVLVPRHSEY NPQLSLLAKF RSASLHSEPL MPHNATYPDS
FQQSLGPAPP SSPGHVFPQS PCPTSYPQSP GSPSESDSPY QHSDFRPVCY EEPLHWCSVA
YYELNNRVGE TFQASSRSVL IDGFTDPSNN RNRFCLGLLS NVNRNSTIEN TRRHIGKGVH
LYYVGGEVYA ECVSDSSIFV QSRNCNYQHG FHPATVCKIP SGCSLKVFNN QLFAQLLAQL
LAQSVHHGFE VVYELTKMCT IRMSFVKGWG AEYHRQDVTS TPCWIEIHLH GPLQWLDKVL
TQMGSPHNPI SSVS
