Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (SMAD family member 1) (SMAD 1) (Smad1)

 SMAD1_BOVIN             Reviewed;         465 AA.
 Q1JQA2; Q06AL6;
 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
 13-JUN-2006, sequence version 1.
 02-DEC-2020, entry version 112.
 RecName: Full=Mothers against decapentaplegic homolog 1;
          Short=MAD homolog 1;
          Short=Mothers against DPP homolog 1;
 AltName: Full=SMAD family member 1;
          Short=SMAD 1;
          Short=Smad1;
 Name=SMAD1;
 Bos taurus (Bovine).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
 Bovinae; Bos.
 NCBI_TaxID=9913;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 Zhang X., Xu S.;
 "Cloning and bioinformatic analysis of cDNA encoding cattle Smad1 gene.";
 Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=Hereford; TISSUE=Ascending colon;
 NIH - Mammalian Gene Collection (MGC) project;
 Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
 -!- FUNCTION: Transcriptional modulator activated by BMP (bone
     morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-
     regulated SMAD (R-SMAD). May act synergistically with SMAD4 and YY1 in
     bone morphogenetic protein (BMP)-mediated cardiac-specific gene
     expression. {ECO:0000250|UniProtKB:Q15797}.
 -!- SUBUNIT: Interacts with HGS, NANOG and ZCCHC12. Upon C-terminus
     phosphorylation: forms trimers with another SMAD1 and the co-SMAD
     SMAD4. Interacts with PEBP2-alpha subunit, CREB-binding protein (CBP),
     p300, SMURF1, SMURF2, USP15 and HOXC8. Associates with ZNF423 or ZNF521
     in response to BMP2 leading to activate transcription of BMP target
     genes. Interacts with SKOR1. Interacts (via MH2 domain) with LEMD3.
     Binding to LEMD3 results in at least a partial reduction of receptor-
     mediated phosphorylation. Found in a complex with SMAD4 and YY1. Found
     in a macromolecular complex with FAM83G. Interacts (via MH2 domain)
     with FAM83G (via MH2 domain); in a SMAD4-independent manner. Interacts
     with ZC3H3. Interacts with TMEM119. Interacts (via MH1 and MH2 domains)
     with ZNF8 (By similarity). Interacts with RANBP3L; the interaction
     increases when SMAD1 is not phosphorylated and mediates SMAD1 nuclear
     export (By similarity). {ECO:0000250|UniProtKB:P70340,
     ECO:0000250|UniProtKB:Q15797}.
 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15797}. Nucleus
     {ECO:0000250|UniProtKB:Q15797}. Note=Cytoplasmic in the absence of
     ligand. Migrates to the nucleus when complexed with SMAD4. Colocalizes
     with LEMD3 at the nucleus inner membrane (By similarity). Forms a
     ternary complex with PSMB4 and OAZ1 before PSMB4 is incorporated into
     the 20S proteasome (By similarity). Exported from the nucleus to the
     cytoplasm when dephosphorylated (By similarity).
     {ECO:0000250|UniProtKB:P70340, ECO:0000250|UniProtKB:Q15797}.
 -!- DOMAIN: The MH2 domain mediates phosphorylation-dependent trimerization
     through L3 loop binding of phosphoserines in the adjacent subunit.
     {ECO:0000250|UniProtKB:Q15797}.
 -!- PTM: Phosphorylation of the C-terminal SVS motif by BMP type 1 receptor
     kinase activates SMAD1 by promoting dissociation from the receptor and
     trimerization with SMAD4 (By similarity). Dephosphorylation, probably
     by PPM1A, induces its export from the nucleus to the cytoplasm (By
     similarity). {ECO:0000250|UniProtKB:P70340,
     ECO:0000250|UniProtKB:Q15797}.
 -!- PTM: Ubiquitinated by SMAD-specific E3 ubiquitin ligase SMURF1, leading
     to its degradation. Monoubiquitinated, leading to prevent DNA-binding.
     Deubiquitination by USP15 alleviates inhibition and promotes activation
     of TGF-beta target genes (By similarity). {ECO:0000250}.
 -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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 EMBL; DQ922947; ABI96185.1; -; mRNA.
 EMBL; BC116117; AAI16118.1; -; mRNA.
 RefSeq; NP_001069691.2; NM_001076223.2.
 RefSeq; XP_005217566.1; XM_005217509.2.
 RefSeq; XP_005217568.1; XM_005217511.2.
 RefSeq; XP_010812017.1; XM_010813715.2.
 RefSeq; XP_010812018.1; XM_010813716.2.
 SMR; Q1JQA2; -.
 STRING; 9913.ENSBTAP00000003668; -.
 PaxDb; Q1JQA2; -.
 PRIDE; Q1JQA2; -.
 Ensembl; ENSBTAT00000003668; ENSBTAP00000003668; ENSBTAG00000002835.
 Ensembl; ENSBTAT00000067295; ENSBTAP00000067920; ENSBTAG00000002835.
 Ensembl; ENSBTAT00000067387; ENSBTAP00000074456; ENSBTAG00000002835.
 Ensembl; ENSBTAT00000072205; ENSBTAP00000057918; ENSBTAG00000002835.
 GeneID; 540488; -.
 KEGG; bta:540488; -.
 CTD; 4086; -.
 VGNC; VGNC:34974; SMAD1.
 eggNOG; KOG3701; Eukaryota.
 GeneTree; ENSGT00940000154391; -.
 HOGENOM; CLU_026736_0_2_1; -.
 InParanoid; Q1JQA2; -.
 OMA; EVFHCNS; -.
 OrthoDB; 608001at2759; -.
 TreeFam; TF314923; -.
 Reactome; R-BTA-201451; Signaling by BMP.
 Reactome; R-BTA-5689880; Ub-specific processing proteases.
 Proteomes; UP000009136; Chromosome 17.
 Bgee; ENSBTAG00000002835; Expressed in longissimus thoracis muscle and 19 other tissues.
 ExpressionAtlas; Q1JQA2; baseline.
 GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
 GO; GO:0005637; C:nuclear inner membrane; IEA:Ensembl.
 GO; GO:0070410; F:co-SMAD binding; IEA:Ensembl.
 GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IEA:Ensembl.
 GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
 GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
 GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0070878; F:primary miRNA binding; IEA:Ensembl.
 GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
 GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
 GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
 GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
 GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
 GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
 GO; GO:0060348; P:bone development; IEA:Ensembl.
 GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
 GO; GO:0051216; P:cartilage development; IEA:Ensembl.
 GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
 GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
 GO; GO:0007276; P:gamete generation; IEA:Ensembl.
 GO; GO:0030902; P:hindbrain development; IEA:Ensembl.
 GO; GO:0042592; P:homeostatic process; IEA:Ensembl.
 GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
 GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
 GO; GO:0001710; P:mesodermal cell fate commitment; IEA:Ensembl.
 GO; GO:0030901; P:midbrain development; IEA:Ensembl.
 GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
 GO; GO:0002051; P:osteoblast fate commitment; IEA:Ensembl.
 GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl.
 GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
 GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IEA:Ensembl.
 GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
 GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IEA:Ensembl.
 GO; GO:0007183; P:SMAD protein complex assembly; IEA:Ensembl.
 GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
 GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
 GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
 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.
 2: Evidence at transcript level;
 Acetylation; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
 Phosphoprotein; Reference proteome; Transcription;
 Transcription regulation; Ubl conjugation; Zinc.
 CHAIN           1..465
                 /note="Mothers against decapentaplegic homolog 1"
                 /id="PRO_0000260256"
 DOMAIN          12..136
                 /note="MH1"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
 DOMAIN          271..465
                 /note="MH2"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
 REGION          418..428
                 /note="L3 loop"
                 /evidence="ECO:0000250|UniProtKB:Q15797"
 COMPBIAS        39..45
                 /note="Poly-Lys"
 COMPBIAS        198..201
                 /note="Poly-Ser"
 METAL           64
                 /note="Zinc"
                 /evidence="ECO:0000250"
 METAL           109
                 /note="Zinc"
                 /evidence="ECO:0000250"
 METAL           121
                 /note="Zinc"
                 /evidence="ECO:0000250"
 METAL           126
                 /note="Zinc"
                 /evidence="ECO:0000250"
 MOD_RES         1
                 /note="N-acetylmethionine"
                 /evidence="ECO:0000250|UniProtKB:Q15797"
 MOD_RES         322
                 /note="Phosphothreonine; by MINK1, TNIK and MAP4K4"
                 /evidence="ECO:0000250|UniProtKB:Q15797"
 MOD_RES         463
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q15797,
                 ECO:0000255|PROSITE-ProRule:PRU00439"
 MOD_RES         465
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q15797,
                 ECO:0000255|PROSITE-ProRule:PRU00439"
 CONFLICT        62
                 /note="S -> G (in Ref. 1; ABI96185)"
                 /evidence="ECO:0000305"
 SEQUENCE   465 AA;  52250 MW;  7C2E679F72B15C4F CRC64;
 MNVTSLFSFT SPAVKRLLGW KQGDEEEKWA EKAVDALVKK LKKKKGAMEE LEKALSCPGQ
 PSNCVTIPRS LDGRLQVSHR KGLPHVIYCR VWRWPDLQSH HELKPLECCE FPFGSKQKEV
 CINPYHYKRV ESPVLPPVLV PRHSEYNPQH SLLAQFRNLG QNEPHMPLNA TFPDSFQQPN
 SHPFPHSPNS SYPNSPGSSS STYPHSPTSS DPGSPFQMPA DTPPPAYLPP EDPMTQDGSQ
 PMDTNMMAPS LPSEINRGDV QAVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT
 DPSNNKNRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD SSIFVQSRNC
 NYHHGFHPTT VCKIPSGCSL KIFNNQEFAQ LLAQSVNHGF ETVYELTKMC TIRMSFVKGW
 GAEYHRQDVT STPCWIEIHL HGPLQWLDKV LTQMGSPHNP ISSVS

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