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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