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

 SMAD1_RAT               Reviewed;         468 AA.
P97588; O70520;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
12-SEP-2018, entry version 152.
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; Synonyms=Mad1, Madh1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8917532; DOI=10.1073/pnas.93.23.12992;
Chen Y., Lebrun J.-J., Vale W.W.;
"Regulation of transforming growth factor beta- and activin-induced
transcription by mammalian Mad proteins.";
Proc. Natl. Acad. Sci. U.S.A. 93:12992-12997(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Intestine;
PubMed=9989785;
DOI=10.1002/(SICI)1097-4652(199903)178:3<387::AID-JCP13>3.3.CO;2-#;
Yue J., Hartsough M.T., Frey R.S., Frielle T., Mulder K.M.;
"Cloning and expression of a rat Smad1: regulation by TGFbeta and
modulation by the Ras/MEK pathway.";
J. Cell. Physiol. 178:387-396(1999).
-!- FUNCTION: Transcriptional modulator activated by BMP (bone
morphogenetic proteins) type 1 receptor kinase. SMAD1 is a
receptor-regulated SMAD (R-SMAD). Has been shown to be also
activated by TGF-beta (transforming growth factor) type I receptor
kinase in rat intestinal epithelial cells (IEC 4-1).
SMAD1/OAZ1/PSMB4 complex mediates the degradation of the
CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4
and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-
specific gene expression (By similarity).
{ECO:0000250|UniProtKB:Q15797}.
-!- SUBUNIT: Found in a complex with SMAD4 and YY1. Upon C-terminus
phosphorylation: forms trimers with another SMAD1 and the co-SMAD
SMAD4. Interacts with PEBP2-alpha subunit, CREB-binding protein
(CBP), NANOG, p300, SMURF1, SMURF2, HOXC8, USP15 and HGS.
Associates with ZNF423 or ZNF521 in response to BMP2 leading to
activate transcription of BMP target genes. Interacts with SKOR1
and ZCCHC12. Interacts (via MH2 domain) with LEMD3. Binding to
LEMD3 results in at least a partial reduction of receptor-mediated
phosphorylation. Forms a ternary complex with PSMB4 and OAZ1
before PSMB4 is incorporated into the 20S proteasome. 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=In the cytoplasm in
the absence of ligand. Migration to the nucleus when complexed
with SMAD4. Colocalizes with LEMD3 at the nucleus inner membrane.
Exported from the nucleus to the cytoplasm when dephosphorylated
(By similarity). {ECO:0000250|UniProtKB:P70340,
ECO:0000250|UniProtKB:Q15797}.
-!- TISSUE SPECIFICITY: Ubiquitous; present in liver, lung, stomach
and spleen with lower level in heart, testes and skeletal muscle.
-!- 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; U66478; AAC52943.1; -; mRNA.
EMBL; AF067727; AAC19116.1; -; mRNA.
UniGene; Rn.10635; -.
ProteinModelPortal; P97588; -.
SMR; P97588; -.
STRING; 10116.ENSRNOP00000025079; -.
PaxDb; P97588; -.
PRIDE; P97588; -.
UCSC; RGD:3030; rat.
RGD; 3030; Smad1.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
HOGENOM; HOG000286018; -.
HOVERGEN; HBG053353; -.
InParanoid; P97588; -.
PhylomeDB; P97588; -.
TreeFam; TF314923; -.
PRO; PR:P97588; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030509; P:BMP signaling pathway; IMP:RGD.
GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
GO; GO:0001822; P:kidney development; IEP:RGD.
GO; GO:0000165; P:MAPK cascade; IMP:RGD.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IEP:RGD.
GO; GO:0045597; P:positive regulation of cell differentiation; IDA:RGD.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IEP:RGD.
GO; GO:0042493; P:response to drug; IDA:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:InterPro.
GO; GO:0042060; P:wound healing; IEP:RGD.
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; Complete proteome; Cytoplasm; DNA-binding; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 468 Mothers against decapentaplegic homolog
1.
/FTId=PRO_0000090849.
DOMAIN 12 136 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 274 468 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
REGION 421 431 L3 loop. {ECO:0000250|UniProtKB:Q15797}.
COMPBIAS 39 45 Poly-Lys.
COMPBIAS 198 201 Poly-Ser.
METAL 64 64 Zinc. {ECO:0000250}.
METAL 109 109 Zinc. {ECO:0000250}.
METAL 121 121 Zinc. {ECO:0000250}.
METAL 126 126 Zinc. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q15797}.
MOD_RES 325 325 Phosphothreonine; by MINK1, TNIK and
MAP4K4. {ECO:0000250|UniProtKB:Q15797}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000250|UniProtKB:Q15797,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000250|UniProtKB:Q15797,
ECO:0000255|PROSITE-ProRule:PRU00439}.
CONFLICT 185 187 AQY -> PQS (in Ref. 2; AAC19116).
{ECO:0000305}.
CONFLICT 289 289 R -> A (in Ref. 2; AAC19116).
{ECO:0000305}.
CONFLICT 406 406 E -> V (in Ref. 2; AAC19116).
{ECO:0000305}.
SEQUENCE 468 AA; 52713 MW; 66A1ED58A0CE3CD1 CRC64;
MNVTSLFSFT SPAVKRLLGW KQGDEEEKWA EKAVDALVKK LKKKKGAMEE LEKALSCPGQ
PSNCVTIPRS LDGRLQVSHR KGLPHVIYCR VWRWPDLQSH HELKPLECCE FPFGSKQKEV
CINPYHYKRV ESPVLPPVLV PRHSEYNPQH SLLAQFRNLG QNEPHMPLNA TFPDSFQQPH
SHPFAQYPNS SYPNSPGSSS STYPHSPTSS DPGSPFQMPA DTPPPAYLPP EDPMAQDGSQ
PMDTNMTNMT APTLPAEINR GDVQAVAYEE PKHWCSIVYY ELNNRVGERF HASSTSVLVD
GFTDPSNNKN RFCLGLLSNV NRNSTIENTR RHIGKGVHLY YVGGEVYAEC LSDSSIFVQS
RNCNYHHGFH PTTVCKIPSG CSLKIFNNQE FAQLLAQSVN HGFETEYELT KMCTIRMSFV
KGWGAEYHRQ DVTSTPCWIE IHLHGPLQWL DKVLTQMGSP HNPISSVS


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