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Database: UniProt
Entry: P84023
LinkDB: P84023
Original site: P84023 
ID   SMAD3_CHICK             Reviewed;         426 AA.
AC   P84023;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   01-OCT-2014, entry version 86.
DE   RecName: Full=Mothers against decapentaplegic homolog 3;
DE            Short=MAD homolog 3;
DE            Short=Mad3;
DE            Short=Mothers against DPP homolog 3;
DE   AltName: Full=SMAD family member 3;
DE            Short=SMAD 3;
DE            Short=Smad3;
GN   Name=SMAD3; Synonyms=MADH3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RA   Liu Y., Zhao X., Zhang Y., Chen Y., Zhu D.;
RT   "Cloning and expression of chicken Smad3.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional modulator activated by TGF-beta
CC       (transforming growth factor) and activin type 1 receptor kinase.
CC       SMAD3 is a receptor-regulated SMAD (R-SMAD) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SARA (SMAD anchor for receptor
CC       activation); form trimers with another SMAD3 and the co-SMAD
CC       SMAD4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=In the cytoplasm in the absence of ligand.
CC       Migration to the nucleus when complexed with SMAD4 (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The MH2 domain is sufficient to carry protein nuclear
CC       export. {ECO:0000250}.
CC   -!- PTM: Phosphorylated on serine by TGF-beta and activin type 1
CC       receptor kinases. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 MH1 (MAD homology 1) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00438}.
CC   -!- SIMILARITY: Contains 1 MH2 (MAD homology 2) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00439}.
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DR   EMBL; AY391265; AAQ89726.1; -; mRNA.
DR   RefSeq; NP_989806.1; NM_204475.1.
DR   UniGene; Gga.28197; -.
DR   ProteinModelPortal; P84023; -.
DR   SMR; P84023; 7-132, 221-417.
DR   BioGrid; 675429; 2.
DR   STRING; 9031.ENSGALP00000012766; -.
DR   Ensembl; ENSGALT00000012780; ENSGALP00000012765; ENSGALG00000007870.
DR   GeneID; 395132; -.
DR   KEGG; gga:395132; -.
DR   CTD; 4088; -.
DR   eggNOG; NOG320700; -.
DR   GeneTree; ENSGT00600000084186; -.
DR   HOGENOM; HOG000286018; -.
DR   HOVERGEN; HBG053353; -.
DR   InParanoid; P84023; -.
DR   KO; K04500; -.
DR   OMA; NINAKCI; -.
DR   PhylomeDB; P84023; -.
DR   TreeFam; TF314923; -.
DR   Reactome; REACT_195006; SMAD2/3 Phosphorylation Motif Mutants in Cancer.
DR   Reactome; REACT_195008; TGF-beta receptor signaling activates SMADs.
DR   Reactome; REACT_197117; Signaling by Activin.
DR   Reactome; REACT_197118; Signaling by NODAL.
DR   Reactome; REACT_198067; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; REACT_211903; SMAD2/3 MH2 Domain Mutants in Cancer.
DR   Reactome; REACT_214793; Downregulation of TGF-beta receptor signaling.
DR   NextBio; 20815224; -.
DR   PRO; PR:P84023; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR   GO; GO:0071141; C:SMAD protein complex; ISS:UniProtKB.
DR   GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR   GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0000988; F:protein binding transcription factor activity; IEA:Ensembl.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0030618; F:transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:Ensembl.
DR   GO; GO:0045216; P:cell-cell junction organization; IEA:Ensembl.
DR   GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR   GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
DR   GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl.
DR   GO; GO:0007492; P:endoderm development; IEA:Ensembl.
DR   GO; GO:0019049; P:evasion or tolerance of host defenses by virus; IEA:Ensembl.
DR   GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; IEA:Ensembl.
DR   GO; GO:0002520; P:immune system development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
DR   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0033689; P:negative regulation of osteoblast proliferation; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0061045; P:negative regulation of wound healing; IEA:Ensembl.
DR   GO; GO:0038092; P:nodal signaling pathway; IEA:Ensembl.
DR   GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR   GO; GO:0048340; P:paraxial mesoderm morphogenesis; IEA:Ensembl.
DR   GO; GO:0060039; P:pericardium development; IEA:Ensembl.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0035413; P:positive regulation of catenin import into nucleus; IEA:Ensembl.
DR   GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:1901313; P:positive regulation of gene expression involved in extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0051098; P:regulation of binding; IEA:Ensembl.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0050776; P:regulation of immune response; IEA:Ensembl.
DR   GO; GO:0016202; P:regulation of striated muscle tissue development; IEA:Ensembl.
DR   GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0032909; P:regulation of transforming growth factor beta2 production; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   GO; GO:0042110; P:T cell activation; IEA:Ensembl.
DR   GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006810; P:transport; IEA:Ensembl.
DR   GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
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_dom-like.
DR   InterPro; IPR001132; SMAD_dom_Dwarfin-type.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   PANTHER; PTHR13703; PTHR13703; 1.
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   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN         1    426       Mothers against decapentaplegic homolog
FT                                3.
FT                                /FTId=PRO_0000090860.
FT   DOMAIN       10    136       MH1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00438}.
FT   DOMAIN      233    426       MH2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00439}.
FT   METAL        64     64       Zinc. {ECO:0000250}.
FT   METAL       109    109       Zinc. {ECO:0000250}.
FT   METAL       121    121       Zinc. {ECO:0000250}.
FT   METAL       126    126       Zinc. {ECO:0000250}.
FT   MOD_RES     424    424       Phosphoserine. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00439}.
FT   MOD_RES     426    426       Phosphoserine. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00439}.
SQ   SEQUENCE   426 AA;  48252 MW;  58DC1F9A664EAC7C CRC64;
     MSSILPFTPP IVKRLLGWKK GEQNGQEEKW CEKAVKSLVK KLKKTGQLDE LEKAITTQNI
     NTKCITIPRS LDGRLQVSHR KGLPHVIYCR LWRWPDLHSH HELRAMEMCE YAFNMKKDEV
     CVNPYHYQRV ETPVLPPVLV PRHTEIPAEF PPLDDYSHSI PENTNFPAGI EPQSNYIPET
     PPPGYLSEDG ETSDHQMNPS MDAGSPNLSP NPMSPAHNNL DLQPVTYCEP AFWCSISYYE
     LNQRVGETFH ASQPSMTVDG FTDPSNSERF CLGLLSNVNR NAAVELTRRH IGRGVRLYYI
     GGEVFAECLS DSAIFVQSPN CNQRYGWHPA TVCKIPPGCN LKIFNNQEFA ALLAQSVNQG
     FEAVYQLTRM CTIRMSFVKG WGAEYRRQTV TSTPCWIELH LNGPLQWLDK VLTQMGSPSI
     RCSSVS
//
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