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 03-APR-2013, entry version 76.
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 Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC Neognathae; Galliformes; Phasianidae; 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 -!- SUBUNIT: Interacts with SARA (SMAD anchor for receptor
CC activation); form trimers with another SMAD3 and the co-SMAD SMAD4
CC (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC similarity). Note=In the cytoplasm in the absence of ligand.
CC Migration to the nucleus when complexed with SMAD4 (By
CC similarity).
CC -!- DOMAIN: The MH2 domain is sufficient to carry protein nuclear
CC export (By similarity).
CC -!- PTM: Phosphorylated on serine by TGF-beta and activin type 1
CC receptor kinases (By similarity).
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family.
CC -!- SIMILARITY: Contains 1 MH1 (MAD homology 1) domain.
CC -!- SIMILARITY: Contains 1 MH2 (MAD homology 2) domain.
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DR EMBL; AY391265; AAQ89726.1; -; mRNA.
DR IPI; IPI00600835; -.
DR RefSeq; NP_989806.1; NM_204475.1.
DR UniGene; Gga.28197; -.
DR ProteinModelPortal; P84023; -.
DR SMR; P84023; 7-132, 221-417.
DR STRING; 9031.ENSGALP00000012766; -.
DR Ensembl; ENSGALT00000012781; ENSGALP00000012766; 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 OrthoDB; EOG48PMK5; -.
DR NextBio; 20815224; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0071141; C:SMAD protein complex; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB.
DR GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
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; SSF56366; MAD_MH1; 1.
DR SUPFAM; SSF49879; SMAD_FHA; 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.
FT DOMAIN 233 426 MH2.
FT METAL 64 64 Zinc (By similarity).
FT METAL 109 109 Zinc (By similarity).
FT METAL 121 121 Zinc (By similarity).
FT METAL 126 126 Zinc (By similarity).
FT MOD_RES 424 424 Phosphoserine (By similarity).
FT MOD_RES 426 426 Phosphoserine (By similarity).
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
//
