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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   10-MAY-2017, entry version 109.
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   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   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       {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|UniProtKB:P84022}.
CC       Nucleus {ECO:0000250|UniProtKB:P84022}. Note=In the cytoplasm in
CC       the absence of ligand. Migration to the nucleus when complexed
CC       with SMAD4. {ECO:0000250|UniProtKB:P84022}.
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}.
DR   EMBL; AY391265; AAQ89726.1; -; mRNA.
DR   RefSeq; NP_989806.1; NM_204475.1.
DR   UniGene; Gga.28197; -.
DR   ProteinModelPortal; P84023; -.
DR   SMR; P84023; -.
DR   BioGrid; 675429; 2.
DR   STRING; 9031.ENSGALP00000012766; -.
DR   PaxDb; P84023; -.
DR   GeneID; 395132; -.
DR   KEGG; gga:395132; -.
DR   CTD; 4088; -.
DR   eggNOG; KOG3701; Eukaryota.
DR   eggNOG; ENOG410XQKU; LUCA.
DR   HOGENOM; HOG000286018; -.
DR   HOVERGEN; HBG053353; -.
DR   InParanoid; P84023; -.
DR   KO; K04500; -.
DR   OMA; AVELCEY; -.
DR   OrthoDB; EOG091G082C; -.
DR   PhylomeDB; P84023; -.
DR   TreeFam; TF314923; -.
DR   PRO; PR:P84023; -.
DR   Proteomes; UP000000539; Unplaced.
DR   Bgee; ENSGALG00000007870; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:AgBase.
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:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
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   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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