SMAD3_CHICK
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-AUG-2022, entry version 135.
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; 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 (transforming
CC growth factor) and activin type 1 receptor kinase. SMAD3 is a receptor-
CC regulated SMAD (R-SMAD) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SARA (SMAD anchor for receptor activation);
CC form trimers with another SMAD3 and the co-SMAD SMAD4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P84022}. Nucleus
CC {ECO:0000250|UniProtKB:P84022}. Note=In the cytoplasm in the absence of
CC ligand. Migration to the nucleus when complexed with SMAD4.
CC {ECO:0000250|UniProtKB:P84022}.
CC -!- DOMAIN: The MH2 domain is sufficient to carry protein nuclear export.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine by TGF-beta and activin type 1 receptor
CC kinases. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR EMBL; AY391265; AAQ89726.1; -; mRNA.
DR RefSeq; NP_989806.1; NM_204475.1.
DR AlphaFoldDB; P84023; -.
DR SMR; P84023; -.
DR BioGRID; 675429; 2.
DR STRING; 9031.ENSGALP00000012765; -.
DR PaxDb; P84023; -.
DR Ensembl; ENSGALT00000074963; ENSGALP00000058076; ENSGALG00000035701.
DR GeneID; 395132; -.
DR KEGG; gga:395132; -.
DR CTD; 4088; -.
DR VEuPathDB; HostDB:geneid_395132; -.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000153499; -.
DR HOGENOM; CLU_026736_0_0_1; -.
DR InParanoid; P84023; -.
DR OMA; MKHRLGA; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; P84023; -.
DR TreeFam; TF314923; -.
DR Reactome; R-GGA-1502540; Signaling by Activin.
DR Reactome; R-GGA-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-GGA-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-GGA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-GGA-5689880; Ub-specific processing proteases.
DR PRO; PR:P84023; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000035701; Expressed in kidney and 12 other tissues.
DR ExpressionAtlas; P84023; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0071141; C:SMAD protein complex; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
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-like_dom_sf.
DR InterPro; IPR001132; SMAD_dom_Dwarfin-type.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036578; SMAD_MH1_sf.
DR PANTHER; PTHR13703; PTHR13703; 2.
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 Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..426
FT /note="Mothers against decapentaplegic homolog 3"
FT /id="PRO_0000090860"
FT DOMAIN 10..136
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 233..426
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT REGION 167..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|PROSITE-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
