ID A0A2K5MU97_CERAT Unreviewed; 483 AA.
AC A0A2K5MU97;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Mothers against decapentaplegic homolog {ECO:0000256|RuleBase:RU361195};
DE Short=MAD homolog {ECO:0000256|RuleBase:RU361195};
DE Short=Mothers against DPP homolog {ECO:0000256|RuleBase:RU361195};
DE AltName: Full=SMAD family member {ECO:0000256|RuleBase:RU361195};
GN Name=SMAD7 {ECO:0000313|Ensembl:ENSCATP00000028813.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000028813.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000028813.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361195}.
CC Nucleus {ECO:0000256|RuleBase:RU361195}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family.
CC {ECO:0000256|ARBA:ARBA00005545, ECO:0000256|RuleBase:RU361195}.
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DR AlphaFoldDB; A0A2K5MU97; -.
DR STRING; 9531.ENSCATP00000028813; -.
DR Ensembl; ENSCATT00000053068.1; ENSCATP00000028813.1; ENSCATG00000037681.1.
DR GeneTree; ENSGT00940000159872; -.
DR OMA; GGRGCCM; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000037681; Expressed in lung and 11 other cell types or tissues.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0070697; F:activin receptor binding; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0070411; F:I-SMAD binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IEA:Ensembl.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IEA:Ensembl.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0034333; P:adherens junction assembly; IEA:Ensembl.
DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0002725; P:negative regulation of T cell cytokine production; IEA:Ensembl.
DR GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IEA:Ensembl.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:1903043; P:positive regulation of chondrocyte hypertrophy; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0031503; P:protein-containing complex localization; IEA:Ensembl.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
DR CDD; cd10494; MH1_SMAD_7; 1.
DR CDD; cd10500; MH2_SMAD_7; 1.
DR Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; SMAD MH1 domain; 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:SF44; MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG 7; 1.
DR PANTHER; PTHR13703; SMAD; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF56366; SMAD MH1 domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU361195};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361195};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU361195};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU361195}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 121..264
FT /note="MH1"
FT /evidence="ECO:0000259|PROSITE:PS51075"
FT DOMAIN 318..483
FT /note="MH2"
FT /evidence="ECO:0000259|PROSITE:PS51076"
FT REGION 74..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 52817 MW; A93CDBE8D7B1E578 CRC64;
HATERPSGRR RSCPGPCCCC CRLRLLPQLG ARLLHGVRRS CSLLSRQTTF LLASSPRMFR
TKRSALVRRL WRSRAPGGED EEEGAGGGGA GGELRGEGAT DSRAHGAGGG GPGRAGCCLG
KAVRGAKGHH HPHPPAAGAG AAGGAETDLK ALTHSVLKKL KERQLELLLQ AVESRGGTRT
ACLLLPGRLD CRLGPGAPAS AQPAQPPSSY SLPLLLCKVF RWPDLRHSSE VKRLCCCESY
GKINPELVCC NPHHLSRLCE LESPPPPYSR YPMDFLKPTA DCPDAVPSSA ETGGTNYLAP
GGLSDSQLLL EPGDRSHWCV VAYWEEKTRV GRLYCVQEPS LDIFYDLPQG NGFCLGQLNS
DNKSQLVQKV RSKIGCGIQL TREVDGVWVY NRSSYPIFIK SATLDNPDSR TLLVHKVFPG
FSIKAFDYEK AYSLQRPNDH EFMQQPWTGF TVQISFVKGW GQCYTRQFIS SCPCWLEVIF
NSR
//
