ID A0A3B4A9D3_9GOBI Unreviewed; 384 AA.
AC A0A3B4A9D3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000013330.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000013330.1}
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; A0A3B4A9D3; -.
DR Ensembl; ENSPMGT00000014225.1; ENSPMGP00000013330.1; ENSPMGG00000009832.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd10492; MH1_SMAD_4; 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:SF34; MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG; 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 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 9..134
FT /note="MH1"
FT /evidence="ECO:0000259|PROSITE:PS51075"
FT DOMAIN 194..384
FT /note="MH2"
FT /evidence="ECO:0000259|PROSITE:PS51076"
FT REGION 144..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 42957 MW; 87170A6082A9C2A0 CRC64;
CVPCPHCPGL VQYILLRLCQ PGESEGFARR AIESLVRKLR ERREELDALV TAVTTRGRQP
GLCVTIQRTL DGRLQVAGRK GFPHVIYARL WRWPDLHKNE LKHATFCRFA FDLKYDSVCV
NPYHYDRVPA PTGVGCSPGV EVQGLIHMSP GQSPPPPHAP SPDYSSPGPE TGPETGSETG
PHTGQQANTG LDFWCSISYL EQDVRVGEVF KAPAGFPIIT VDGYMDPSGG DRFCLGRLSN
VQRTEASHRA RLHIGRGLQL EHRGDGDVWM RCLSDHALFV QSFYLDRESG RTPGGAVHKI
YPGAYIKVWN LGRASPVSNQ RRPHVDALRG LCVFRVSLVK GWGQQYPRRC IQDTPCWLEV
HLHRALQLLD QVLHALSPRQ HHDL
//
