ID A0A3Q1EBC4_9TELE Unreviewed; 467 AA.
AC A0A3Q1EBC4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000000584.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000000584.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q1EBC4; -.
DR STRING; 80966.ENSAPOP00000000584; -.
DR Ensembl; ENSAPOT00000016614.1; ENSAPOP00000000584.1; ENSAPOG00000001781.1.
DR GeneTree; ENSGT00940000153499; -.
DR InParanoid; A0A3Q1EBC4; -.
DR OrthoDB; 2891561at2759; -.
DR Proteomes; UP000257200; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; cd10491; MH1_SMAD_2_3; 1.
DR CDD; cd10985; MH2_SMAD_2_3; 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:SF42; MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG 2; 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:UP000257200};
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 10..176
FT /note="MH1"
FT /evidence="ECO:0000259|PROSITE:PS51075"
FT DOMAIN 274..467
FT /note="MH2"
FT /evidence="ECO:0000259|PROSITE:PS51076"
FT REGION 18..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 52337 MW; 0B6FFD853B5D6B7F CRC64;
MSSILPFTPP VVKRLLGWKK STSGPGGAGG GEQNGQEEKW CEKAVKSLVK KLKKTGQLDE
LEKAITTQNC NTKCVTIPSN CSEIWGLSTP NTIEQWDTSG LYSYPDQTRS LDGRLQVSHR
KGLPHVIYCR LWRWPDLHSH HELRAIEACE YAFHLKKDEV CINPYHYQRV ETPVLPPVLV
PRHSEILPEL PPLDDYTHSI PENTNFPAGI EPPNNYIPET PPPGYISEDG EASDQQMNQS
MDTGSPAELS PSTLSPVNHS MDLQPVTYSE PAFWCSIAYY ELNQRVGETF HASQPSLTVD
GFTDPSNSER FCLGLLSNVN RNATVEMTRR HIGRGVRLYY IGGEVFAECL SDSAIFVQSP
NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF AALLAQSVNQ GFEAVYQLTR MCTIRMSFVK
GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD KVLTQMGSPS ARCSSMS
//
