ID A0A3B3ZMI1_9GOBI Unreviewed; 428 AA.
AC A0A3B3ZMI1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSPMGP00000005760.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000005760.1}
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; A0A3B3ZMI1; -.
DR STRING; 409849.ENSPMGP00000005760; -.
DR Ensembl; ENSPMGT00000006120.1; ENSPMGP00000005760.1; ENSPMGG00000004841.1.
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; cd10490; MH1_SMAD_1_5_9; 1.
DR CDD; cd10497; MH2_SMAD_1_5_9; 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:SF61; PROTEIN MOTHERS AGAINST DPP; 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 13..137
FT /note="MH1"
FT /evidence="ECO:0000259|PROSITE:PS51075"
FT DOMAIN 234..428
FT /note="MH2"
FT /evidence="ECO:0000259|PROSITE:PS51076"
FT REGION 168..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 48054 MW; B4197C9F037F78A4 CRC64;
MTSMSSLFSF TSPAVKRLLG WKQGDEEEKW AEKAVDALVK KLKKKKGAME DLEKALSCPG
QPSKCVTIPR SLDGRLQVSH RKGLPHVIYC RVWRWPDLQS HHELKPLELC EFPFGSKQKE
VCINPYHYKR VESPVLPPVL VPRHSEFNPQ HSLLVQFRNL THNEPHMPLN ATFPESFQPP
HSAGSSNISP NSPYGPPSPA SSGTYPNSPA SSGPASPFQL PDVQPVEYEE PSHWCSIMYY
ELNNRVGEAY HASSTSVLVD GFTDPSNNKN RFCLGLLSNV NRNSTIENTR RHIGKGVHLY
YVGGEVYAEC LSDTSIFVQS RNCNYHHGFH PTTVCKIPSG CSLKIFNNQE FAQLLAQSVN
HGFEAVYELT KMCTIRMSFV KGWGAEYHRQ DVTSTPCWIE VHLHGPLQWL DKVLTQMGSP
LNPISSVS
//
