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Database: UniProt
Entry: A0A3Q2VDQ2_HAPBU
LinkDB: A0A3Q2VDQ2_HAPBU
Original site: A0A3Q2VDQ2_HAPBU 
ID   A0A3Q2VDQ2_HAPBU        Unreviewed;       497 AA.
AC   A0A3Q2VDQ2;
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};
GN   Name=SMAD4 {ECO:0000313|Ensembl:ENSHBUP00000008954.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000008954.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000008954.1}
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; A0A3Q2VDQ2; -.
DR   Ensembl; ENSHBUT00000001074.1; ENSHBUP00000008954.1; ENSHBUG00000010531.1.
DR   GeneTree; ENSGT00940000157435; -.
DR   OMA; CWIEVQI; -.
DR   Proteomes; UP000264840; 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   CDD; cd10498; MH2_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:SF63; MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG 4; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|RuleBase:RU361195};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361195};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU361195};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU361195};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          15..139
FT                   /note="MH1"
FT                   /evidence="ECO:0000259|PROSITE:PS51075"
FT   DOMAIN          268..497
FT                   /note="MH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51076"
FT   REGION          166..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          34..61
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        166..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..206
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  54115 MW;  F922891CCBAF6776 CRC64;
     MSITNTPTSN DACLSIVHSL MCHRQGGESE TFAKRAIESL VKKLKEKKDE LDSLITAITT
     NGAHPSKCVT IQRTLDGRLQ VAGRKGFPHV IYARLWRWPD LHKNELKHVK YCQFAFDLKC
     DCVCVNPYHY ERVVSPGIDL SGLTINSSAG HSSSMIVKDE FDFDGQQSVS SIDGSHSLQT
     IQHPPTSSRP PPSESFPTPT LLPPPEPSTS ASTASFPAVA AGSGNPTSAW PRNGFTPTIP
     HHSNGHLQHH PPIPHPIFLP SVSAPDYWCS IAYFEMDVQV GETFKVPSSC PIVTVDGYVD
     PSGGDRFCLG QLSNVHRTEA IERARLHIGK GVQLECKGEG DVWVRCLSDH AVFVQSYYLD
     REAGRAPGDA VHKIYPSAYI KVFDLRQCHR QMQQQAATAQ AAAAAQAAAV AGNIPGPGSV
     GGIAPAISLS AAAGIGVDDL RRLCILRMSF VKGWGPDYPR QSIKETPCWI EIHLHRALQL
     LDEVLHTMPI ADPQPLD
//
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