ID   SMAD1_DANRE             Reviewed;         472 AA.
AC   Q9I8V2; Q9PUQ3;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Mothers against decapentaplegic homolog 1;
DE            Short=MAD homolog 1;
DE            Short=Mothers against DPP homolog 1;
DE   AltName: Full=SMAD family member 1;
DE            Short=SMAD 1;
DE            Short=Smad1;
GN   Name=smad1; Synonyms=madh1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=AB; TISSUE=Embryo;
RX   PubMed=10590480;
RX   DOI=10.1002/(sici)1097-0177(199911)216:3<285::aid-dvdy7>3.0.co;2-l;
RA   Dick A., Meier A., Hammerschmidt M.;
RT   "Smad1 and smad5 have distinct roles during dorsoventral patterning of the
RT   zebrafish embryo.";
RL   Dev. Dyn. 216:285-298(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=10525190; DOI=10.1016/s0925-4773(99)00173-2;
RA   Mueller F., Blader P., Rastegar S., Fischer N., Knoechel W., Straehle U.;
RT   "Characterization of zebrafish smad1, smad2 and smad5: the amino-terminus
RT   of Smad1 and Smad5 is required for specific function in the embryo.";
RL   Mech. Dev. 88:73-88(1999).
CC   -!- FUNCTION: Involved in ventralization. May mediate Bmp2b signaling
CC       during embryonic dorsal-ventral pattern formation, and may itself be a
CC       transcriptional target for Smad5-mediated Bmp2b signaling.
CC       {ECO:0000269|PubMed:10525190, ECO:0000269|PubMed:10590480}.
CC   -!- SUBUNIT: May form trimers with another Smad1 and the co-Smad Smad4.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15797}. Nucleus
CC       {ECO:0000250|UniProtKB:Q15797}. Note=In the cytoplasm in the absence of
CC       ligand. Migration to the nucleus when complexed with Smad4.
CC       {ECO:0000250|UniProtKB:Q15797}.
CC   -!- DEVELOPMENTAL STAGE: Zygotically expressed. First detected 1 h after
CC       the midblastula transition. During gastrulation, expression is
CC       restricted to ventral regions. Later, expressed in the somites, eyes
CC       and a subset of dorsal cells in the hindbrain. Levels increase until
CC       the end of gastrulation and then remain high.
CC       {ECO:0000269|PubMed:10525190, ECO:0000269|PubMed:10590480}.
CC   -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR   EMBL; AF174434; AAF82402.1; -; mRNA.
DR   EMBL; AF167985; AAF06361.1; -; mRNA.
DR   RefSeq; NP_571431.1; NM_131356.1.
DR   AlphaFoldDB; Q9I8V2; -.
DR   SMR; Q9I8V2; -.
DR   STRING; 7955.ENSDARP00000109288; -.
DR   PaxDb; Q9I8V2; -.
DR   GeneID; 30628; -.
DR   KEGG; dre:30628; -.
DR   CTD; 4086; -.
DR   ZFIN; ZDB-GENE-991119-8; smad1.
DR   eggNOG; KOG3701; Eukaryota.
DR   InParanoid; Q9I8V2; -.
DR   OrthoDB; 608001at2759; -.
DR   Reactome; R-DRE-201451; Signaling by BMP.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   Reactome; R-DRE-8941326; RUNX2 regulates bone development.
DR   SignaLink; Q9I8V2; -.
DR   PRO; PR:Q9I8V2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; IGI:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:ZFIN.
DR   GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
DR   GO; GO:0061515; P:myeloid cell development; IMP:ZFIN.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:ZFIN.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.60.200.10; -; 1.
DR   Gene3D; 3.90.520.10; -; 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; PTHR13703; 1.
DR   Pfam; PF03165; MH1; 1.
DR   Pfam; PF03166; MH2; 1.
DR   SMART; SM00523; DWA; 1.
DR   SMART; SM00524; DWB; 1.
DR   SUPFAM; SSF49879; SSF49879; 1.
DR   SUPFAM; SSF56366; SSF56366; 1.
DR   PROSITE; PS51075; MH1; 1.
DR   PROSITE; PS51076; MH2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..472
FT                   /note="Mothers against decapentaplegic homolog 1"
FT                   /id="PRO_0000090851"
FT   DOMAIN          12..136
FT                   /note="MH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT   DOMAIN          278..472
FT                   /note="MH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT   REGION          158..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..238
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        82
FT                   /note="G -> V (in Ref. 2; AAF06361)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   472 AA;  53066 MW;  84E53B60ADB71BC9 CRC64;
     MNVTSLFSFT SPAVKRLLGW KQGDEEEKWA EKAVDALVKK LKKKKGAMEE LERALSCPGQ
     PSNCVTIPRS LDGRLQVSHR KGLPHVIYCR VWRWPDLQSH HELKALECCE FPFGSKQKDV
     CINPYHYKRV DSPVLPPVLV PRNSEFNAKL SMLPRFRNPL HQTEPPMPQN ATFPDSFPQQ
     PANALPFTPN SPTNSYPSSP NSGTGSTATF PHSPSSSDPG SPFQMPETPP PAYMPPEEPM
     TQDCPQPMDT NLLAPNLPLE ISNRTDVHPV AYQEPKHWCS IVYYELNNRV GEAFLASSTS
     VLVDGFTDPS NNRNRFCLGL LSNVNRNSTI ENTRRHIGKG VHLYYVGGEV YAECLSDSSI
     FVQSRNCNYH HGFHPTTVCK IPSRCSLKIF NNQEFAELLA QSVNHGFEAV YELTKMCTIR
     MSFVKGWGAK YHRQDVTSTP CWIEIHLHGP LQWLDKVLTQ MGSPHNPISS VS