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SMAD2_DANRE
ID   SMAD2_DANRE             Reviewed;         468 AA.
AC   Q9I9P9; Q4V964; Q9PUN4;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Mothers against decapentaplegic homolog 2;
DE            Short=MAD homolog 2;
DE            Short=Mothers against DPP homolog 2;
DE   AltName: Full=SMAD family member 2;
DE            Short=SMAD 2;
DE            Short=Smad2;
GN   Name=smad2; Synonyms=madh2;
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   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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Kidney;
RX   PubMed=10767528; DOI=10.1016/s0378-1119(00)00056-1;
RA   Dick A., Mayr T., Bauer H., Meier A., Hammerschmidt M.;
RT   "Cloning and characterization of zebrafish smad2, smad3 and smad4.";
RL   Gene 246:69-80(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes differentiation of dorsal tissues. May be involved
CC       in the mediation of Ndr2 signaling during mesoderm and axis formation
CC       during embryogenesis. {ECO:0000269|PubMed:10525190,
CC       ECO:0000269|PubMed:10767528}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15796}. Nucleus
CC       {ECO:0000250|UniProtKB:Q15796}. Note=In the cytoplasm in the absence of
CC       ligand. Migration to the nucleus when complexed with Smad4.
CC       {ECO:0000250|UniProtKB:Q15796}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed ubiquitously in the cleavage, blastula, gastrula and early
CC       somitogenesis stages. Expression declines during gastrulation. At 26
CC       hours, expressed weakly throughout the head, and more strongly in the
CC       mesenchymal neural crest cells behind the eyes and in the endoderm and
CC       haemangiogenic region of the tail. {ECO:0000269|PubMed:10525190,
CC       ECO:0000269|PubMed:10767528}.
CC   -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR   EMBL; AF168774; AAF06737.1; -; mRNA.
DR   EMBL; AF229022; AAF66239.1; -; mRNA.
DR   EMBL; BC097043; AAH97043.1; -; mRNA.
DR   RefSeq; NP_001276944.1; NM_001290015.1.
DR   RefSeq; NP_571441.3; NM_131366.3.
DR   AlphaFoldDB; Q9I9P9; -.
DR   SMR; Q9I9P9; -.
DR   DIP; DIP-41211N; -.
DR   IntAct; Q9I9P9; 1.
DR   STRING; 7955.ENSDARP00000111803; -.
DR   iPTMnet; Q9I9P9; -.
DR   PaxDb; Q9I9P9; -.
DR   ABCD; Q9I9P9; 1 sequenced antibody.
DR   Ensembl; ENSDART00000044756; ENSDARP00000044755; ENSDARG00000006389.
DR   Ensembl; ENSDART00000128579; ENSDARP00000111803; ENSDARG00000006389.
DR   Ensembl; ENSDART00000184617; ENSDARP00000145128; ENSDARG00000006389.
DR   GeneID; 30639; -.
DR   KEGG; dre:30639; -.
DR   CTD; 4087; -.
DR   ZFIN; ZDB-GENE-990603-7; smad2.
DR   eggNOG; KOG3701; Eukaryota.
DR   GeneTree; ENSGT00940000153499; -.
DR   InParanoid; Q9I9P9; -.
DR   OrthoDB; 608001at2759; -.
DR   PhylomeDB; Q9I9P9; -.
DR   Reactome; R-DRE-1181150; Signaling by NODAL.
DR   Reactome; R-DRE-1502540; Signaling by Activin.
DR   Reactome; R-DRE-2173788; Downregulation of TGF-beta receptor signaling.
DR   Reactome; R-DRE-2173789; TGF-beta receptor signaling activates SMADs.
DR   Reactome; R-DRE-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-DRE-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   Reactome; R-DRE-9617828; FOXO-mediated transcription of cell cycle genes.
DR   SignaLink; Q9I9P9; -.
DR   PRO; PR:Q9I9P9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 10.
DR   Bgee; ENSDARG00000006389; Expressed in cleaving embryo and 33 other tissues.
DR   ExpressionAtlas; Q9I9P9; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IDA:ZFIN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:ZFIN.
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; IDA:ZFIN.
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; IDA:ZFIN.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:ZFIN.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IGI:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:ZFIN.
DR   GO; GO:0021999; P:neural plate anterior/posterior regionalization; IGI:ZFIN.
DR   GO; GO:0038092; P:nodal signaling pathway; IDA:ZFIN.
DR   GO; GO:0060282; P:positive regulation of oocyte development; IMP:ZFIN.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:ZFIN.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IPI:ZFIN.
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..468
FT                   /note="Mothers against decapentaplegic homolog 2"
FT                   /id="PRO_0000090855"
FT   DOMAIN          10..177
FT                   /note="MH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT   DOMAIN          275..468
FT                   /note="MH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT   REGION          224..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        315
FT                   /note="G -> C (in Ref. 1; AAF06737)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   468 AA;  52453 MW;  464F4EFDF01D3270 CRC64;
     MSSILPFTPP VVKRLLGWKK SASGSSGAGG GGEQNGQEEK WCEKAVKSLV KKLKKTGQLD
     ELEKAITTQN RNTKCVTIPS NCSEIWGLST PNTIEQWDTS GLYSYPDQTR SLDGRLQVSH
     RKGLPHVIYC RLWRWPDLHS HHELRAIETC EYAFNLKKDE VCVNPYHYQR VETPVLPPVL
     VPRHTEILTE LPPLDDYTNS IPENTNFPTG IEPPNNYIPE TPPPGYISED GEASDQQMNQ
     SMDTGSPAEL SPSTLSPVNH GMDLQPVTYS EPAFWCSIAY YELNQRVGET FHASQPSLTV
     DGFTDPSNSE RFCLGLLSNV NRNATVEMTR RHIGRGVRLY YIGGEVFAEC LSDSAIFVQS
     PNCNQRYGWH PATVCKIPPG CNLKIFNNQE FAALLAQSVN QGFEAVYQLT RMCTIRMSFV
     KGWGAEYRRQ TVTSTPCWIE LHLNGPLQWL DKVLTQMGSP SVRCSSMS
 
 
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