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SMAD5_DANRE
ID   SMAD5_DANRE             Reviewed;         464 AA.
AC   Q9W7E7;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Mothers against decapentaplegic homolog 5;
DE            Short=MAD homolog 5;
DE            Short=Mothers against DPP homolog 5;
DE   AltName: Full=Protein somitabun;
DE   AltName: Full=SMAD family member 5;
DE            Short=SMAD 5;
DE            Short=Smad5;
GN   Name=smad5; Synonyms=madh5, sbn;
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], VARIANT ILE-429, FUNCTION, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Embryo;
RX   PubMed=10207140; DOI=10.1242/dev.126.10.2149;
RA   Hild M., Dick A., Rauch G.J., Meier A., Bouwmeester T., Haffter P.,
RA   Hammerschmidt M.;
RT   "The smad5 mutation somitabun blocks Bmp2b signaling during early
RT   dorsoventral patterning of the zebrafish embryo.";
RL   Development 126:2149-2159(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
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).
CC   -!- FUNCTION: Involved in ventralization. May mediate Bmp2b signaling
CC       during early phases of embryonic dorsal-ventral pattern formation.
CC       Required for initiation of Smad1 expression during gastrulation.
CC       {ECO:0000269|PubMed:10207140, ECO:0000269|PubMed:10590480}.
CC   -!- SUBUNIT: May form trimers with the co-SMAD SMAD4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=In the cytoplasm in the absence of ligand. Migration to the
CC       nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Uniform
CC       distribution at the cleavage, blastula, gastrula and early
CC       somitogenesis stages. Levels decline during the early gastrula stages.
CC       At 26 hours, still expressed in the head, forming gut and dorsal neural
CC       tube. {ECO:0000269|PubMed:10207140, ECO:0000269|PubMed:10525190}.
CC   -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR   EMBL; AF127920; AAD43904.1; -; mRNA.
DR   EMBL; AF168775; AAF06738.1; -; mRNA.
DR   EMBL; BC065644; AAH65644.1; -; mRNA.
DR   RefSeq; NP_001333238.1; NM_001346309.1.
DR   RefSeq; NP_571443.3; NM_131368.3.
DR   RefSeq; XP_005173221.1; XM_005173164.3.
DR   RefSeq; XP_009289292.1; XM_009291017.2.
DR   AlphaFoldDB; Q9W7E7; -.
DR   SMR; Q9W7E7; -.
DR   STRING; 7955.ENSDARP00000054174; -.
DR   PaxDb; Q9W7E7; -.
DR   Ensembl; ENSDART00000054175; ENSDARP00000054174; ENSDARG00000037238.
DR   Ensembl; ENSDART00000183347; ENSDARP00000155132; ENSDARG00000037238.
DR   Ensembl; ENSDART00000187280; ENSDARP00000153815; ENSDARG00000037238.
DR   Ensembl; ENSDART00000191084; ENSDARP00000149901; ENSDARG00000037238.
DR   Ensembl; ENSDART00000191143; ENSDARP00000154529; ENSDARG00000037238.
DR   GeneID; 30641; -.
DR   KEGG; dre:30641; -.
DR   CTD; 4090; -.
DR   ZFIN; ZDB-GENE-990603-9; smad5.
DR   eggNOG; KOG3701; Eukaryota.
DR   GeneTree; ENSGT00940000155437; -.
DR   HOGENOM; CLU_026736_0_2_1; -.
DR   InParanoid; Q9W7E7; -.
DR   OMA; PPEEQMG; -.
DR   OrthoDB; 608001at2759; -.
DR   PhylomeDB; Q9W7E7; -.
DR   TreeFam; TF314923; -.
DR   Reactome; R-DRE-201451; Signaling by BMP.
DR   SignaLink; Q9W7E7; -.
DR   PRO; PR:Q9W7E7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 14.
DR   Bgee; ENSDARG00000037238; Expressed in mature ovarian follicle and 31 other tissues.
DR   ExpressionAtlas; Q9W7E7; baseline and differential.
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:0000976; F:transcription cis-regulatory region binding; IDA:ZFIN.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IGI:ZFIN.
DR   GO; GO:0030509; P:BMP signaling pathway; IMP:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR   GO; GO:0048264; P:determination of ventral identity; IDA:ZFIN.
DR   GO; GO:0060030; P:dorsal convergence; IMP:ZFIN.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR   GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:ZFIN.
DR   GO; GO:0009880; P:embryonic pattern specification; IMP:UniProtKB.
DR   GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR   GO; GO:0001945; P:lymph vessel development; IMP:ZFIN.
DR   GO; GO:0043049; P:otic placode formation; IEP:ZFIN.
DR   GO; GO:0060037; P:pharyngeal system development; IMP:ZFIN.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:ZFIN.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IMP:ZFIN.
DR   GO; GO:0048922; P:posterior lateral line neuromast deposition; IMP:ZFIN.
DR   GO; GO:0048919; P:posterior lateral line neuromast development; IMP:ZFIN.
DR   GO; GO:2000223; P:regulation of BMP signaling pathway involved in heart jogging; IMP:ZFIN.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR   GO; GO:0060021; P:roof of mouth development; IMP: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..464
FT                   /note="Mothers against decapentaplegic homolog 5"
FT                   /id="PRO_0000090868"
FT   DOMAIN          13..137
FT                   /note="MH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT   DOMAIN          270..464
FT                   /note="MH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT   REGION          166..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   VARIANT         429
FT                   /note="T -> I (in allele DTC24; dorsalized embryos)"
FT                   /evidence="ECO:0000269|PubMed:10207140"
SQ   SEQUENCE   464 AA;  51861 MW;  5018387FBA4072DC CRC64;
     MTSMSSLFSF TSPAVKRLLG WKQGDEEEKW AEKAVDALVK KLKKKKGAME DLEKALSSPG
     QPSKCVTIPR SLDGRLQVSH RKGLPHVIYC RVWRWPDLQS HHELKPLEVC EYPFGSKQKE
     VCINPYHYKR VESPVLPPVL VPRHSEFNPQ HSLLVQFRNL SHNEPHMPLN ATFPESFQQH
     SGGSSFPISP NSPYPPSPAS SGTYPNSPAS SGPSSPFQLP ADTPPPAYMP PDEQMGQDGS
     QSMETGSSLA PQNMPRGDVQ PVEYQEPSHW CSIVYYELNN RVGEAYHASS TSVLVDGFTD
     PSNNKNRFCL GLLSNVNRNS TIENTRRHIG KGVHLYYVGG EVYAECLSDT SIFVQSRNCN
     YHHGFHPTTV CKIPSGCSLK IFNNQEFAQL LAQSVNHGFE AVYELTKMCT IRMSFVKGWG
     AEYHRQDVTS TPCWIEVHLH GPLQWLDKVL TQMGSPLNPI SSVS
 
 
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