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FOXH1_DANRE
ID   FOXH1_DANRE             Reviewed;         472 AA.
AC   Q9I9E1; Q9I8K6;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Forkhead box protein H1;
DE   AltName: Full=Forkhead activin signal transducer 1;
DE            Short=Fast-1;
DE   AltName: Full=Schmalspur protein;
GN   Name=foxh1; Synonyms=fast1, sur;
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, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, MUTAGENESIS OF ARG-94 AND LYS-97, AND DISRUPTION PHENOTYPE.
RX   PubMed=10996071; DOI=10.1016/s0960-9822(00)00669-2;
RA   Pogoda H.-M., Solnica-Krezel L., Driever W., Meyer D.;
RT   "The zebrafish forkhead transcription factor FoxH1/Fast1 is a modulator of
RT   nodal signaling required for organizer formation.";
RL   Curr. Biol. 10:1041-1049(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS
RP   OF ARG-94.
RC   TISSUE=Embryo;
RX   PubMed=10996072; DOI=10.1016/s0960-9822(00)00679-5;
RA   Sirotkin H.I., Gates M.A., Kelly P.D., Schier A.F., Talbot W.S.;
RT   "Fast1 is required for the development of dorsal axial structures in
RT   zebrafish.";
RL   Curr. Biol. 10:1051-1054(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=11091091; DOI=10.1016/s0925-4773(00)00485-8;
RA   Boggetti B., Argenton F., Haffter P., Bianchi M.E., Cotelli F.,
RA   Beltrame M.;
RT   "Cloning and expression pattern of a zebrafish homolog of forkhead activin
RT   signal transducer (FAST), a transcription factor mediating Nodal-related
RT   signals.";
RL   Mech. Dev. 99:187-190(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional activator. Activates an activin response
CC       element (ARE). Recognizes and binds to the DNA sequence 5'-
CC       TGT[GT][GT]ATT-3'. Modulator of nodal signaling required for organizer
CC       formation. Also required for the development of dorsal axial structures
CC       and left-right symmetry. {ECO:0000269|PubMed:10996071,
CC       ECO:0000269|PubMed:10996072}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089,
CC       ECO:0000269|PubMed:10996071}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Localized to the prospective animal pole during oogenesis. Ubiquitous
CC       expression during the blastula stages. During early gastrulation,
CC       levels are higher ventrally and in the presumptive shield (organizer
CC       region). Later in gastrulation, expression is restricted to midline and
CC       ventral cells. At the start of somatogenesis, expression is restricted
CC       to notochord, lateral plate mesoderm and a stripe of anterior dorsal
CC       neuroectoderm. By the 19-somite stage, expression in the lateral plate
CC       and midline diminishes but forebrain expression persists. All
CC       expression is lost by 24 hours post-fertilization (hpf).
CC       {ECO:0000269|PubMed:10996071, ECO:0000269|PubMed:10996072,
CC       ECO:0000269|PubMed:11091091}.
CC   -!- DOMAIN: The FM region is required for binding smad2/smad4 complexes.
CC       FM2 is more effective than FM1 and only interacts with phosphorylated
CC       smad2 that is in an activated smad complex (By similarity).
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Fishes exhibit ventral body curvature, reduced
CC       spacing of the eyes, and absence or reduction of ventral neuroectoderm,
CC       including the floor plate. {ECO:0000269|PubMed:10996071}.
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DR   EMBL; AF263000; AAF72712.1; -; mRNA.
DR   EMBL; AF264751; AAF81247.1; -; mRNA.
DR   EMBL; BC044340; AAH44340.1; -; mRNA.
DR   RefSeq; NP_571577.1; NM_131502.1.
DR   AlphaFoldDB; Q9I9E1; -.
DR   SMR; Q9I9E1; -.
DR   STRING; 7955.ENSDARP00000127073; -.
DR   PaxDb; Q9I9E1; -.
DR   GeneID; 57930; -.
DR   KEGG; dre:57930; -.
DR   CTD; 8928; -.
DR   ZFIN; ZDB-GENE-000616-15; foxh1.
DR   eggNOG; KOG2294; Eukaryota.
DR   InParanoid; Q9I9E1; -.
DR   OrthoDB; 1270467at2759; -.
DR   PhylomeDB; Q9I9E1; -.
DR   PRO; PR:Q9I9E1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0000785; C:chromatin; IDA:ZFIN.
DR   GO; GO:0005634; C:nucleus; IC:ZFIN.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:ZFIN.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ZFIN.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:ZFIN.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:ZFIN.
DR   GO; GO:0046332; F:SMAD binding; IMP:ZFIN.
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:0048319; P:axial mesoderm morphogenesis; IMP:ZFIN.
DR   GO; GO:0048327; P:axial mesodermal cell fate specification; IMP:ZFIN.
DR   GO; GO:0001568; P:blood vessel development; IMP:ZFIN.
DR   GO; GO:0048854; P:brain morphogenesis; IMP:ZFIN.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0042074; P:cell migration involved in gastrulation; IMP:ZFIN.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR   GO; GO:0060971; P:embryonic heart tube left/right pattern formation; IMP:ZFIN.
DR   GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:ZFIN.
DR   GO; GO:0001706; P:endoderm formation; IMP:ZFIN.
DR   GO; GO:0033504; P:floor plate development; IMP:ZFIN.
DR   GO; GO:0021508; P:floor plate formation; IMP:ZFIN.
DR   GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR   GO; GO:0021854; P:hypothalamus development; IMP:ZFIN.
DR   GO; GO:0046619; P:lens placode formation involved in camera-type eye formation; IMP:ZFIN.
DR   GO; GO:0048382; P:mesendoderm development; IGI:ZFIN.
DR   GO; GO:0001707; P:mesoderm formation; IMP:ZFIN.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ZFIN.
DR   GO; GO:0030903; P:notochord development; IMP:ZFIN.
DR   GO; GO:0014028; P:notochord formation; IMP:ZFIN.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0021501; P:prechordal plate formation; IMP:ZFIN.
DR   GO; GO:2000223; P:regulation of BMP signaling pathway involved in heart jogging; IMP:ZFIN.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:ZFIN.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:ZFIN.
DR   GO; GO:0032525; P:somite rostral/caudal axis specification; IMP:ZFIN.
DR   GO; GO:0010159; P:specification of animal organ position; IMP:ZFIN.
DR   GO; GO:0060063; P:Spemann organizer formation at the embryonic shield; IMP:ZFIN.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR030456; TF_fork_head_CS_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00250; Forkhead; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..472
FT                   /note="Forkhead box protein H1"
FT                   /id="PRO_0000091844"
FT   DNA_BIND        97..193
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          36..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..465
FT                   /note="SMAD-interaction domain (SID)"
FT   MOTIF           357..361
FT                   /note="Fast/FoxH1 motif 1 (FM1)"
FT   MOTIF           367..373
FT                   /note="Fast/FoxH1 motif 2 (FM2)"
FT   MOTIF           428..448
FT                   /note="SMAD interaction motif (SIM)"
FT   COMPBIAS        220..242
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         94
FT                   /note="R->H: In sur(m768); loss of function."
FT                   /evidence="ECO:0000269|PubMed:10996071,
FT                   ECO:0000269|PubMed:10996072"
FT   MUTAGEN         97
FT                   /note="K->N: In sur(ty68b); loss of function."
FT                   /evidence="ECO:0000269|PubMed:10996071"
FT   CONFLICT        233
FT                   /note="Q -> H (in Ref. 3; AAF81247)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        318
FT                   /note="G -> R (in Ref. 3; AAF81247)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="G -> S (in Ref. 3; AAF81247)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   472 AA;  51620 MW;  EC6285F1BFA970CA CRC64;
     MTKHWGGPGL LAPPVITVGE GAQRDHHLDC RIGYSSSKRS CHRSSNPLLE LGGRLDKSTG
     MAQDSCYRAK ATNQGPWELQ DGNSSGGKKK NYQRYPKPPY SYLAMIAMVI QNSPEKKLTL
     SEILKEISTL FPFFKGNYKG WRDSVRHNLS SYDCFVKVLK DPGKPQGKGN FWTVEVNRIP
     LELLKRQNTA VSRQDETIFA QDLAPYIFQG YSQPNKSKPL PPESSLPPVP TRQSPPPSED
     PYRPKLDSTF AIDSLLHSLR PASSAGEGLR ERESWGVGPP PHTRSTTPPR PCNASYNGSS
     SASSVSPASD FSDEDWRGVT VVGKRSGDRG ITSDAYSDSC PPPNKSSKRG NTPPWELPTS
     YAKYTPPNAV APPSMRFNGN PFMPLGGIPF YGYGGAHVTT SHLIGHPYWP ILPSGPVSIQ
     APPLLMDLDS MLQSVPPNKS VFDALGSNNQ TVHPSPNQYA LQNGPSLCKY SL
 
 
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