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FXC1B_DANRE
ID   FXC1B_DANRE             Reviewed;         433 AA.
AC   Q9DE24;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Forkhead box C1-B;
GN   Name=foxc1b; Synonyms=foxc1.2;
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 [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=11165495; DOI=10.1016/s0925-4773(00)00534-7;
RA   Topczewska J.M., Topczewski J., Solnica-Krezel L., Hogan B.L.;
RT   "Sequence and expression of zebrafish foxc1a and foxc1b, encoding conserved
RT   forkhead/winged helix transcription factors.";
RL   Mech. Dev. 100:343-347(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-binding transcriptional factor that plays a role in a
CC       broad range of cellular and developmental processes such as eye, bones,
CC       cardiovascular, kidney and skin development. Acts either as a
CC       transcriptional activator or repressor. Binds to the consensus binding
CC       site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes. Upon
CC       DNA-binding, promotes DNA bending. Required for cell viability and
CC       resistance to oxidative stress in the eye. Promotes cell growth
CC       inhibition by stopping the cell cycle in the G1 phase through TGFB1-
CC       mediated signals. Involved in epithelial-mesenchymal transition (EMT)
CC       induction by increasing cell proliferation, migration and invasion.
CC       Involved in chemokine-induced endothelial cell migration. Plays a role
CC       in epidermal keratinocyte terminal differentiation. Essential
CC       developmental transcriptional factor required for mesoderm-derived
CC       tissues formation, such as the somites, skin, bone and cartilage. Plays
CC       a role in the development and maintenance of mesenchymal niches for
CC       haematopoietic stem and progenitor cells (HSPC). Plays a role in
CC       corneal transparency by preventing both blood vessel and lymphatic
CC       vessel growth during embryonic development in a VEGF-dependent manner.
CC       {ECO:0000250|UniProtKB:Q12948, ECO:0000250|UniProtKB:Q61572}.
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61572}.
CC   -!- DEVELOPMENTAL STAGE: First detected at the shield stage of gastrulation
CC       in the involuting mesendoderm with levels being highest in the paraxial
CC       mesoderm and decline laterally to become undetectable in the ventral
CC       mesoderm. Expression spreads in the hypoblast towards the animal pole
CC       and converges dorsally. At the tail bud stage (9.5 hpf), transcripts
CC       are seen in adaxial cells flanking the future notochord and in the
CC       presomitic mesoderm (PSM). During early somitogenesis, expression also
CC       extends into the future head, in two stripes continuous with the
CC       adaxial cells. Expression continues under the hindbrain as far as the
CC       midbrain/hindbrain boundary, in the presomitic mesoderm (PSM), trunk
CC       adaxial cells and somites. Expression still found, in the early
CC       pharyngula stage. in the PSM and adaxial cells in the tail and, at 33
CC       to 70 hpf, strong expression in the pharyngeal arches and saggital
CC       sections. {ECO:0000269|PubMed:11165495}.
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DR   EMBL; AF219950; AAG44242.1; -; Genomic_DNA.
DR   EMBL; BX510653; CAI12069.1; -; Genomic_DNA.
DR   EMBL; BC046028; AAH46028.1; -; mRNA.
DR   RefSeq; NP_571804.1; NM_131729.2.
DR   AlphaFoldDB; Q9DE24; -.
DR   SMR; Q9DE24; -.
DR   STRING; 7955.ENSDARP00000072219; -.
DR   PaxDb; Q9DE24; -.
DR   Ensembl; ENSDART00000077753; ENSDARP00000072219; ENSDARG00000055398.
DR   GeneID; 79375; -.
DR   KEGG; dre:79375; -.
DR   CTD; 79375; -.
DR   ZFIN; ZDB-GENE-010302-2; foxc1b.
DR   eggNOG; KOG2294; Eukaryota.
DR   GeneTree; ENSGT00940000162303; -.
DR   HOGENOM; CLU_035722_3_1_1; -.
DR   InParanoid; Q9DE24; -.
DR   OMA; LAPWYLN; -.
DR   OrthoDB; 1270467at2759; -.
DR   PhylomeDB; Q9DE24; -.
DR   TreeFam; TF316127; -.
DR   PRO; PR:Q9DE24; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 20.
DR   Bgee; ENSDARG00000055398; Expressed in zone of skin and 39 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0001568; P:blood vessel development; IGI:ZFIN.
DR   GO; GO:0043010; P:camera-type eye development; IGI:ZFIN.
DR   GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0061300; P:cerebellum vasculature development; IGI:ZFIN.
DR   GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IGI:ZFIN.
DR   GO; GO:0001755; P:neural crest cell migration; IGI:ZFIN.
DR   GO; GO:2000583; P:regulation of platelet-derived growth factor receptor-alpha signaling pathway; IGI:ZFIN.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0043114; P:regulation of vascular permeability; IGI:ZFIN.
DR   GO; GO:0001944; P:vasculature development; IMP:ZFIN.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR033067; FoxC1.
DR   InterPro; IPR018122; TF_fork_head_CS_1.
DR   InterPro; IPR030456; TF_fork_head_CS_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11829:SF68; PTHR11829:SF68; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS00657; FORK_HEAD_1; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..433
FT                   /note="Forkhead box C1-B"
FT                   /id="PRO_0000419249"
FT   DNA_BIND        74..168
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          174..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..190
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  47918 MW;  8941A9DBB9B837B9 CRC64;
     MQARYPVSSQ SPLGVVPYIP GDQGFYRTAT GGGYTGMPAP MSMYSHATHE QYPGGMARAY
     GPYAPAQQPK DMVKPPYSYI ALITMAIQNS SDKKITLNGI YQFIMERFPF YRDNKQGWQN
     SIRHNLSLNE CFVKVPRDDK KPGKGSYWTL DPDSYNMFEN GSFLRRRRRF KKKDVLREKE
     DRDRQGKDNP GQACEQDAQQ PVKLRDIKTE NGACTPPHDS TPPLSTVPKT ESPDRSGGSA
     CSGSPQSQTP QQAFSMDTIM TGLRGSPQHA AELPASRAAL PGSVSLTYSP TPQPAHYSPP
     CGQPATYHCN MQATSLYTGD RGHGDDTLPE YTNTTNASSI SHPHQSSSQE SQHLQQNRLA
     PWYLNQSGEL GHLSASYPGQ QQNFHAVREM FETQRIALNS SPVTGSNSCQ MAFPSSQPLY
     RASGAFVYDC SKF
 
 
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