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FOXJ1_MOUSE
ID   FOXJ1_MOUSE             Reviewed;         421 AA.
AC   Q61660; Q3US42;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Forkhead box protein J1 {ECO:0000305};
DE   AltName: Full=Hepatocyte nuclear factor 3 forkhead homolog 4 {ECO:0000303|PubMed:7683413};
DE            Short=HFH-4 {ECO:0000303|PubMed:7683413};
GN   Name=Foxj1 {ECO:0000312|MGI:MGI:1347474};
GN   Synonyms=Hfh4 {ECO:0000303|PubMed:7683413};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX   PubMed=7683413; DOI=10.1073/pnas.90.9.3948;
RA   Clevidence D.E., Overdier D.G., Tao W., Qian X., Pani L., Lai E.,
RA   Costa R.H.;
RT   "Identification of nine tissue-specific transcription factors of the
RT   hepatocyte nuclear factor 3/forkhead DNA-binding-domain family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:3948-3952(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=9096351; DOI=10.1073/pnas.94.7.3094;
RA   Lim L., Zhou H., Costa R.H.;
RT   "The winged helix transcription factor HFH-4 is expressed during choroid
RT   plexus epithelial development in the mouse embryo.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3094-3099(1997).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9739041; DOI=10.1172/jci4786;
RA   Chen J., Knowles H.J., Hebert J.L., Hackett B.P.;
RT   "Mutation of the mouse hepatocyte nuclear factor/forkhead homologue 4 gene
RT   results in an absence of cilia and random left-right asymmetry.";
RL   J. Clin. Invest. 102:1077-1082(1998).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10873152; DOI=10.1165/ajrcmb.23.1.4070;
RA   Brody S.L., Yan X.H., Wuerffel M.K., Song S.K., Shapiro S.D.;
RT   "Ciliogenesis and left-right axis defects in forkhead factor HFH-4-null
RT   mice.";
RL   Am. J. Respir. Cell Mol. Biol. 23:45-51(2000).
RN   [8]
RP   FUNCTION.
RX   PubMed=14996907; DOI=10.1242/jcs.00978;
RA   Gomperts B.N., Gong-Cooper X., Hackett B.P.;
RT   "Foxj1 regulates basal body anchoring to the cytoskeleton of ciliated
RT   pulmonary epithelial cells.";
RL   J. Cell Sci. 117:1329-1337(2004).
RN   [9]
RP   FUNCTION.
RX   PubMed=22357932; DOI=10.1242/dev.072728;
RA   Alten L., Schuster-Gossler K., Beckers A., Groos S., Ulmer B.,
RA   Hegermann J., Ochs M., Gossler A.;
RT   "Differential regulation of node formation, nodal ciliogenesis and cilia
RT   positioning by Noto and Foxj1.";
RL   Development 139:1276-1284(2012).
RN   [10]
RP   FUNCTION.
RX   PubMed=27965440; DOI=10.1242/dev.139626;
RA   Weidemann M., Schuster-Gossler K., Stauber M., Wrede C., Hegermann J.,
RA   Ott T., Boldt K., Beyer T., Serth K., Kremmer E., Blum M., Ueffing M.,
RA   Gossler A.;
RT   "CFAP157 is a murine downstream effector of FOXJ1 that is specifically
RT   required for flagellum morphogenesis and sperm motility.";
RL   Development 143:4736-4748(2016).
RN   [11]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=27914912; DOI=10.1016/j.ydbio.2016.11.019;
RA   Stauber M., Weidemann M., Dittrich-Breiholz O., Lobschat K., Alten L.,
RA   Mai M., Beckers A., Kracht M., Gossler A.;
RT   "Identification of FOXJ1 effectors during ciliogenesis in the foetal
RT   respiratory epithelium and embryonic left-right organiser of the mouse.";
RL   Dev. Biol. 423:170-188(2017).
RN   [12]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=28666954; DOI=10.1016/j.ydbio.2017.06.027;
RA   Stauber M., Boldt K., Wrede C., Weidemann M., Kellner M.,
RA   Schuster-Gossler K., Kuehnel M.P., Hegermann J., Ueffing M., Gossler A.;
RT   "1700012B09Rik, a FOXJ1 effector gene active in ciliated tissues of the
RT   mouse but not essential for motile ciliogenesis.";
RL   Dev. Biol. 429:186-199(2017).
CC   -!- FUNCTION: Transcription factor specifically required for the formation
CC       of motile cilia (PubMed:9096351, PubMed:9739041, PubMed:10873152,
CC       PubMed:14996907, PubMed:22357932, PubMed:27965440). Acts by activating
CC       transcription of genes that mediate assembly of motile cilia, such as
CC       CFAP157 (PubMed:27965440). Binds the DNA consensus sequences 5'-
CC       HWDTGTTTGTTTA-3' or 5'-KTTTGTTGTTKTW-3' (where H is not G, W is A or T,
CC       D is not C, and K is G or T) (PubMed:9096351). Activates the
CC       transcription of a variety of ciliary proteins in the developing brain
CC       and lung (PubMed:28666954, PubMed:27914912).
CC       {ECO:0000269|PubMed:10873152, ECO:0000269|PubMed:14996907,
CC       ECO:0000269|PubMed:22357932, ECO:0000269|PubMed:27914912,
CC       ECO:0000269|PubMed:27965440, ECO:0000269|PubMed:28666954,
CC       ECO:0000269|PubMed:9096351, ECO:0000269|PubMed:9739041}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:9096351}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in tissues containing
CC       motile cilia. {ECO:0000269|PubMed:27914912,
CC       ECO:0000269|PubMed:28666954}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing fetal lung epithelium
CC       and developing brain (at protein level). {ECO:0000269|PubMed:27914912,
CC       ECO:0000269|PubMed:28666954}.
CC   -!- DISRUPTION PHENOTYPE: Mice lack motile respiratory tract cilia and
CC       exhibit randomization of the left-right body axis due to loss of motile
CC       cilia in the embryonic node (PubMed:9739041, PubMed:10873152). Motile
CC       type cilia with a '9 + 2' microtubule ultrastructure are absent in
CC       epithelial cells, including those in the airways (PubMed:10873152).
CC       {ECO:0000269|PubMed:10873152, ECO:0000269|PubMed:9739041}.
CC   -!- SIMILARITY: Belongs to the FOXJ1 family. {ECO:0000305}.
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DR   EMBL; L13204; AAA21689.1; -; mRNA.
DR   EMBL; AK140847; BAE24495.1; -; mRNA.
DR   EMBL; AL645861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466558; EDL34572.1; -; Genomic_DNA.
DR   CCDS; CCDS25665.1; -.
DR   PIR; I49734; I49734.
DR   RefSeq; NP_032266.3; NM_008240.3.
DR   RefSeq; XP_006532332.1; XM_006532269.2.
DR   AlphaFoldDB; Q61660; -.
DR   SMR; Q61660; -.
DR   BioGRID; 200289; 1.
DR   IntAct; Q61660; 1.
DR   STRING; 10090.ENSMUSP00000038351; -.
DR   iPTMnet; Q61660; -.
DR   PhosphoSitePlus; Q61660; -.
DR   MaxQB; Q61660; -.
DR   PaxDb; Q61660; -.
DR   PRIDE; Q61660; -.
DR   ProteomicsDB; 267497; -.
DR   Antibodypedia; 1443; 250 antibodies from 32 providers.
DR   DNASU; 15223; -.
DR   Ensembl; ENSMUST00000036215; ENSMUSP00000038351; ENSMUSG00000034227.
DR   GeneID; 15223; -.
DR   KEGG; mmu:15223; -.
DR   UCSC; uc007mkv.2; mouse.
DR   CTD; 2302; -.
DR   MGI; MGI:1347474; Foxj1.
DR   VEuPathDB; HostDB:ENSMUSG00000034227; -.
DR   eggNOG; KOG2294; Eukaryota.
DR   GeneTree; ENSGT00940000156895; -.
DR   HOGENOM; CLU_050055_0_0_1; -.
DR   InParanoid; Q61660; -.
DR   OMA; FKKRRMP; -.
DR   OrthoDB; 1270467at2759; -.
DR   PhylomeDB; Q61660; -.
DR   TreeFam; TF333250; -.
DR   BioGRID-ORCS; 15223; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Foxj1; mouse.
DR   PRO; PR:Q61660; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q61660; protein.
DR   Bgee; ENSMUSG00000034227; Expressed in choroid plexus of fourth ventricle and 102 other tissues.
DR   Genevisible; Q61660; MM.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
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; IDA:NTNU_SB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:BHF-UCL.
DR   GO; GO:0090630; P:activation of GTPase activity; IDA:BHF-UCL.
DR   GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; IEP:BHF-UCL.
DR   GO; GO:0002508; P:central tolerance induction; IMP:BHF-UCL.
DR   GO; GO:0032053; P:ciliary basal body organization; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0060429; P:epithelium development; IEP:BHF-UCL.
DR   GO; GO:0035089; P:establishment of apical/basal cell polarity; IMP:MGI.
DR   GO; GO:0072016; P:glomerular parietal epithelial cell development; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0006959; P:humoral immune response; IMP:BHF-UCL.
DR   GO; GO:0060972; P:left/right pattern formation; IMP:MGI.
DR   GO; GO:0050900; P:leukocyte migration; IMP:BHF-UCL.
DR   GO; GO:0060428; P:lung epithelium development; IEA:Ensembl.
DR   GO; GO:0035502; P:metanephric part of ureteric bud development; IEA:Ensembl.
DR   GO; GO:0044458; P:motile cilium assembly; IMP:UniProtKB.
DR   GO; GO:0050869; P:negative regulation of B cell activation; IMP:BHF-UCL.
DR   GO; GO:0002635; P:negative regulation of germinal center formation; IMP:BHF-UCL.
DR   GO; GO:0002924; P:negative regulation of humoral immune response mediated by circulating immunoglobulin; IMP:BHF-UCL.
DR   GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:BHF-UCL.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
DR   GO; GO:0033085; P:negative regulation of T cell differentiation in thymus; IMP:BHF-UCL.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0002897; P:positive regulation of central B cell tolerance induction; IMP:BHF-UCL.
DR   GO; GO:1901248; P:positive regulation of lung ciliated cell differentiation; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR   GO; GO:0030856; P:regulation of epithelial cell differentiation; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001766; Fork_head_dom.
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   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   1: Evidence at protein level;
KW   Activator; Cilium biogenesis/degradation; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..421
FT                   /note="Forkhead box protein J1"
FT                   /id="PRO_0000091851"
FT   DNA_BIND        120..210
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        275..276
FT                   /note="KQ -> NE (in Ref. 1; AAA21689)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        317
FT                   /note="A -> R (in Ref. 1; AAA21689)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  45474 MW;  B5EB01D747672DFA CRC64;
     MAESWLRLCG AGPGEEAGPE GGMEEPDALD DSLTSLQWLQ EFSILNAKAP TLPPGGTDPH
     GYHQVPGLVA PGSPLAADPA CLGQPHTPGK PTSSCTSRSA PPGLQAPPPD DVDYATNPHV
     KPPYSYATLI CMAMQASKAT KITLSAIYKW ITDNFCYFRH ADPTWQNSIR HNLSLNKCFI
     KVPREKDEPG KGGFWRIDPQ YAERLLSGAF KKRRLPPVHI HPAFARQASQ EPSAAPWGGP
     LTVNREAQQL LQEFEEATGE GGWGTGEGRL GHKRKQPLPK RVAKVLRPPS TLLLTQEEQG
     ELEPLKGNFD WEAIFEAGAL GEELSSLEGL ELSPPLSPSS HGDVDLTVHG RHINCPATWG
     PPAEQAADSL DFDETFLATS FLQHPWDESG SGCLPPEPIF EAGDATLAAD LQDWASVGAF
     L
 
 
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