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FJX1_MOUSE
ID   FJX1_MOUSE              Reviewed;         450 AA.
AC   Q8BQB4; Q9Z1M1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Four-jointed box protein 1;
DE            Short=Four-jointed protein x1;
DE   AltName: Full=Four-jointed protein homolog;
DE   Flags: Precursor;
GN   Name=Fjx1;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=129/SvJ;
RX   PubMed=10072791; DOI=10.1016/s0925-4773(98)00218-4;
RA   Ashery-Padan R., Alvarez-Bolado G., Klamt B., Gessler M., Gruss P.;
RT   "Fjx1, the murine homologue of the Drosophila four-jointed gene, codes for
RT   a putative secreted protein expressed in restricted domains of the
RT   developing and adult brain.";
RL   Mech. Dev. 80:213-217(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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 MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INDUCTION, PROTEOLYTIC CLEAVAGE, GLYCOSYLATION, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=16145673; DOI=10.1002/dvdy.20553;
RA   Rock R., Heinrich A.C., Schumacher N., Gessler M.;
RT   "Fjx1: a notch-inducible secreted ligand with specific binding sites in
RT   developing mouse embryos and adult brain.";
RL   Dev. Dyn. 234:602-612(2005).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16059920; DOI=10.1002/dvdy.20515;
RA   Rock R., Schrauth S., Gessler M.;
RT   "Expression of mouse dchs1, fjx1, and fat-j suggests conservation of the
RT   planar cell polarity pathway identified in Drosophila.";
RL   Dev. Dyn. 234:747-755(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=18028897; DOI=10.1016/j.ydbio.2007.09.054;
RA   Probst B., Rock R., Gessler M., Vortkamp A., Pueschel A.W.;
RT   "The rodent four-jointed ortholog Fjx1 regulates dendrite extension.";
RL   Dev. Biol. 312:461-470(2007).
CC   -!- FUNCTION: Acts as an inhibitor of dendrite extension and branching.
CC       {ECO:0000269|PubMed:18028897}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16145673}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, kidney and lung. In the
CC       telencephalon, expressed in the piriform cortex, hippocampus and
CC       olfactory bulb. In the diencephalon, expressed in the dorsal thalamus.
CC       Expressed in Purkinje cells of the cerebellum and in numerous medullary
CC       nuclei. {ECO:0000269|PubMed:10072791, ECO:0000269|PubMed:16059920,
CC       ECO:0000269|PubMed:16145673}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 8.5 dpc onward. In the
CC       neural plate, expressed in the presumptive forebrain and midbrain and
CC       in rhombomere at 4 and 8.5 dpc. Expressed in the limb buds and in the
CC       ectoderm of the first branchial arches at 9.5 dpc. In the brain,
CC       expressed in the dorsal mesencephalon (tectum) and prosencephalon
CC       (presumptive isocortex) at 9.5, 10.5 and 11.5 dpc. In the cortex,
CC       expressed in dorsolateral patch of the neuroepithelium at 10.5 dpc.
CC       Expressed in the ectoderm of the branchial arch and the oral ectoderm
CC       at 10.5 dpc. In the limbs, expressed in the apical ectodermal ridge at
CC       11.5 dpc. Expressed in the telecephalon, ventricles, diencephalon and
CC       medulla oblongata at 12.5 dpc. Expressed in the neural tube, cochlear
CC       ganglion and olfactory bulb at 14.5 dpc. In the kidney, lung and
CC       intestine, expressed in epithelial cells at 14.5 dpc.
CC       {ECO:0000269|PubMed:10072791, ECO:0000269|PubMed:16059920,
CC       ECO:0000269|PubMed:16145673}.
CC   -!- INDUCTION: Up-regulated by Notch. {ECO:0000269|PubMed:16145673}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:16145673}.
CC   -!- PTM: Undergoes proteolytic cleavage. {ECO:0000269|PubMed:16145673}.
CC   -!- MISCELLANEOUS: Knockout mice for this gene exhibited an increase in
CC       dendrite extension and branching of pyramidal neurons in the CA1 region
CC       of the hippocampus.
CC   -!- SIMILARITY: Belongs to the FJX1/FJ family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA08764.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ009634; CAA08764.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AK051097; BAC34524.1; -; mRNA.
DR   EMBL; AL691444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC051990; AAH51990.1; -; mRNA.
DR   CCDS; CCDS16467.1; -.
DR   RefSeq; NP_034348.2; NM_010218.2.
DR   AlphaFoldDB; Q8BQB4; -.
DR   SMR; Q8BQB4; -.
DR   STRING; 10090.ENSMUSP00000097270; -.
DR   GlyGen; Q8BQB4; 2 sites.
DR   PhosphoSitePlus; Q8BQB4; -.
DR   MaxQB; Q8BQB4; -.
DR   PaxDb; Q8BQB4; -.
DR   PRIDE; Q8BQB4; -.
DR   ProteomicsDB; 266851; -.
DR   Antibodypedia; 25981; 87 antibodies from 23 providers.
DR   DNASU; 14221; -.
DR   Ensembl; ENSMUST00000099678; ENSMUSP00000097270; ENSMUSG00000075012.
DR   GeneID; 14221; -.
DR   KEGG; mmu:14221; -.
DR   UCSC; uc008lhw.1; mouse.
DR   CTD; 24147; -.
DR   MGI; MGI:1341907; Fjx1.
DR   VEuPathDB; HostDB:ENSMUSG00000075012; -.
DR   eggNOG; ENOG502QUJ4; Eukaryota.
DR   GeneTree; ENSGT00390000016768; -.
DR   HOGENOM; CLU_033850_0_0_1; -.
DR   InParanoid; Q8BQB4; -.
DR   OMA; YRRHEPR; -.
DR   OrthoDB; 1414662at2759; -.
DR   PhylomeDB; Q8BQB4; -.
DR   TreeFam; TF324767; -.
DR   BioGRID-ORCS; 14221; 2 hits in 73 CRISPR screens.
DR   PRO; PR:Q8BQB4; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8BQB4; protein.
DR   Bgee; ENSMUSG00000075012; Expressed in subiculum and 191 other tissues.
DR   Genevisible; Q8BQB4; MM.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR   GO; GO:0010842; P:retina layer formation; IGI:MGI.
DR   InterPro; IPR024868; FJX1/FJ.
DR   PANTHER; PTHR13147; PTHR13147; 1.
DR   PRINTS; PR02072; 4JOINTEDBOX1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..450
FT                   /note="Four-jointed box protein 1"
FT                   /id="PRO_0000333046"
FT   REGION          36..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        109
FT                   /note="L -> C (in Ref. 1; CAA08764)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  50396 MW;  4DC00C72457ECE87 CRC64;
     MGRKMRGAAA AAGLWLLALS SLLTLWGGLL PPRTELPASR PPEDRLPPHP IQSGGPAPEP
     RFPLPPPLVW DARGGSLKTF RALLTLAAGA DNPPRRHQDD RGRHEPSGLS WPEERRAVHG
     GVFWSRGLEE QVPRGFSEAQ AAAWLEVARG ARVVALDRGG CGRSSNRLAR FADGTRACVR
     YGINPEQIQG EALSYYLARL LGLQRHVPPL ALARVEARGA QWVQVQEELR TAHWTEGSVV
     SLTRWLPNLT DVVVPEPWRS EDGRLRPLRD AGGELTNLSQ AELVDLVQWT DLILFDYLTA
     NFDRLVSNLF SLQWDPRVMH RATSNLHRGP GGALVFLDNE AGLVHGYRVA GMWDKYNEPL
     LQSVCVFRER TARRVLELHR GQDAAARLLR LYSRHEPRFP ELAELSEPHA QLLQRRLDFL
     AKHILHCKAK YGRRPGDLIT LRGREGLGYE
 
 
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