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FOXQ1_MOUSE
ID   FOXQ1_MOUSE             Reviewed;         400 AA.
AC   O70220; Q9JJ18;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Forkhead box protein Q1;
DE   AltName: Full=HFH-1l;
DE   AltName: Full=HNF-3/forkhead-like protein 1;
DE            Short=HFH-1;
DE   AltName: Full=Hepatocyte nuclear factor 3 forkhead homolog 1;
GN   Name=Foxq1; Synonyms=Hfh1, Hfh1l;
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], AND TISSUE SPECIFICITY.
RC   STRAIN=129; TISSUE=Kidney;
RX   PubMed=9726250; DOI=10.1089/dna.1998.17.679;
RA   Frank S., Zoll B.;
RT   "Mouse HNF-3/fork head homolog-1-like gene: structure, chromosomal
RT   location, and expression in adult and embryonic kidney.";
RL   DNA Cell Biol. 17:679-688(1998).
RN   [2]
RP   SEQUENCE REVISION.
RA   Pasche B., Bieller A., Zoll B.;
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISEASE.
RC   STRAIN=129;
RX   PubMed=11309849; DOI=10.1002/gene.1020;
RA   Hong H.-K., Noveroske J.K., Headon D.J., Liu T., Sy M.S., Justice M.J.,
RA   Chakravarti A.;
RT   "The winged helix/forkhead transcription factor Foxq1 regulates
RT   differentiation of hair in satin mice.";
RL   Genesis 29:163-171(2001).
RN   [4]
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   [5]
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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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   [8]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16835220; DOI=10.1074/jbc.m603646200;
RA   Potter C.S., Peterson R.L., Barth J.L., Pruett N.D., Jacobs D.F.,
RA   Kern M.J., Argraves W.S., Sundberg J.P., Awgulewitsch A.;
RT   "Evidence that the satin hair mutant gene Foxq1 is among multiple and
RT   functionally diverse regulatory targets for Hoxc13 during hair follicle
RT   differentiation.";
RL   J. Biol. Chem. 281:29245-29255(2006).
CC   -!- FUNCTION: Plays a role in hair follicle differentiation.
CC       {ECO:0000269|PubMed:16835220}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney and stomach. Expression in the
CC       outer medulla of the kidney and the transitional epithelium. Expressed
CC       in the hair follicle medulla. {ECO:0000269|PubMed:16835220,
CC       ECO:0000269|PubMed:9726250}.
CC   -!- DISEASE: Note=Defects in Foxq1 are the cause of the satin (sa)
CC       phenotype and results in a silky coat with high sheen arising from
CC       structurally abnormal medulla cells and defects in differentiation of
CC       the hair shaft. {ECO:0000269|PubMed:11309849}.
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DR   EMBL; AF010405; AAC12973.2; -; Genomic_DNA.
DR   EMBL; AF154426; AAF74524.1; -; Genomic_DNA.
DR   EMBL; AK147202; BAE27760.1; -; mRNA.
DR   EMBL; AL589738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466561; EDL32371.1; -; Genomic_DNA.
DR   EMBL; BC047155; AAH47155.1; -; mRNA.
DR   CCDS; CCDS26423.1; -.
DR   RefSeq; NP_032265.3; NM_008239.4.
DR   AlphaFoldDB; O70220; -.
DR   SMR; O70220; -.
DR   BioGRID; 200287; 2.
DR   IntAct; O70220; 2.
DR   STRING; 10090.ENSMUSP00000036952; -.
DR   iPTMnet; O70220; -.
DR   PhosphoSitePlus; O70220; -.
DR   PaxDb; O70220; -.
DR   PRIDE; O70220; -.
DR   ProteomicsDB; 267512; -.
DR   Antibodypedia; 9198; 475 antibodies from 31 providers.
DR   DNASU; 15220; -.
DR   Ensembl; ENSMUST00000042118; ENSMUSP00000036952; ENSMUSG00000038415.
DR   GeneID; 15220; -.
DR   KEGG; mmu:15220; -.
DR   UCSC; uc007pzj.2; mouse.
DR   CTD; 94234; -.
DR   MGI; MGI:1298228; Foxq1.
DR   VEuPathDB; HostDB:ENSMUSG00000038415; -.
DR   eggNOG; KOG2294; Eukaryota.
DR   GeneTree; ENSGT00940000162937; -.
DR   HOGENOM; CLU_055457_0_0_1; -.
DR   InParanoid; O70220; -.
DR   OMA; AYGMGEP; -.
DR   OrthoDB; 1270467at2759; -.
DR   TreeFam; TF316127; -.
DR   BioGRID-ORCS; 15220; 2 hits in 75 CRISPR screens.
DR   PRO; PR:O70220; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; O70220; protein.
DR   Bgee; ENSMUSG00000038415; Expressed in urinary bladder urothelium and 134 other tissues.
DR   Genevisible; O70220; MM.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..400
FT                   /note="Forkhead box protein Q1"
FT                   /id="PRO_0000091891"
FT   DNA_BIND        115..210
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        238
FT                   /note="P -> A (in Ref. 1; AAC12973)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  41368 MW;  F286AEEF81D4759B CRC64;
     MKLEVFVPRA AHGDKMGSDL EGAGSSDVPS PLSAAGDDSL GSDGDCAANS PAAGSGAGDL
     EGGGGERNSS GGPSAQDGPE ATDDSRTQAS AAGPCAGGVG GGEGARSKPY TRRPKPPYSY
     IALIAMAIRD SAGGRLTLAE INEYLMGKFP FFRGSYTGWR NSVRHNLSLN DCFVKVLRDP
     SRPWGKDNYW MLNPNSEYTF ADGVFRRRRK RLSHRTTVSA SGLRPEEAPP GPAGTPQPAP
     AARSSPIARS PARQEERSSP ASKFSSSFAI DSILSKPFRS RRDGDSALGV QLPWGAAPCP
     PLRAYPALLP AAPGGALLPL CAYGASEPTL LASRGTEVQP AAPLLLAPLS TAAPAKPFRG
     PETAGAAHLY CPLRLPTALQ AAAACGPGPH LSYPVETLLA
 
 
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