FOXD1_MOUSE
ID FOXD1_MOUSE Reviewed; 456 AA.
AC Q61345; Q3UQW8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Forkhead box protein D1;
DE AltName: Full=Brain factor 2;
DE Short=BF-2;
DE AltName: Full=Forkhead-related protein FKHL8;
DE AltName: Full=Forkhead-related transcription factor 4;
DE Short=FREAC-4;
DE AltName: Full=HFH-BF-2;
GN Name=Foxd1; Synonyms=Fkhl8, Freac4, Hfhbf2;
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=BALB/cJ; TISSUE=Embryo;
RX PubMed=7815060; DOI=10.1002/neu.480251010;
RA Hatini V., Tao W., Lai E.;
RT "Expression of winged helix genes, BF-1 and BF-2, define adjacent domains
RT within the developing forebrain and retina.";
RL J. Neurobiol. 25:1293-1309(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and 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 FUNCTION.
RX PubMed=9811586; DOI=10.1242/dev.125.24.5019;
RA Mariani F.V., Harland R.M.;
RT "XBF-2 is a transcriptional repressor that converts ectoderm into neural
RT tissue.";
RL Development 125:5019-5031(1998).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15509772; DOI=10.1242/dev.01431;
RA Herrera E., Marcus R., Li S., Williams S.E., Erskine L., Lai E., Mason C.;
RT "Foxd1 is required for proper formation of the optic chiasm.";
RL Development 131:5727-5739(2004).
RN [5]
RP FUNCTION.
RX PubMed=15634693; DOI=10.1242/dev.01604;
RA Levinson R.S., Batourina E., Choi C., Vorontchikhina M., Kitajewski J.,
RA Mendelsohn C.L.;
RT "Foxd1-dependent signals control cellularity in the renal capsule, a
RT structure required for normal renal development.";
RL Development 132:529-539(2005).
CC -!- FUNCTION: Transcription factor involved in regulation of gene
CC expression in a variety of processes including formation of positional
CC identity in the developing retina, regionalization of the optic chiasm,
CC morphogenesis of the kidney, and neuralization of ectodermal cells
CC (PubMed:15509772, PubMed:15634693, PubMed:9811586). Involved in
CC transcriptional activation of PGF and C3 genes (By similarity).
CC {ECO:0000250|UniProtKB:Q16676, ECO:0000269|PubMed:15509772,
CC ECO:0000269|PubMed:15634693, ECO:0000269|PubMed:9811586}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the CNS and temporal
CC half of the retina. Also expressed in the condensed head mesenchyme,
CC metanephric blastema of the developing kidney, cortex of the adrenal
CC gland, condensed mesenchyme at the base of the follicles of vibrassae
CC and cartilage perichondrium of the developing vertebrate.
CC -!- DEVELOPMENTAL STAGE: At 9.5 dpc embryos, expressed in a limited region
CC of the neuroepithelium and also in the temporal half of the primary
CC optic cup and the optic stalk. At 10.5 dpc, seen in the hypothalamus,
CC temporal half of the optic stalk, and temporal hemiretina. At 12.5 dpc
CC and 13.5 dpc a high expression is seen in regions of condensed
CC mesenchyme of the head, and as neuroepithelial cells begin to
CC differentiate and migrate outward from the ventricular zone, expression
CC declines markedly. By 16.5 dpc levels are diminished and restricted to
CC unfused pockets along the exhausted ventricular zone.
CC -!- DISRUPTION PHENOTYPE: Mice show disrupted cell identity in the
CC ventrotemporal area of the retina and aberrant morphogenesis of the
CC optic chiasm. Their kidneys remain fused, have a disorganised ureteric
CC tree and fail to ascend to a lumbar position.
CC {ECO:0000269|PubMed:15509772}.
CC -!- CAUTION: Was originally assigned to be BF-2 (FOXG1).
CC {ECO:0000305|PubMed:7815060}.
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DR EMBL; L38607; AAC42042.1; -; mRNA.
DR EMBL; AK132390; BAE21140.1; -; mRNA.
DR EMBL; AK142034; BAE24920.1; -; mRNA.
DR CCDS; CCDS36759.1; -.
DR RefSeq; NP_032268.2; NM_008242.2.
DR AlphaFoldDB; Q61345; -.
DR SMR; Q61345; -.
DR STRING; 10090.ENSMUSP00000100725; -.
DR PhosphoSitePlus; Q61345; -.
DR PaxDb; Q61345; -.
DR PRIDE; Q61345; -.
DR ProteomicsDB; 267398; -.
DR Antibodypedia; 62630; 211 antibodies from 23 providers.
DR DNASU; 15229; -.
DR Ensembl; ENSMUST00000105098; ENSMUSP00000100725; ENSMUSG00000078302.
DR GeneID; 15229; -.
DR KEGG; mmu:15229; -.
DR UCSC; uc009van.1; mouse.
DR CTD; 2297; -.
DR MGI; MGI:1347463; Foxd1.
DR VEuPathDB; HostDB:ENSMUSG00000078302; -.
DR eggNOG; KOG2294; Eukaryota.
DR GeneTree; ENSGT00940000161645; -.
DR HOGENOM; CLU_040357_5_1_1; -.
DR InParanoid; Q61345; -.
DR OMA; HAGTIIP; -.
DR OrthoDB; 1270467at2759; -.
DR TreeFam; TF316127; -.
DR BioGRID-ORCS; 15229; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q61345; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61345; protein.
DR Bgee; ENSMUSG00000078302; Expressed in external carotid artery and 140 other tissues.
DR Genevisible; Q61345; MM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0008301; F:DNA binding, bending; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IDA:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0060678; P:dichotomous subdivision of terminal units involved in ureteric bud branching; IMP:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0032275; P:luteinizing hormone secretion; IMP:CACAO.
DR GO; GO:0072213; P:metanephric capsule development; IMP:UniProtKB.
DR GO; GO:0072267; P:metanephric capsule specification; IMP:UniProtKB.
DR GO; GO:0072210; P:metanephric nephron development; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0072076; P:nephrogenic mesenchyme development; IMP:UniProtKB.
DR GO; GO:0072268; P:pattern specification involved in metanephros development; IMP:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0090184; P:positive regulation of kidney development; IMP:UniProtKB.
DR GO; GO:0045944; P:positive 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 Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..456
FT /note="Forkhead box protein D1"
FT /id="PRO_0000091812"
FT DNA_BIND 130..224
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 355
FT /note="P -> R (in Ref. 1; AAC42042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 45371 MW; 3153172991DC99A4 CRC64;
MTLSTEMSDA SGLAEETDID VVGEGEDDEE EEDDDDEGGG GRGGGGSRLP SSAQRRRRSY
AGEDDLEDLE EEDDDDLLLA SRPAASPAPP GPAPAPGTGS GGCSGAGAGG GAGGGTGAGT
GGGAKNPLVK PPYSYIALIT MAILQSPKKR LTLSEICEFI SSRFPYYREK FPAWQNSIRH
NLSLNDCFVK IPREPGNPGK GNYWTLDPES ADMFDNGSFL RRRKRFKRQP LLAPHAAAEA
LLLRGAGPAA GAGDPGAALF PPPPPPPACG YGAYGCAYGL QLPPCAPPSA LFAAAAAAAA
AAFHPHSPPP PPPPPPPPPG AAAELARTAF GYRSHALAAA LPGPLQAAAV KAGGPGAAAL
ARSPFSIESL IGRTRGPAAA GAHVSSGAAS GTAPGPGGGG CAVQAAAGPA VALTRSLVVA
AAAAASSVSS SAALGTLHQG TALSSVENFT ARISNC
