FOXP4_MOUSE
ID FOXP4_MOUSE Reviewed; 795 AA.
AC Q9DBY0; Q80V92; Q8CG10; Q8CIS1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Forkhead box protein P4;
DE AltName: Full=Fork head-related protein-like A;
DE Short=mFKHLA;
GN Name=Foxp4 {ECO:0000312|MGI:MGI:1921373};
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] {ECO:0000305, ECO:0000312|EMBL:AAN08624.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAN08624.1};
RC TISSUE=Lung {ECO:0000269|PubMed:14516685};
RX PubMed=14516685; DOI=10.1016/s0925-4773(03)00116-3;
RA Lu M.M., Li S., Yang H., Morrisey E.E.;
RT "Foxp4: a novel member of the Foxp subfamily of winged-helix genes co-
RT expressed with Foxp1 and Foxp2 in pulmonary and gut tissues.";
RL Mech. Dev. 119:S197-S202(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC53799.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Daigo Y., Takayama I., Fujino M.A.;
RT "Isolation and characterization of novel human and mouse genes, which are
RT expressed in the digestive tract.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAB23479.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB23479.1};
RC TISSUE=Lung {ECO:0000312|EMBL:BAB23479.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAH52407.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52407.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH43702.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH52407.1}, and
RC Mammary gland {ECO:0000269|PubMed:15489334};
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] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12818433; DOI=10.1016/s0167-4781(03)00074-5;
RA Teufel A., Wong E.A., Mukhopadhyay M., Malik N., Westphal H.;
RT "FoxP4, a novel forkhead transcription factor.";
RL Biochim. Biophys. Acta 1627:147-152(2003).
RN [6] {ECO:0000305}
RP FUNCTION, DIMERIZATION, DOMAIN, AND MUTAGENESIS OF GLU-366.
RX PubMed=14701752; DOI=10.1128/mcb.24.2.809-822.2004;
RA Li S., Weidenfeld J., Morrisey E.E.;
RT "Transcriptional and DNA binding activity of the Foxp1/2/4 family is
RT modulated by heterotypic and homotypic protein interactions.";
RL Mol. Cell. Biol. 24:809-822(2004).
CC -!- FUNCTION: Transcriptional repressor that represses lung-specific
CC expression. {ECO:0000269|PubMed:14701752}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with FOXP1 and FOXP2.
CC Dimerization is required for DNA-binding.
CC {ECO:0000269|PubMed:14701752}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q9DBY0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q9DBY0-2; Sequence=VSP_052130, VSP_052131;
CC Name=3 {ECO:0000269|PubMed:15489334};
CC IsoId=Q9DBY0-3; Sequence=VSP_052129, VSP_052130, VSP_052131;
CC -!- TISSUE SPECIFICITY: Expressed in the adult heart, brain, spleen lung,
CC liver, kidney and testes. {ECO:0000269|PubMed:12818433,
CC ECO:0000269|PubMed:14516685}.
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly in the lung and brain
CC during embryogenesis. Expressed in the lung epithelium and the
CC mesenchyme immediately adjacent to the epithelium from 10.5 dpc. At 9.5
CC dpc, expressed in the foregut endoderm but not in the heart. At 16.5
CC and 18.5 dpc, expressed in both the proximal and distal airway
CC epithelium. Also expressed in the developing gut. In the hindgut,
CC primarily expressed in epithelial cells of the intestine and stomach.
CC Expressed in the brain in a dynamic pattern. At 14.5 dpc, expressed at
CC high levels in the intermediate zone of the neopallial cortex with
CC lower levels in the surrounding cells. By 16.5 dpc, no longer expressed
CC in the intermediate zone, but still present in the surrounding cells of
CC the neopallial cortex. {ECO:0000269|PubMed:12818433,
CC ECO:0000269|PubMed:14516685}.
CC -!- DOMAIN: The leucine-zipper is required for dimerization and
CC transcriptional repression. {ECO:0000269|PubMed:14701752}.
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DR EMBL; AY135029; AAN08624.1; -; mRNA.
DR EMBL; AB052766; BAC53799.1; -; mRNA.
DR EMBL; AK004693; BAB23479.1; -; mRNA.
DR EMBL; BC043702; AAH43702.1; -; mRNA.
DR EMBL; BC052407; AAH52407.1; -; mRNA.
DR EMBL; BC057110; AAH57110.1; -; mRNA.
DR CCDS; CCDS50135.1; -. [Q9DBY0-2]
DR RefSeq; NP_001104294.1; NM_001110824.1.
DR RefSeq; NP_001104295.1; NM_001110825.1.
DR RefSeq; NP_083043.2; NM_028767.2. [Q9DBY0-2]
DR AlphaFoldDB; Q9DBY0; -.
DR SMR; Q9DBY0; -.
DR BioGRID; 216509; 3.
DR IntAct; Q9DBY0; 1.
DR STRING; 10090.ENSMUSP00000094916; -.
DR iPTMnet; Q9DBY0; -.
DR PhosphoSitePlus; Q9DBY0; -.
DR EPD; Q9DBY0; -.
DR MaxQB; Q9DBY0; -.
DR PaxDb; Q9DBY0; -.
DR PRIDE; Q9DBY0; -.
DR ProteomicsDB; 267618; -. [Q9DBY0-1]
DR ProteomicsDB; 267619; -. [Q9DBY0-2]
DR ProteomicsDB; 267620; -. [Q9DBY0-3]
DR Antibodypedia; 1453; 272 antibodies from 35 providers.
DR DNASU; 74123; -.
DR Ensembl; ENSMUST00000113265; ENSMUSP00000108890; ENSMUSG00000023991. [Q9DBY0-2]
DR GeneID; 74123; -.
DR KEGG; mmu:74123; -.
DR UCSC; uc008cwm.2; mouse. [Q9DBY0-3]
DR UCSC; uc008cwn.2; mouse. [Q9DBY0-2]
DR CTD; 116113; -.
DR MGI; MGI:1921373; Foxp4.
DR VEuPathDB; HostDB:ENSMUSG00000023991; -.
DR eggNOG; KOG4385; Eukaryota.
DR GeneTree; ENSGT00940000158700; -.
DR HOGENOM; CLU_019502_3_1_1; -.
DR InParanoid; Q9DBY0; -.
DR OrthoDB; 836427at2759; -.
DR PhylomeDB; Q9DBY0; -.
DR TreeFam; TF326978; -.
DR BioGRID-ORCS; 74123; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Foxp4; mouse.
DR PRO; PR:Q9DBY0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9DBY0; protein.
DR Bgee; ENSMUSG00000023991; Expressed in sphenoid bone and 128 other tissues.
DR ExpressionAtlas; Q9DBY0; baseline and differential.
DR Genevisible; Q9DBY0; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
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:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0061140; P:lung secretory cell differentiation; IGI:MGI.
DR GO; GO:1901250; P:negative regulation of lung goblet cell differentiation; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:1901249; P:regulation of lung goblet cell differentiation; IGI: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; IPR032354; FOXP-CC.
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 Pfam; PF16159; FOXP-CC; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..795
FT /note="Forkhead box protein P4"
FT /id="PRO_0000247653"
FT ZN_FING 312..337
FT /note="C2H2-type"
FT /evidence="ECO:0000255"
FT DNA_BIND 459..549
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..375
FT /note="Leucine-zipper"
FT REGION 379..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVH2"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVH2"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVH2"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IVH2"
FT CROSSLNK 383
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IVH2"
FT VAR_SEQ 388
FT /note="P -> PLNPVPGSSSFSK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14516685,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_052129"
FT VAR_SEQ 672
FT /note="P -> S (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14516685,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_052130"
FT VAR_SEQ 673..795
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14516685,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_052131"
FT MUTAGEN 366
FT /note="Missing: Loss of dimerization. Almost complete loss
FT of DNA-binding. Reduced transcriptional repression
FT activity."
FT /evidence="ECO:0000269|PubMed:14701752"
FT CONFLICT 226
FT /note="A -> AA (in Ref. 2; AAN08624 and 4; AAH43702/
FT AAH52407)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 85981 MW; 860AE60AAD3742CE CRC64;
MMVESASETI RSAPSGQNGV GSLSAQADGG GGAGTAGTAP AAGRDASGRE AASGGADSNG
EMSPAELLHF QQQQALQVAR QFLLQQASSL NSPGNNDSKQ SASAVQVPVS VAMMSQQMLT
PQQMQQILSP PQLQALLQQQ QALMLQQLQE YYKKQQEQLH LQLLTQQQAG KQQPKEALGN
KQLAFQQQLL QMQQLQQQHL LNLQRQGLVS LQPSQASGPL QALPQAVCPT DLPQLWKGEG
APGQPAEDSG RQEGLDLAST AVTATSFASP PKVSPPLSHH PLPNGQPTVL TSRRDSSSHE
ETPSSHPLYG HGECKWPGCE TLCEDLGQFI KHLNTEHALD DRSTAQCRVQ MQVVQQLEIQ
LAKESERLQA MMAHLHMRPS EPKPFSQPVT VSADPFPDGL VHPPTSAAAP VTPLRPPGLG
SASLHSGGPA RRRSNDKFCS PISSELAQNH EFYKNADVRP PFTYASLIRQ AILETPDRQL
TLNEIYNWFT RMFAYFRRNT ATWKNAVRHN LSLHKCFVRV ENVKGAVWTV DEREYQKRRP
PKMTGSPTLV KNMISGLSYG ALNASYQAAL AESSFPLLSN PGMLNPGSAS SLLPLSQEDL
GVPGEPLPSN GSSSPPRLSP PQYSHQIQVK EEPAEAEEDR RPGPPLGAPN PSTVGPPEDR
DLEEDLGGED MPSQPCPLIP GWKPSLLHLS YCVKPKFTVS VGSKTPSSPL PPPPRVQGSY
SLPPCSYLAY GDMRGQNPAP SPGLLSGVGG GLFRCLHRTK SPSLPGVWIL AAELETMRFH
RPPMGDPQPK TADWV
