FOXC2_MOUSE
ID FOXC2_MOUSE Reviewed; 494 AA.
AC Q61850; P97948; Q63869; Q8C694;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Forkhead box protein C2;
DE AltName: Full=Brain factor 3;
DE Short=BF-3;
DE AltName: Full=Forkhead-related protein FKHL14;
DE AltName: Full=Mesenchyme fork head protein 1;
DE Short=MFH-1 protein;
DE AltName: Full=Transcription factor FKH-14;
GN Name=Foxc2; Synonyms=Fkh14, Fkhl14, Mfh1;
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/6J; TISSUE=Embryo;
RX PubMed=8674414; DOI=10.1242/dev.122.6.1751;
RA Kaestner K.H., Bleckmann S.C., Monaghan A.P., Schlondorff J., Mincheva A.,
RA Lichter P., Schuetz G.;
RT "Clustered arrangement of winged helix genes fkh-6 and MFH-1: possible
RT implications for mesoderm development.";
RL Development 122:1751-1758(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC STRAIN=129, and ICR; TISSUE=Embryo;
RX PubMed=9169153; DOI=10.1006/geno.1997.4695;
RA Miura N., Iida K., Kakinuma H., Yang X.-L., Sugiyama T.;
RT "Isolation of the mouse (MFH-1) and human (FKHL 14) mesenchyme fork head-1
RT genes reveals conservation of their gene and protein structures.";
RL Genomics 41:489-492(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-494.
RX PubMed=8325367; DOI=10.1016/0014-5793(93)81785-x;
RA Miura N., Wanaka A., Tohyama M., Tanaka K.;
RT "MFH-1, a new member of the fork head domain family, is expressed in
RT developing mesenchyme.";
RL FEBS Lett. 326:171-176(1993).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-239 AND SER-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-278; ARG-292 AND ARG-452, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Transcriptional activator. Might be involved in the formation
CC of special mesenchymal tissues. {ECO:0000269|PubMed:9169153}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC -!- DEVELOPMENTAL STAGE: Expressed temporally in developing embryos, first
CC in the non-notochordal mesoderm and later in areas of mesenchymal
CC condensation in the trunk, head and limbs.
CC -!- PTM: Phosphorylation regulates FOXC2 transcriptional activity by
CC promoting its recruitment to chromatin. {ECO:0000250}.
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DR EMBL; X92499; CAA63244.1; -; mRNA.
DR EMBL; Y08222; CAA69399.1; -; Genomic_DNA.
DR EMBL; X74040; CAA52192.1; -; mRNA.
DR EMBL; AK076319; BAC36298.1; -; mRNA.
DR EMBL; S63607; AAB27463.1; -; mRNA.
DR CCDS; CCDS40499.1; -.
DR PIR; S34472; S34472.
DR RefSeq; NP_038547.2; NM_013519.2.
DR AlphaFoldDB; Q61850; -.
DR SMR; Q61850; -.
DR STRING; 10090.ENSMUSP00000055290; -.
DR iPTMnet; Q61850; -.
DR PhosphoSitePlus; Q61850; -.
DR MaxQB; Q61850; -.
DR PaxDb; Q61850; -.
DR PRIDE; Q61850; -.
DR ProteomicsDB; 271791; -.
DR Antibodypedia; 17195; 567 antibodies from 36 providers.
DR DNASU; 14234; -.
DR Ensembl; ENSMUST00000054691; ENSMUSP00000055290; ENSMUSG00000046714.
DR GeneID; 14234; -.
DR KEGG; mmu:14234; -.
DR UCSC; uc012glx.1; mouse.
DR CTD; 2303; -.
DR MGI; MGI:1347481; Foxc2.
DR VEuPathDB; HostDB:ENSMUSG00000046714; -.
DR eggNOG; KOG2294; Eukaryota.
DR GeneTree; ENSGT00940000162619; -.
DR HOGENOM; CLU_035722_3_1_1; -.
DR InParanoid; Q61850; -.
DR OMA; REMFTSH; -.
DR OrthoDB; 1270467at2759; -.
DR PhylomeDB; Q61850; -.
DR TreeFam; TF316127; -.
DR BioGRID-ORCS; 14234; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q61850; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61850; protein.
DR Bgee; ENSMUSG00000046714; Expressed in metanephric mesenchyme and 213 other tissues.
DR ExpressionAtlas; Q61850; baseline and differential.
DR Genevisible; Q61850; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IGI:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0003275; P:apoptotic process involved in outflow tract morphogenesis; IGI:MGI.
DR GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IGI:MGI.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IGI:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IGI:MGI.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IGI:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IGI:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IGI:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:MGI.
DR GO; GO:0072011; P:glomerular endothelium development; IMP:MGI.
DR GO; GO:0072144; P:glomerular mesangial cell development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0001945; P:lymph vessel development; IGI:MGI.
DR GO; GO:0001946; P:lymphangiogenesis; ISS:UniProtKB.
DR GO; GO:0001656; P:metanephros development; IMP:MGI.
DR GO; GO:1902257; P:negative regulation of apoptotic process involved in outflow tract morphogenesis; IGI:MGI.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0014032; P:neural crest cell development; IGI:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IGI:MGI.
DR GO; GO:0001503; P:ossification; IMP:MGI.
DR GO; GO:0048341; P:paraxial mesoderm formation; IGI:MGI.
DR GO; GO:0048343; P:paraxial mesodermal cell fate commitment; IMP:MGI.
DR GO; GO:0072112; P:podocyte differentiation; IMP:MGI.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IDA:BHF-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0033625; P:positive regulation of integrin activation; IC:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0035470; P:positive regulation of vascular wound healing; IDA:BHF-UCL.
DR GO; GO:0046620; P:regulation of organ growth; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0001756; P:somitogenesis; IGI:UniProtKB.
DR GO; GO:0001657; P:ureteric bud development; IMP:MGI.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IGI:MGI.
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; Developmental protein; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..494
FT /note="Forkhead box protein C2"
FT /id="PRO_0000091809"
FT DNA_BIND 70..161
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 166..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99958"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99958"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99958"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99958"
FT MOD_RES 278
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99958"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 292
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99958"
FT MOD_RES 452
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 183
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99958"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99958"
FT CONFLICT 12..13
FT /note="AL -> V (in Ref. 1; CAA63244)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="L -> I (in Ref. 3; BAC36298)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="H -> Q (in Ref. 3; BAC36298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 52874 MW; 232C0D6FA64320A6 CRC64;
MQARYSVSDP NALGVVPYLS EQNYYRAAGS YGGMASPMGV YSGHPEQYGA GMGRSYAPYH
HQPAAPKDLV KPPYSYIALI TMAIQNAPEK KITLNGIYQF IMDRFPFYRE NKQGWQNSIR
HNLSLNECFV KVPRDDKKPG KGSYWTLDPD SYNMFENGSF LRRRRRFKKK DVPKDKEERA
HLKEPPSTTA KGAPTGTPVA DGPKEAEKKV VVKSEAASPA LPVITKVETL SPEGALQASP
RSASSTPAGS PDGSLPEHHA AAPNGLPGFS VETIMTLRTS PPGGDLSPAA ARAGLVVPPL
ALPYAAAPPA AYTQPCAQGL EAAGSAGYQC SMRAMSLYTG AERPAHVCVP PALDEALSDH
PSGPGSPLGA LNLAAGQEGA LGASGHHHQH HGHLHPQAPP PAPQPPPAPQ PATQATSWYL
NHGGDLSHLP GHTFATQQQT FPNVREMFNS HRLGLDNSSL GESQVSNASC QLPYRATPSL
YRHAAPYSYD CTKY
