FOXP1_RAT
ID FOXP1_RAT Reviewed; 711 AA.
AC Q498D1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Forkhead box protein P1;
GN Name=Foxp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional repressor. Can act with CTBP1 to
CC synergistically repress transcription but CTPBP1 is not essential.
CC Plays an important role in the specification and differentiation of
CC lung epithelium. Acts cooperatively with FOXP4 to regulate lung
CC secretory epithelial cell fate and regeneration by restricting the
CC goblet cell lineage program; the function may involve regulation of
CC AGR2. Essential transcriptional regulator of B-cell development.
CC Involved in regulation of cardiac muscle cell proliferation. Involved
CC in the columnar organization of spinal motor neurons. Promotes the
CC formation of the lateral motor neuron column (LMC) and the
CC preganglionic motor column (PGC) and is required for respective
CC appropriate motor axon projections. The segment-appropriate generation
CC of spinal cord motor columns requires cooperation with other Hox
CC proteins. Can regulate PITX3 promoter activity; may promote midbrain
CC identity in embryonic stem cell-derived dopamine neurons by regulating
CC PITX3. Negatively regulates the differentiation of T follicular helper
CC cells T(FH)s. Involved in maintenance of hair follicle stem cell
CC quiescence; the function probably involves regulation of FGF18.
CC Represses transcription of various pro-apoptotic genes and cooperates
CC with NF-kappa B-signaling in promoting B-cell expansion by inhibition
CC of caspase-dependent apoptosis. Binds to CSF1R promoter elements and is
CC involved in regulation of monocyte differentiation and macrophage
CC functions; repression of CSF1R in monocytes seems to involve NCOR2 as
CC corepressor. Involved in endothelial cell proliferation, tube formation
CC and migration indicative for a role in angiogenesis; the role in
CC neovascularization seems to implicate suppression of SEMA5B. Can
CC negatively regulate androgen receptor signaling (By similarity). Acts
CC as a transcriptional activator of the FBXL7 promoter; this activity is
CC regulated by AURKA (By similarity). {ECO:0000250|UniProtKB:P58462,
CC ECO:0000250|UniProtKB:Q9H334}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with FOXP2 and FOXP4.
CC Dimerization is required for DNA-binding. Self-associates. Interacts
CC with CTBP1. Interacts with NCOR2 and AR. Interacts with FOXP2 (By
CC similarity). Interacts with TBR1 (By similarity). Interacts with AURKA;
CC this interaction facilitates the phosphorylation of FOXP1, which
CC suppresses the expression of FBXL7 (By similarity). Interacts with
CC ZMYM2 (By similarity). {ECO:0000250|UniProtKB:P58462,
CC ECO:0000250|UniProtKB:Q9H334}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H334}. Note=Not
CC found in the nucleolus. {ECO:0000250|UniProtKB:Q9H334}.
CC -!- DOMAIN: The leucine-zipper is required for dimerization and
CC transcriptional repression. {ECO:0000250|UniProtKB:P58462}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC100267; AAI00268.1; -; mRNA.
DR RefSeq; NP_001029303.1; NM_001034131.1.
DR RefSeq; XP_008761370.1; XM_008763148.1.
DR RefSeq; XP_008761371.1; XM_008763149.2.
DR RefSeq; XP_008761372.1; XM_008763150.2.
DR RefSeq; XP_008761374.1; XM_008763152.2.
DR RefSeq; XP_008761375.1; XM_008763153.2.
DR AlphaFoldDB; Q498D1; -.
DR SMR; Q498D1; -.
DR STRING; 10116.ENSRNOP00000013271; -.
DR iPTMnet; Q498D1; -.
DR PhosphoSitePlus; Q498D1; -.
DR PaxDb; Q498D1; -.
DR PRIDE; Q498D1; -.
DR Ensembl; ENSRNOT00000013271; ENSRNOP00000013271; ENSRNOG00000009184.
DR GeneID; 297480; -.
DR KEGG; rno:297480; -.
DR UCSC; RGD:1308669; rat.
DR CTD; 27086; -.
DR RGD; 1308669; Foxp1.
DR eggNOG; KOG4385; Eukaryota.
DR GeneTree; ENSGT00940000159892; -.
DR HOGENOM; CLU_019502_3_1_1; -.
DR InParanoid; Q498D1; -.
DR OMA; GHAYCTP; -.
DR OrthoDB; 836427at2759; -.
DR PhylomeDB; Q498D1; -.
DR TreeFam; TF326978; -.
DR PRO; PR:Q498D1; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009184; Expressed in spleen and 19 other tissues.
DR Genevisible; Q498D1; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:RGD.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0072359; P:circulatory system development; ISO:RGD.
DR GO; GO:0042118; P:endothelial cell activation; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0033152; P:immunoglobulin V(D)J recombination; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0098582; P:innate vocalization behavior; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0061140; P:lung secretory cell differentiation; ISO:RGD.
DR GO; GO:0042116; P:macrophage activation; ISO:RGD.
DR GO; GO:0042117; P:monocyte activation; ISO:RGD.
DR GO; GO:0008045; P:motor neuron axon guidance; ISO:RGD.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:RGD.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; ISO:RGD.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:1901250; P:negative regulation of lung goblet cell differentiation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0036035; P:osteoclast development; ISO:RGD.
DR GO; GO:0030316; P:osteoclast differentiation; ISO:RGD.
DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:1905206; P:positive regulation of hydrogen peroxide-induced cell death; IMP:RGD.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:RGD.
DR GO; GO:0032745; P:positive regulation of interleukin-21 production; ISO:RGD.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0002329; P:pre-B cell differentiation; ISO:RGD.
DR GO; GO:0098900; P:regulation of action potential; ISO:RGD.
DR GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; ISO:RGD.
DR GO; GO:2000341; P:regulation of chemokine (C-X-C motif) ligand 2 production; ISO:RGD.
DR GO; GO:1900424; P:regulation of defense response to bacterium; ISO:RGD.
DR GO; GO:1901509; P:regulation of endothelial tube morphogenesis; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; ISO:RGD.
DR GO; GO:0032655; P:regulation of interleukin-12 production; ISO:RGD.
DR GO; GO:1901249; P:regulation of lung goblet cell differentiation; ISO:RGD.
DR GO; GO:1901256; P:regulation of macrophage colony-stimulating factor production; ISO:RGD.
DR GO; GO:0045655; P:regulation of monocyte differentiation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0048745; P:smooth muscle tissue development; ISO:RGD.
DR GO; GO:0021756; P:striatum development; IEP:RGD.
DR GO; GO:0061470; P:T follicular helper cell differentiation; ISO:RGD.
DR GO; GO:0021517; P:ventral spinal cord development; ISO:RGD.
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 DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..711
FT /note="Forkhead box protein P1"
FT /id="PRO_0000294519"
FT ZN_FING 340..365
FT /note="C2H2-type"
FT DNA_BIND 499..589
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..403
FT /note="Leucine-zipper"
FT REGION 416..420
FT /note="CTBP1-binding"
FT /evidence="ECO:0000250"
FT REGION 424..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT MOD_RES 687
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT CROSSLNK 321
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT CROSSLNK 411
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
SQ SEQUENCE 711 AA; 79586 MW; 9DE9B570A79CAFB9 CRC64;
MMQESGSEAK SNGSTIQNGS SGGNHLLECG TLRDTRSNGE APAVDLGAAD LAHVQQQQQQ
ALQVARQLLL QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQV SGLKSPKRND
KQPALQVPVS VAMMTPQVIT PQQMQQILQQ QVLSPQQLQV LLQQQQALML QQQQLQEFYK
KQQEQLQLQL LQQQHAGKQP KEQQQQQVAT QQLAFQQQLL QMQQLQQQHL LSLQRQGLLT
IQPGQPALPL QPLAQGMIPT ELQQLWKEVT SAHTAEETTG SNHSSLDLTS TCVSSSAPSK
TSLIMNPHAS TNGQLSVHTP KRESLSHEEH PHSHPLYGHG VCKWPGCEAV CDDFPAFLKH
LNSEHALDDR STAQCRVQMQ VVQQLELQLA KDKERLQAMM THLHVKSTEP KAAPQPLNLV
SSVTLSKSAS EASPQSLPHT PTTPTAPLTP VTQGPSVITT TSMHTVGPIR RRYSDKYNVP
ISSADIAQNQ EFYKNAEVRP PFTYASLIRQ AILESPEKQL TLNEIYNWFT RMFAYFRRNA
ATWKNAVRHN LSLHKCFVRV ENVKGAVWTV DEVEFQKRRP QKISGNPSLI KNMQSGHAYC
TPLNAALQAS MAENSIPLYT TASMGNPTLG SLASAIREEL NGAMEHTNSN ESDSSPGRSP
MQAVHPIHVK EEPLDPEEAE GPLSLVTTAN HSPDFDHDRD YEDEPVNEDM E
