FOXP1_BOVIN
ID FOXP1_BOVIN Reviewed; 674 AA.
AC A4IFD2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Forkhead box protein P1;
GN Name=FOXP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; BC134525; AAI34526.1; -; mRNA.
DR RefSeq; NP_001077158.1; NM_001083689.1.
DR RefSeq; XP_005222715.1; XM_005222658.3.
DR AlphaFoldDB; A4IFD2; -.
DR SMR; A4IFD2; -.
DR STRING; 9913.ENSBTAP00000021993; -.
DR PaxDb; A4IFD2; -.
DR PRIDE; A4IFD2; -.
DR Ensembl; ENSBTAT00000021993; ENSBTAP00000021993; ENSBTAG00000016533.
DR Ensembl; ENSBTAT00000074124; ENSBTAP00000073678; ENSBTAG00000016533.
DR Ensembl; ENSBTAT00000077052; ENSBTAP00000058568; ENSBTAG00000016533.
DR Ensembl; ENSBTAT00000077766; ENSBTAP00000061757; ENSBTAG00000016533.
DR Ensembl; ENSBTAT00000085764; ENSBTAP00000072283; ENSBTAG00000016533.
DR GeneID; 515903; -.
DR KEGG; bta:515903; -.
DR CTD; 27086; -.
DR VEuPathDB; HostDB:ENSBTAG00000016533; -.
DR VGNC; VGNC:29101; FOXP1.
DR eggNOG; KOG4385; Eukaryota.
DR GeneTree; ENSGT00940000159892; -.
DR HOGENOM; CLU_019502_3_1_1; -.
DR InParanoid; A4IFD2; -.
DR TreeFam; TF326978; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000016533; Expressed in intramuscular adipose tissue and 109 other tissues.
DR ExpressionAtlas; A4IFD2; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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 2: Evidence at transcript 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..674
FT /note="Forkhead box protein P1"
FT /id="PRO_0000294518"
FT ZN_FING 304..329
FT /note="C2H2-type"
FT DNA_BIND 462..552
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..367
FT /note="Leucine-zipper"
FT REGION 380..384
FT /note="CTBP1-binding"
FT /evidence="ECO:0000250"
FT REGION 388..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..674
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 269..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT MOD_RES 650
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT CROSSLNK 370
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT CROSSLNK 375
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
FT CROSSLNK 440
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H334"
SQ SEQUENCE 674 AA; 75121 MW; 66D1C73E37ACDD80 CRC64;
MMQESGTETK SNGSAIQNGS SGGNHLLECG SLREGRSNGE TPAVDVGTAD LAHVQQQQQA
LQVARQLLLQ QQQQQQVSGL KSPKRNDKQP ALQVPVSVAM MTPQVITPQQ MQQILQQQVL
SPQQLQVLLQ QQQALMLQQQ QLQEFYKKQQ EQLQLQLLQQ HAGKQPKEQQ QVATQQLAFQ
QQLLQMQQLQ QQHLLSLQRQ GLLTIQPGQP ALPLQPLTQG MIPTELQQLW KEVTSAHTTE
ETTGNNHSSL DLTTTCVSSS APSKTSLIMN PHASTNGQLS VHTPKRESLS HEEHPHSHPL
YGHGVCKWPG CEAVCEDFQS FLKHLNSEHA LDDRSTAQCR VQMQVVQQLE LQLAKDKERL
QAMMTHLHVK STEPKTAPQP LNLVSSVTLS KSASEASPQS LPHTPTTPTA PITPATQGPS
VITTTSMHTV GPIRRRYSDK YNVPISSDIA QNQEFYKNAE VRPPFTYASL IRQAILESPE
KQLTLNEIYN WFTRMFAYFR RNAATWKNAV RHNLSLHKCF VRVENVKGAV WTVDEVEFQK
RRPQKISGNP SLIKNMQTSH AYCTPLNAAL QASMAENSIP LYTTASMGNP TLGNLASAIR
EELNGAMEHT NSNESDSSPG RSPLQAVHPV HVKEEPLDPE EAEGPLSLVT TANHSPDFDH
DRDYEDEPVN EDME
