FXC1B_XENLA
ID FXC1B_XENLA Reviewed; 495 AA.
AC Q32NP8;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Forkhead box protein C1-B;
GN Name=foxc1-b; Synonyms=foxc1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAI08536.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula {ECO:0000312|EMBL:AAI08536.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-binding transcriptional factor that plays a role in a
CC broad range of cellular and developmental processes such as eye, bones,
CC cardiovascular, kidney and skin development. Acts either as a
CC transcriptional activator or repressor. Binds to the consensus binding
CC site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in promoter of target genes. Upon
CC DNA-binding, promotes DNA bending. Required for cell viability and
CC resistance to oxidative stress in the eye. Promotes cell growth
CC inhibition by stopping the cell cycle in the G1 phase through TGFB1-
CC mediated signals. Involved in epithelial-mesenchymal transition (EMT)
CC induction by increasing cell proliferation, migration and invasion.
CC Involved in chemokine-induced endothelial cell migration. Plays a role
CC in epidermal keratinocyte terminal differentiation. Essential
CC developmental transcriptional factor required for mesoderm-derived
CC tissues formation, such as the somites, skin, bone and cartilage. Plays
CC a role in the development and maintenance of mesenchymal niches for
CC haematopoietic stem and progenitor cells (HSPC). Plays a role in
CC corneal transparency by preventing both blood vessel and lymphatic
CC vessel growth during embryonic development in a VEGF-dependent manner.
CC Plays a role at the gastrula stage for expression of several mesodermal
CC and endodermal genes. At the late neurula stage, regulates expression
CC of adhesion genes to maintain cell adhesion in the mesodermal germ
CC layer. {ECO:0000250|UniProtKB:Q12948, ECO:0000250|UniProtKB:Q61572,
CC ECO:0000250|UniProtKB:Q9PVZ3}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61572}.
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; BC108535; AAI08536.1; -; mRNA.
DR RefSeq; NP_001089846.1; NM_001096377.1.
DR AlphaFoldDB; Q32NP8; -.
DR SMR; Q32NP8; -.
DR DNASU; 734912; -.
DR GeneID; 734912; -.
DR KEGG; xla:734912; -.
DR CTD; 734912; -.
DR Xenbase; XB-GENE-865236; foxc1.L.
DR OMA; HCNLQAM; -.
DR OrthoDB; 1270467at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 734912; Expressed in internal ear and 14 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0001568; P:blood vessel development; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:1990869; P:cellular response to chemokine; ISS:UniProtKB.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0007498; P:mesoderm development; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0048793; P:pronephros development; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR033067; FoxC1.
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 PANTHER; PTHR11829:SF68; PTHR11829:SF68; 1.
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..495
FT /note="Forkhead box protein C1-B"
FT /id="PRO_0000390738"
FT DNA_BIND 79..173
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 175..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 53980 MW; 7417E99391781079 CRC64;
MQARYSVSSP NSLGVVPYLS GEQSYYRAAA AAAAAGGGYT GMAAPMSMYS HPAHEQYQAG
MARAYGPYTP QPQPKDMVKP PYSYIALITM AIQNAPDKKI TLNGIYQFIM ERFPFYRDNK
QGWQNSIRHN LSLNECFVKV PRDDKKPGKG SYWTLDPDSY NMFENGSFLR RRRRFKKKDV
SKDATKEDKE RLLKEHNGSQ SAAAQQQRQQ QNQAQAEQDG SSQPVRIQDI KTENGTSSPP
QSMSPALSAV PKIESPDSSS SMSSGSPHSI PSNRSMSLEA AESHHPHQQQ HHHHSQGFSV
DNIMTSLRGS PQGSGELPSP LISSSRTGIA PSLSLTYSPS QGSIYSPPCS QGSSSGGGAG
TYHCNMQAMS LYSGDRSGHL TPANTPAATT VEETLPDYSI TTTTSALSHG NQEHPHQGRL
PSWYLNQTGD LGHLAGASYP GQQQNFHSVR EMFESQRLGL NSSPVNGNSS CQMSFPPSQS
LYRTSGAFVY DCSKF