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FOXC1_XENTR
ID   FOXC1_XENTR             Reviewed;         495 AA.
AC   Q68F77;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Forkhead box protein C1 {ECO:0000312|EMBL:AAH79966.1};
GN   Name=foxc1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAH79966.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula {ECO:0000312|EMBL:AAH79966.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) 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}.
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DR   EMBL; BC079966; AAH79966.1; -; mRNA.
DR   RefSeq; NP_001007864.1; NM_001007863.1.
DR   AlphaFoldDB; Q68F77; -.
DR   SMR; Q68F77; -.
DR   STRING; 8364.ENSXETP00000001313; -.
DR   PaxDb; Q68F77; -.
DR   DNASU; 493250; -.
DR   Ensembl; ENSXETT00000001313; ENSXETP00000001313; ENSXETG00000000594.
DR   GeneID; 493250; -.
DR   KEGG; xtr:493250; -.
DR   CTD; 2296; -.
DR   Xenbase; XB-GENE-479055; foxc1.
DR   eggNOG; KOG2294; Eukaryota.
DR   HOGENOM; CLU_035722_3_1_1; -.
DR   InParanoid; Q68F77; -.
DR   OMA; ASWYGDL; -.
DR   OrthoDB; 1270467at2759; -.
DR   PhylomeDB; Q68F77; -.
DR   TreeFam; TF316127; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000000594; Expressed in gastrula and 25 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR   GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:1990869; P:cellular response to chemokine; ISS:UniProtKB.
DR   GO; GO:0061300; P:cerebellum vasculature development; IEA:Ensembl.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0061386; P:closure of optic fissure; IEA:Ensembl.
DR   GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0007498; P:mesoderm development; ISS:UniProtKB.
DR   GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR   GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl.
DR   GO; GO:0033339; P:pectoral fin development; IEA:Ensembl.
DR   GO; GO:0072149; P:podocyte cell fate commitment; IEA:Ensembl.
DR   GO; GO:0072015; P:podocyte development; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0039021; P:pronephric glomerulus development; IEA:Ensembl.
DR   GO; GO:0048793; P:pronephros development; ISS:UniProtKB.
DR   GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:1902366; P:regulation of Notch signaling pathway involved in somitogenesis; IEA:Ensembl.
DR   GO; GO:2000583; P:regulation of platelet-derived growth factor receptor-alpha signaling pathway; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0043114; P:regulation of vascular permeability; IEA:Ensembl.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0035886; P:vascular associated smooth muscle cell differentiation; IEA:Ensembl.
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"
FT                   /id="PRO_0000390739"
FT   DNA_BIND        79..173
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          175..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   495 AA;  53900 MW;  ACA1620E6D20B799 CRC64;
     MQARYSVSSP NSLGVVPYLS GEQSYYRAAA AAAAAGGGYT GMAAPMSMYS HPAHEQYQAG
     MARAYGPYTP QPQPKDMVKP PYSYIALITM AIQNAPEKKI TLNGIYQFIM ERFPFYRDNK
     QGWQNSIRHN LSLNECFVKV PRDDKKPGKG SYWTLDPDSY NMFENGSFLR RRRRFKKKDV
     VKDATKEDKD RLLKEHHGSQ PAAAQQQRQQ QQGQAQAEQD SGSQPVRIQD IKTENGTSSP
     PQAMSPALST VPKIESPDSS SSMSSGSPHS IPSNRSMSLE AAESHHPHQQ HHHSQGFSVD
     NIMTSLRGSP QGSGELPSPL ISSSRTGIAP SSLLTYSPGQ GSIYSPPCSQ GTSSGGGAGT
     YHCNMQAMSL YSGDRSGHLT PANTPAATTV EDTLPDYSIT TTTTSALSHG NQEHPHQGRL
     PSWYLNQAGD LGHLAGATYP GQQQNFHSVR EMFESQRLGL NSSPVNGNSS CQMSFPPSQS
     LYRTSGAFVY DCSKF
 
 
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