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FXC1A_XENLA
ID   FXC1A_XENLA             Reviewed;         492 AA.
AC   Q9PVZ3; B7ZQ99; B7ZQA1; B7ZRK5; Q9YHB2;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Forkhead box protein C1-A;
DE            Short=FoxC1 {ECO:0000303|PubMed:17705306};
DE   AltName: Full=Fork head domain-related protein 11 {ECO:0000303|PubMed:9767159};
DE            Short=XFD-11 {ECO:0000303|PubMed:9767159, ECO:0000312|EMBL:CAB44727.1};
GN   Name=foxc1-a; 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:0000305, ECO:0000312|EMBL:AAC99469.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Gastrula {ECO:0000269|PubMed:9767159};
RX   PubMed=9767159; DOI=10.1016/s0925-4773(98)00123-3;
RA   Koester M., Dillinger K., Knoechel W.;
RT   "Expression pattern of the winged helix factor XFD-11 during Xenopus
RT   embryogenesis.";
RL   Mech. Dev. 76:169-173(1998).
RN   [2] {ECO:0000312|EMBL:CAB44727.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Knoechel W.;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|EMBL:CAB44727.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula {ECO:0000312|EMBL:AAI69731.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000305}
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17705306; DOI=10.1002/dvdy.21240;
RA   Cha J.Y., Birsoy B., Kofron M., Mahoney E., Lang S., Wylie C., Heasman J.;
RT   "The role of FoxC1 in early Xenopus development.";
RL   Dev. Dyn. 236:2731-2741(2007).
RN   [5] {ECO:0000305}
RP   REVIEW.
RX   PubMed=15656969; DOI=10.1016/j.gene.2004.09.037;
RA   Pohl B.S., Knoechel W.;
RT   "Of fox and frogs: fox (fork head/winged helix) transcription factors in
RT   Xenopus development.";
RL   Gene 344:21-32(2005).
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       (By similarity). Plays a role at the gastrula stage for expression of
CC       several mesodermal and endodermal genes (PubMed:17705306). At the late
CC       neurula stage, regulates expression of adhesion genes to maintain cell
CC       adhesion in the mesodermal germ layer (PubMed:17705306).
CC       {ECO:0000250|UniProtKB:Q12948, ECO:0000250|UniProtKB:Q61572,
CC       ECO:0000269|PubMed:17705306}.
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61572}.
CC   -!- TISSUE SPECIFICITY: In gastrulae, expressed in ventral and lateral but
CC       not dorsal mesoderm. In neurulae, expressed in the posterior mesoderm
CC       except for the dorsal midline, and also at the lateral border of the
CC       neural plate and within anterior neuroectoderm. From tailbud stages,
CC       expressed in the pronephros, heart, neural crest cells surrounding the
CC       eye, in the mandibular, hyoid and branchial arches, and within the
CC       tail. {ECO:0000269|PubMed:17705306, ECO:0000269|PubMed:9767159}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from late blastula/early gastrula stage
CC       throughout embryogenesis. {ECO:0000269|PubMed:9767159}.
CC   -!- INDUCTION: By vegt, acting via nodal signaling.
CC       {ECO:0000269|PubMed:17705306}.
CC   -!- DISRUPTION PHENOTYPE: Embryos gastrulate and neurulate, but at the
CC       tailbud stage show stunted growth and loss of cells at the blastopore.
CC       Embryos continue to develop but display shortened axes and abnormal gut
CC       and heart development by the swimming tadpole stage.
CC       {ECO:0000269|PubMed:17705306}.
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DR   EMBL; AF116844; AAC99469.1; -; mRNA.
DR   EMBL; AJ242675; CAB44727.1; -; mRNA.
DR   EMBL; BC169731; AAI69731.1; -; mRNA.
DR   EMBL; BC169733; AAI69733.1; -; mRNA.
DR   EMBL; BC170199; AAI70199.1; -; mRNA.
DR   EMBL; BC170201; AAI70201.1; -; mRNA.
DR   RefSeq; NP_001080937.1; NM_001087468.1.
DR   RefSeq; NP_001081683.1; NM_001088214.1.
DR   AlphaFoldDB; Q9PVZ3; -.
DR   SMR; Q9PVZ3; -.
DR   PRIDE; Q9PVZ3; -.
DR   GeneID; 394280; -.
DR   GeneID; 397996; -.
DR   KEGG; xla:397996; -.
DR   CTD; 394280; -.
DR   CTD; 397996; -.
DR   Xenbase; XB-GENE-6252135; foxc1.S.
DR   OMA; ASWYGDL; -.
DR   OrthoDB; 1270467at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 397996; Expressed in internal ear and 10 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; IMP: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; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0048793; P:pronephros development; IEP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IMP: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..492
FT                   /note="Forkhead box protein C1-A"
FT                   /id="PRO_0000390737"
FT   DNA_BIND        79..173
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          175..323
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        199..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        51
FT                   /note="H -> F (in Ref. 1; AAC99469)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="R -> E (in Ref. 1; AAC99469)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="T -> A (in Ref. 1; AAC99469)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="G -> V (in Ref. 3; AAI69731)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="P -> L (in Ref. 1; AAC99469)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="L -> F (in Ref. 3; AAI70199)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        358
FT                   /note="G -> E (in Ref. 3; AAI69731/AAI69733)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   492 AA;  53674 MW;  66906A5A99A2FD4E CRC64;
     MQARYSVSSP NSLGVVPYLS GEQSYYRAAA AAAAAGGGYT GMAAPMSMYS HPAHEQYQAG
     MARAYGPYTP QPQPKDMVKP PYSYIALITM AIQNAPDKKI TLNGIYQFIM ERFPFYRDNK
     QGWQNSIRHN LSLNECFVKV PRDDKKPGKG SYWTLDPDSY NMFENGSFLR RRRRFKKKDV
     SKDATKEDKE RLLKEHHGSQ SAAAQQQRQQ QQSQAQAEQD SNSQPVRIQD IKTENGTSSP
     PQSMSPALSA VPKIESPDSS SSMSSGSPHS IPSNRSMSLE AAESHHPHHQ QHSQGFSVDN
     IMTSLRGSPQ GSAELPSPLI SSSRTGIAPS LSLSYSPGQG SIYSSPCSQG TSSGGGAGTY
     HCNMQAMSLY SGDRSGHLTP ANTPAATTVE ETLPDYSIST TSAQSHGNQE HPHQGRLPSW
     YLNQTGELGH LAGATYPGQQ QNFHSVREMF ESQRLALNSS PVNGNSSCQM SFPPSQSLYR
     TSGAFVYDCS KF
 
 
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