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FXI1B_XENLA
ID   FXI1B_XENLA             Reviewed;         367 AA.
AC   Q91905; Q6DCJ0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Forkhead box protein I1-B;
DE            Short=FoxI1-B;
DE            Short=FoxI1b;
DE            Short=xFoxI1b;
DE   AltName: Full=Fork head domain-related protein 2';
DE            Short=xFD-2';
DE            Short=xFD2';
GN   Name=foxi1-b;
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:CAA52365.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Gastrula {ECO:0000269|PubMed:8199048};
RX   PubMed=8199048; DOI=10.1016/0925-4773(94)90025-6;
RA   Lef J., Clement J.H., Oschwald R., Koester M., Knoechel W.;
RT   "Spatial and temporal transcription patterns of the forkhead related XFD-
RT   2/XFD-2' genes in Xenopus laevis embryos.";
RL   Mech. Dev. 45:117-126(1994).
RN   [2] {ECO:0000312|EMBL:AAH78036.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH78036.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 119-214.
RC   TISSUE=Gastrula {ECO:0000269|PubMed:1358174};
RX   PubMed=1358174; DOI=10.1016/0925-4773(92)90007-7;
RA   Knoechel S., Lef J., Clement J.H., Klocke B., Hille S., Koester M.,
RA   Knoechel W.;
RT   "Activin A induced expression of a fork head related gene in posterior
RT   chordamesoderm (notochord) of Xenopus laevis embryos.";
RL   Mech. Dev. 38:157-165(1992).
RN   [4] {ECO:0000305}
RP   IDENTIFICATION.
RX   PubMed=7937122; DOI=10.1093/nar/22.19.3990;
RA   King M.W., Moore M.J.;
RT   "Novel HOX, POU and FKH genes expressed during bFGF-induced mesodermal
RT   differentiation in Xenopus.";
RL   Nucleic Acids Res. 22:3990-3996(1994).
RN   [5] {ECO:0000305}
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=16079156; DOI=10.1242/dev.01959;
RA   Matsuo-Takasaki M., Matsumura M., Sasai Y.;
RT   "An essential role of Xenopus Foxi1a for ventral specification of the
RT   cephalic ectoderm during gastrulation.";
RL   Development 132:3885-3894(2005).
RN   [6] {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: Transcription factor. Essential for ventral specification of
CC       the early cephalic (head) ectoderm during gastrulation, playing a role
CC       in the 'non-neural' versus 'neural' cell fate choice. Binds to DNA via
CC       the target sequence 5'-[AG]TAAA[CT]A-3', with 5'-ATAAACA-3' being the
CC       preferred binding site. {ECO:0000269|PubMed:16079156}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Initially localized to the animal hemisphere (the
CC       presumptive ectoderm) of early-mid blastula embryos. Becomes restricted
CC       to head placodes, excluding the otic placodes, by the tailbud stages.
CC       {ECO:0000269|PubMed:16079156, ECO:0000269|PubMed:8199048}.
CC   -!- DEVELOPMENTAL STAGE: Expression begins at the early-mid blastula stage.
CC       Levels are highest in the blastula and gastrula stages, after which
CC       levels decrease until the somite segregation stages. Expression
CC       persists to later developmental stages at a slightly higher extent than
CC       that of foxi1-A. {ECO:0000269|PubMed:16079156,
CC       ECO:0000269|PubMed:8199048}.
CC   -!- INDUCTION: Induced by Bmp-signaling. Suppressed by Wnt-signaling.
CC       {ECO:0000269|PubMed:16079156}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH78036.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X74316; CAA52365.1; -; mRNA.
DR   EMBL; BC078036; AAH78036.1; ALT_INIT; mRNA.
DR   PIR; C56556; C56556.
DR   PIR; S49009; S49009.
DR   RefSeq; NP_001081619.1; NM_001088150.1.
DR   AlphaFoldDB; Q91905; -.
DR   SMR; Q91905; -.
DR   GeneID; 397955; -.
DR   KEGG; xla:397955; -.
DR   CTD; 397955; -.
DR   Xenbase; XB-GENE-6252155; foxi4.2.L.
DR   OrthoDB; 1270467at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 397955; Expressed in gastrula and 3 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0048264; P:determination of ventral identity; IMP:UniProtKB.
DR   GO; GO:0007398; P:ectoderm development; IMP:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0045893; P:positive regulation of 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; 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   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; Differentiation; DNA-binding; Neurogenesis; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..367
FT                   /note="Forkhead box protein I1-B"
FT                   /id="PRO_0000258002"
FT   DNA_BIND        128..222
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        3
FT                   /note="P -> S (in Ref. 2; AAH78036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        33
FT                   /note="L -> F (in Ref. 2; AAH78036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47
FT                   /note="P -> H (in Ref. 2; AAH78036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="H -> Q (in Ref. 2; AAH78036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="G -> D (in Ref. 3; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        214
FT                   /note="N -> RN (in Ref. 3; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   367 AA;  40971 MW;  3C893C5A4F8F6382 CRC64;
     MNPVQQPAQH RSPASLLHLP HPKRAQEAPD MGLYCDNFMF SQQNLHPSQR APNFSIGGEF
     TPPANPYLWL GGPGMNNAPN YSPAPAPYIP SAFSAPQRHF MANSAAFGGA DLGWMSAASQ
     EELLKMVRPP YSYSALIAMA IQNASDKRLT LSQIYQYVAE NFPFYKKSKA GWQNSIRHNL
     SLNDCFKKMP RDENDPGKGN YWTLDSNCEK MFDNGNFRRK RKPKSESNNA KIAKRDEDHL
     NPKGKESPPM ITPSSSPEVL SPTGHSKSPS PPTVTYTPCL TNFIGSMTAV DSATMNRQSP
     LGLLNELSQR NITGLSSFIS GSAVDQSSEH QDNSLFYNRS PYYTNQKQPH FLQQLHPQQP
     PLYQGRY
 
 
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