FOXI1_XENTR
ID FOXI1_XENTR Reviewed; 363 AA.
AC Q6P2Z3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Forkhead box protein I1;
DE Short=FoxI1;
GN Name=foxi1 {ECO:0000312|EMBL:CAJ81516.1}; ORFNames=TGas064e18.1;
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:CAJ81516.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:CAJ81516.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAJ81516.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud {ECO:0000312|EMBL:AAH64241.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
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DR EMBL; CR761756; CAJ81516.1; -; mRNA.
DR EMBL; BC064241; AAH64241.1; -; mRNA.
DR RefSeq; NP_989265.1; NM_203934.1.
DR AlphaFoldDB; Q6P2Z3; -.
DR SMR; Q6P2Z3; -.
DR STRING; 8364.ENSXETP00000004118; -.
DR PaxDb; Q6P2Z3; -.
DR DNASU; 394878; -.
DR GeneID; 394878; -.
DR KEGG; xtr:394878; -.
DR CTD; 394878; -.
DR Xenbase; XB-GENE-487658; foxi4.2.
DR eggNOG; KOG2294; Eukaryota.
DR HOGENOM; CLU_046860_0_0_1; -.
DR InParanoid; Q6P2Z3; -.
DR OMA; RTPNTSY; -.
DR OrthoDB; 1270467at2759; -.
DR PhylomeDB; Q6P2Z3; -.
DR TreeFam; TF316127; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048264; P:determination of ventral identity; ISS:UniProtKB.
DR GO; GO:0007398; P:ectoderm development; ISS: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 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; 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..363
FT /note="Forkhead box protein I1"
FT /id="PRO_0000258003"
FT DNA_BIND 125..219
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 40236 MW; B48FF16064D64120 CRC64;
MNPVQQPAQQ RSPASSLPHP KRAQEAPDMA LYCDNFMYPQ QSLHPSQRGP NFAIGEYTSP
ANPYLWLGGH GVNNAPNYSP SPAPYMPPSF GAPQRQFLPN SPAFGGTELS WMSAASQEEL
LKMVRPPYSY SALIAMAIQH ASDRRLTLSQ IYQYVAENFP FYKKSKAGWQ NSIRHNLSLN
DCFKKVPRDE NDPGKGNYWT LDPNCEKMFD NGNFRRKRKP KSDANSAKIA KIGEDHLNPK
GKESPPMITP SSPEEPSPTG HSKSPSPPAV TYTPCLTNFI GSMTAVDAAT ANRQGPLGLL
NELSQRNISS LSSFISGSAV DQSAEHPDTS LFYNRSPYYS SFPTTAQKQP QFLQQPPLYQ
GRY