FOXP4_XENLA
ID FOXP4_XENLA Reviewed; 641 AA.
AC Q4VYR7; Q08AZ6; Q4VYR8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Forkhead box protein P4;
DE AltName: Full=XlFoxP4;
GN Name=foxp4 {ECO:0000303|PubMed:16609867};
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:CAI96566.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Tadpole {ECO:0000269|PubMed:16609867};
RX PubMed=16609867; DOI=10.1007/s00427-006-0073-8;
RA Schoen C., Wochnik A., Roessner A., Donow C., Knoechel W.;
RT "The FoxP subclass in Xenopus laevis development.";
RL Dev. Genes Evol. 216:641-646(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional repressor. {ECO:0000250|UniProtKB:Q9DBY0}.
CC -!- SUBUNIT: Dimerization is required for DNA-binding.
CC {ECO:0000250|UniProtKB:Q9DBY0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: First expressed in the anterior neural field of
CC stage 15 embryos. At stage 18, localized in three domains of the brain
CC (rostral forebrain, midbrain and hindbrain) and in the eye anlage.
CC Cerebral and retinal expression persists at later stages with
CC additional expression in the branchial arches, at the base of the
CC hatching gland, and in the pancreas. {ECO:0000269|PubMed:16609867}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Maternal expression is weak but still detectable at the blastula stage.
CC Zygotic expression starts during gastrulation and progresses to strong
CC expression at stages 30 and 45. {ECO:0000269|PubMed:16609867}.
CC -!- DOMAIN: The leucine-zipper is required for dimerization and
CC transcriptional repression. {ECO:0000250|UniProtKB:Q9DBY0}.
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DR EMBL; AJ971477; CAI96565.1; -; mRNA.
DR EMBL; AJ971478; CAI96566.1; -; mRNA.
DR EMBL; AJ971479; CAI96567.1; -; mRNA.
DR EMBL; BC124940; AAI24941.1; -; mRNA.
DR RefSeq; NP_001089084.1; NM_001095615.1.
DR RefSeq; XP_018103929.1; XM_018248440.1.
DR RefSeq; XP_018103930.1; XM_018248441.1.
DR RefSeq; XP_018103931.1; XM_018248442.1.
DR AlphaFoldDB; Q4VYR7; -.
DR SMR; Q4VYR7; -.
DR PRIDE; Q4VYR7; -.
DR DNASU; 733240; -.
DR GeneID; 733240; -.
DR KEGG; xla:733240; -.
DR CTD; 733240; -.
DR Xenbase; XB-GENE-982697; foxp4.S.
DR OrthoDB; 836427at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 733240; Expressed in lung and 18 other tissues.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative 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; IPR032354; FOXP-CC.
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 Pfam; PF16159; FOXP-CC; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..641
FT /note="Forkhead box protein P4"
FT /id="PRO_0000247654"
FT ZN_FING 278..303
FT /note="C2H2-type"
FT /evidence="ECO:0000255"
FT DNA_BIND 436..526
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..341
FT /note="Leucine-zipper"
FT REGION 354..358
FT /note="ctbp1-binding"
FT /evidence="ECO:0000250|UniProtKB:P58462"
FT REGION 563..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 70
FT /note="C -> G (in Ref. 1; CAI96566 and 2; AAI24941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 71245 MW; 33FD1EC8401793DD CRC64;
MMVESESIRS TPTSQNGVGS LPNQSDSCVG REGSGSGETN GELNPAELLH FQQQQALQMA
RQLLLQQATC LNSPSTDNKQ PSVQVPVSVA MMSPQMITPQ QMQQILSPAQ LQAVLQQQQA
LMLQQLQEYY KKQQEQLHLQ LLSQQQAGKQ QPKELALGNK QLAFQQQLLQ MQQLQQQHLI
NLQRQNLVGL QSGQGPVPMQ SLPQVSPSDL HQLLKEMSSS QEESSKQDTV DLMTSITTSF
PTTKVSPPTM HPSLSNGQNT RRESTSHYES SHLLYGHGEC RWPGCEALCE DMGQFIKHLN
TEHALDDRST AQCRVQMQVV QQLEIQLAKE SERLQAMMTH LHMRPSEPKP FSQPLNLVSS
ASNNKMSHDT FPDGLPQPPT SATAPITPLR QGTSVISSSS LPSVGPVRRR IVDKFCTPIS
SELAQNHEFY KNAEVRPPFT YASLIRQAIL ETPDRQLTLN EIYNWFTRMF AYFRRNTATW
KNAVRHNLSL HKCFVRVENV KGAVWTVDEL EYQKRRPPKM TGSPTLVKNM ISGLGYSALN
ASYQAALAES SFPLLNSPPL HNSSGSVLHG GHDDVTSTGE PGNSNGSSPR LSPQYSQSIH
VKEEPAEDDV RPASISAPTN QTTVLPEDRD LESESPMEDL P
