ID FXP1B_DANRE Reviewed; 659 AA.
AC Q2LE08;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Forkhead box protein P1-B;
GN Name=foxp1b; Synonyms=foxp1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=17876603; DOI=10.1007/s00427-007-0177-9;
RA Cheng L., Chong M., Fan W., Guo X., Zhang W., Yang X., Liu F., Gui Y.,
RA Lu D.;
RT "Molecular cloning, characterization, and developmental expression of foxp1
RT in zebrafish.";
RL Dev. Genes Evol. 217:699-707(2007).
CC -!- FUNCTION: Transcriptional repressor. {ECO:0000250|UniProtKB:Q9H334}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H334}.
CC -!- TISSUE SPECIFICITY: Shows complex and dynamic expression during early
CC embryonic development. Prominent in many regions of the developing
CC central nervous system, particularly in midbrain-hindbrain boundary,
CC hindbrain and spinal cord. Strongly expressed in the retina, ear,
CC branchial arches, hatching gland, heart, pronephric duct, gut,
CC proctodeum, pectoral fin and swim bladder.
CC {ECO:0000269|PubMed:17876603}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically with
CC continuous expression from the zygote to the early larva. Expression
CC dramatically decreases at 30 and 50% epiboly stages, then increases
CC from midgastrulaion onwards, being maintained at a high level until the
CC protruding-mouth stage. {ECO:0000269|PubMed:17876603}.
CC -!- DOMAIN: The leucine-zipper is required for dimerization and
CC transcriptional repression. {ECO:0000250|UniProtKB:P58462}.
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DR EMBL; DQ333303; ABC60256.1; -; mRNA.
DR RefSeq; NP_001034726.1; NM_001039637.1.
DR AlphaFoldDB; Q2LE08; -.
DR SMR; Q2LE08; -.
DR STRING; 7955.ENSDARP00000064937; -.
DR PaxDb; 7955-ENSDARP00000109350; -.
DR GeneID; 569047; -.
DR KEGG; dre:569047; -.
DR AGR; ZFIN:ZDB-GENE-041203-1; -.
DR CTD; 569047; -.
DR ZFIN; ZDB-GENE-041203-1; foxp1b.
DR eggNOG; KOG4385; Eukaryota.
DR InParanoid; Q2LE08; -.
DR OrthoDB; 5385885at2759; -.
DR PhylomeDB; Q2LE08; -.
DR PRO; PR:Q2LE08; -.
DR Proteomes; UP000000437; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd20065; FH_FOXP2; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR047412; FH_FOXP1_P2.
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 PANTHER; PTHR45796; FORKHEAD BOX P, ISOFORM C; 1.
DR PANTHER; PTHR45796:SF3; FORKHEAD BOX PROTEIN P1; 1.
DR Pfam; PF00250; Forkhead; 1.
DR Pfam; PF16159; FOXP-CC; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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..659
FT /note="Forkhead box protein P1-B"
FT /id="PRO_0000294521"
FT ZN_FING 289..314
FT /note="C2H2-type"
FT DNA_BIND 448..538
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..352
FT /note="Leucine-zipper"
FT REGION 365..369
FT /note="CTBP1-binding"
FT /evidence="ECO:0000250"
FT REGION 379..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 659 AA; 73845 MW; 7AEA930FCE6E70B0 CRC64;
MMQESGTEAA NGTAHQNGAP PSVEGHREVR SKSTTPSSDI TASDIINFQQ HQALQVARQI
LLQQQQQSSV HKSPKNNDKQ PATQVPVSVA MMTPQVITPQ QMQQILQHQV LSPQQLQLLL
QQQQALMLQQ QLQEFYKKQQ EQLHLQLIQQ QHGSKQQSKE VSAQQLAFQQ QLLQVQQLQQ
QHLLSLQRQG LLSIQPNQTL PLHTLTQGMI PAELQQLWKE VTNSHVKEEN SVTNNGHRGL
DLSSPSPVPL KNHNQHGSTN GQYISHSLKR EGSTLDDHSP HSHPLYGHGV CKWPGCEAVF
EDFQSFLKHL NNEHALDDRS TAQCRVQMQV VQQLELQLAK DKERLQAMMT HLHVKSTEPK
PTPQPLNLVS NVALSKTAPA ASPPLSLPQT PTTPTAPLTP LSQTHSVITP TSLHSVGPIR
RRYSDKYNMP ISPDIVQNKE FYMNAEVRPP FTYASLIRQA ILESPEKQLT LNEIYNWFTR
MFAYFRRNAA TWKNAVRHNL SLHKCFVRVE NVKGAVWTVD ELEFQKRRPQ KISGSPALVK
NIHTTLGYGP ALSAAFQASM AENIPLYTTA SIGSPTLNSL ASVIREEMNG AMDHGNSNGS
DSSPGRSPLP AMHHISVKEE PMDPEEHEGP LSLVTTANHS PDFDHHRDYE DDHGTEDML
//
