FOXP2_XENLA
ID FOXP2_XENLA Reviewed; 706 AA.
AC Q4VYS1; Q4VYS0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Forkhead box protein P2;
DE AltName: Full=XlFoxP2;
GN Name=foxp2 {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:CAI96563.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), TISSUE SPECIFICITY, AND
RP 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).
CC -!- FUNCTION: Transcriptional repressor. {ECO:0000250|UniProtKB:P58463}.
CC -!- SUBUNIT: Dimerization is required for DNA-binding.
CC {ECO:0000250|UniProtKB:P58463}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:16609867};
CC IsoId=Q4VYS1-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:16609867};
CC IsoId=Q4VYS1-2; Sequence=VSP_052126, VSP_052127, VSP_052128;
CC -!- TISSUE SPECIFICITY: At stage 15, expressed in the anterior/superior eye
CC field and the caudal branchial arch. At later stages, expression
CC persists in the retina and in the caudal branchial arch. Expressed in
CC the pronephros and the tip of the tail. Beginning with stage 35,
CC expression in the brain is localized to distinct subdomains of the
CC anterior prosencephalon, the medial mesencephalon and to lateral
CC domains of the hindbrain. {ECO:0000269|PubMed:16609867}.
CC -!- DEVELOPMENTAL STAGE: First expressed weakly at mid-gastrula (stage 11)
CC but expression becomes prominent at stage 15.
CC {ECO:0000269|PubMed:16609867}.
CC -!- DOMAIN: The leucine-zipper is required for dimerization and
CC transcriptional repression. {ECO:0000250|UniProtKB:P58463}.
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DR EMBL; AJ971475; CAI96563.1; -; mRNA.
DR EMBL; AJ971476; CAI96564.1; -; mRNA.
DR RefSeq; NP_001089138.1; NM_001095669.1. [Q4VYS1-1]
DR AlphaFoldDB; Q4VYS1; -.
DR SMR; Q4VYS1; -.
DR GeneID; 734154; -.
DR KEGG; xla:734154; -.
DR CTD; 734154; -.
DR Xenbase; XB-GENE-864899; foxp2.L.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 734154; Expressed in zone of skin and 9 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:0021757; P:caudate nucleus development; ISS:UniProtKB.
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 GO; GO:0021758; P:putamen development; 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 Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..706
FT /note="Forkhead box protein P2"
FT /id="PRO_0000247655"
FT ZN_FING 337..362
FT /note="C2H2-type"
FT /evidence="ECO:0000255"
FT DNA_BIND 495..585
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..400
FT /note="Leucine-zipper"
FT REGION 413..417
FT /note="Ctbp1-binding"
FT /evidence="ECO:0000250|UniProtKB:P58463"
FT REGION 672..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..90
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:16609867"
FT /id="VSP_052126"
FT VAR_SEQ 135..154
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:16609867"
FT /id="VSP_052127"
FT VAR_SEQ 659
FT /note="I -> ISFKFLVTPLDKRIIPVPCHSTLRLLQCLQR (in isoform b)"
FT /evidence="ECO:0000303|PubMed:16609867"
FT /id="VSP_052128"
FT CONFLICT 581
FT /note="A -> G (in Ref. 1; CAI96564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 78908 MW; B91CAB0A465B0E36 CRC64;
MMQESATETI SNSSMNQNGM STLSSQLDAG SRDGRSSSDT SSEVSTVELL HLQQQQALQA
ARQLLLQQQT SGLKSPKNNE KQRPLQVPVS MAMMTPQVIT PQQMQQILQQ QVLSPQQLQA
LLQQQQAVML QQQQLQEFYK KQQEQLHLQL LQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQPQPH PGKQAKEQQQ LAAQQLVFQQ QLLQMQQLQQ QQHLLNLQRQ GLISIPPSQS
ALPVQSLPQA GLSPAEIQQL WKEVTGVHSM EDNGIKHGGL DLTTNISSST TSTTTSKASP
PITHHSLLNG QASVLSARRD SSSHEETGAS HTLYGHGVCK WPGCENICED FGQFLKHLNN
EHALDDRSTA QCRVQMQVVQ QLEIQLSKER ERLQAMMTHL HMRPSEPKPS PKPLNLVSTV
TMSKNMLETS PQSLPQTPTT PTAPVTPLAQ GPSVITPASV PNVGAIRRRH SDKYNIPMSS
EIAPNYEFYK NADVRPPFTY ATLIRQAIME SSDRQLTLNE IYSWFTRTFA YFRRNAATWK
NAVRHNLSLH KCFVRVENVK GAVWTVDEAE YQKRRSQKIT ASPTLVKNIP TSLGYGAALN
ASLQAALAES SLPLLSNTGL LNNASTGLLQ AVHEDLNGSL DHIDSNGNSS AGCSPQPHIH
SIHVKEEPLI ADDEDCPMSL VTTANHSPEL EEDRELEEEP LSEDLE
