FOXP1_XENLA
ID FOXP1_XENLA Reviewed; 578 AA.
AC Q5W1J5; Q4VYS2; Q4VYS3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Forkhead box protein P1;
DE AltName: Full=XlFoxP1;
GN Name=foxp1 {ECO:0000312|EMBL:CAH68561.1};
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:CAH68561.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:15744668};
RX PubMed=15744668; DOI=10.1387/ijdb.051977bp;
RA Pohl B.S., Roessner A., Knoechel W.;
RT "The Fox gene family in Xenopus laevis: FoxI2, FoxM1 and FoxP1 in early
RT development.";
RL Int. J. Dev. Biol. 49:53-58(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAI96562.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), ALTERNATIVE SPLICING,
RP INTERACTION WITH CTBP1, 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).
CC -!- FUNCTION: Transcriptional repressor. {ECO:0000250|UniProtKB:P58462}.
CC -!- SUBUNIT: Dimerization is required for DNA-binding (By similarity).
CC Isoform a, but not isoform b, interacts with ctbp1.
CC {ECO:0000250|UniProtKB:P58462, ECO:0000269|PubMed:16609867}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255, ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000269|PubMed:15744668};
CC IsoId=Q5W1J5-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:16609867};
CC IsoId=Q5W1J5-2; Sequence=VSP_052125;
CC Name=c {ECO:0000269|PubMed:16609867};
CC IsoId=Q5W1J5-3; Sequence=VSP_052122, VSP_052123, VSP_052124;
CC -!- TISSUE SPECIFICITY: All isoforms show similar spatial expression.
CC Localized to the animal hemisphere of early cleavage stage embryos. At
CC tailbud stages, expressed in regions of the brain, eye and the
CC splanchnic mesodermal layer of the lateral plate mesoderm surrounding
CC the gut. At stage 35, expressed within the lens of the eye, in distinct
CC regions of the head mesenchyme and in the area anterior to the gut. In
CC the brain the anterior-most expression is restricted to the outer
CC region of the mesencephalon. With ongoing development, additional
CC expression is found in the curling gut. {ECO:0000269|PubMed:15744668,
CC ECO:0000269|PubMed:16609867}.
CC -!- DEVELOPMENTAL STAGE: Isoform a and isoform b are expressed both
CC maternally and zygotically. Maternal expression disappears before
CC gastrulation and zygotic expression begins after stage 20 and continues
CC throughout embryogenesis. In contrast, isoform c is only detected from
CC stage 30. {ECO:0000269|PubMed:15744668, ECO:0000269|PubMed:16609867}.
CC -!- DOMAIN: The leucine-zipper is required for dimerization and
CC transcriptional repression. {ECO:0000250|UniProtKB:P58462}.
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DR EMBL; AJ853463; CAH68561.1; -; mRNA.
DR EMBL; AJ971473; CAI96561.1; -; mRNA.
DR EMBL; AJ971474; CAI96562.1; -; mRNA.
DR RefSeq; NP_001089002.1; NM_001095533.1.
DR RefSeq; NP_001090174.1; NM_001096705.1. [Q5W1J5-3]
DR AlphaFoldDB; Q5W1J5; -.
DR SMR; Q5W1J5; -.
DR GeneID; 496386; -.
DR GeneID; 779033; -.
DR KEGG; xla:496386; -.
DR CTD; 496386; -.
DR CTD; 779033; -.
DR Xenbase; XB-GENE-961750; foxp1.S.
DR OrthoDB; 836427at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 496386; Expressed in stomach 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:0001222; F:transcription corepressor binding; IPI: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 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 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..578
FT /note="Forkhead box protein P1"
FT /id="PRO_0000247651"
FT ZN_FING 208..233
FT /note="C2H2-type"
FT /evidence="ECO:0000255"
FT DNA_BIND 366..456
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 250..271
FT /note="Leucine-zipper"
FT REGION 284..288
FT /note="Ctbp1-binding"
FT /evidence="ECO:0000250|UniProtKB:P58462"
FT REGION 293..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1
FT /note="M -> MMQESGTETKSNDSVIQNGAGPGNHLLECTLRESRSNGETPLEVGAV
FT ELAHLQQQQALQAARQLLINQQPFSGIKANKRNDKHPSLQVPVSVAM (in isoform
FT c)"
FT /evidence="ECO:0000303|PubMed:16609867"
FT /id="VSP_052122"
FT VAR_SEQ 257..263
FT /note="LSKDKER -> VKHSGAS (in isoform c)"
FT /evidence="ECO:0000303|PubMed:16609867"
FT /id="VSP_052123"
FT VAR_SEQ 264..578
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:16609867"
FT /id="VSP_052124"
FT VAR_SEQ 284
FT /note="P -> PQLCTTFGRENGWICYSQQLEEGITGILKG (in isoform b)"
FT /evidence="ECO:0000303|PubMed:16609867"
FT /id="VSP_052125"
FT CONFLICT 564
FT /note="R -> P (in Ref. 2; CAI96561)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="D -> E (in Ref. 2; CAI96561)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="D -> E (in Ref. 2; CAI96561)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 65019 MW; 9EE64499EE99CB43 CRC64;
MMTPQVITPQ QMQQILQQQV LTPQQLQVLL QQQQALMLQQ QLQEFYKKQQ EQLQLQLLQQ
QHAGKQPKEQ QQQQQVATQQ LAFQQQLLQM QQLQQQHLLT LQRQGLLSIQ PGQPTLPLQS
LAQGMIPAEL QQLWKEVTGS HTADDVVCNN HSTLDLSTTC VSSTAQPKTS LLLNSQASTN
GQASVLTLKR ESSSHEEYTH NHPLYGHGVC KWPGCETICE DFPSFLKHLN SEHALDDRST
AQCRVQMQVV QQLELQLSKD KERLQAMMSH LHVKSTEPKA SPQPLNLVSS ATLSKTASEA
SPQSLPHTPT TPTAPLTPIT QGPSVITTTS IHNVGPIRRR YSDKYNIPIS SDFAQNQEFY
KNAEVRPPFT YASLIRQGIL ESPEKQLTLN EIYNWFTRQF AYFRRNAATW KNAVRHNLSL
HKCFVRVENV KGAVWTVDEM EFQKRRPQKI SGSPTLIKNI QTSHAYCSPL SAALQASMAE
NSLPLYTTAS MGNPALNSLA NAIREDLNGV MEHTSSNGSD SSPGRSPMQG MHQVHVKEEP
LDHDDNDGPL SLVTTANHSP DFDRDRDYED DPVNDDME
