ID W5MV53_LEPOC Unreviewed; 678 AA.
AC W5MV53;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Forkhead box P1 {ECO:0000313|Ensembl:ENSLOCP00000012262.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012262.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000012262.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR EMBL; AHAT01020688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MV53; -.
DR STRING; 7918.ENSLOCP00000012262; -.
DR Ensembl; ENSLOCT00000012283.1; ENSLOCP00000012262.1; ENSLOCG00000010009.1.
DR eggNOG; KOG4385; Eukaryota.
DR GeneTree; ENSGT00940000165920; -.
DR InParanoid; W5MV53; -.
DR OMA; HEEHSHN; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000010009; Expressed in larva and 13 other cell types or tissues.
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: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.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00089}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 466..539
FT /note="Fork-head"
FT /evidence="ECO:0000259|PROSITE:PS50039"
FT DNA_BIND 466..539
FT /note="Fork-head"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
FT REGION 244..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 76184 MW; A00FF508E262C7FA CRC64;
QCSSTFSFQN VLQPHSTSCL FKYLHILETP TSLKQPDHSF SATTELSRSL VKSFVMKLYD
LGALQVARQI LLHQQHQQSS GLKSPKSNEK QTGLQIPVSV AMMTPQVITP QQMQQILQQQ
VLTPQQLQVL LQQQQALMLQ QQQLQEFYKK QQEQLHLQLL QQQHAGKQSK EQQQAAAQQL
AFQQQLLQVQ QLQQQHLLNL QRQGLLTIQP GQPALPLQPL TQGMIPADLQ QLWKEVTGTH
VKDENTANSH GSLDLSTSAI TSPAPPKNTL INQHASTNGQ PMGHTPKRES SLLEEPHHHS
HPLYGHGVCK WPGCEAVFED FQSFLKHLNH EHALDDRSTA QCRVQMQVVQ QLELQLAKDK
ERLQAMMTHL HVKSTEPKPT PQPLNLVSNV TLSKTASETS PQSLPQTPTT PTAPLTPISQ
GPSVITQNNL HSVGPIRRRY SEKYNMPISP ADIVQNKEFY MNAEVRPPFT YASLIRQAIL
ESPEKQLTLN EIYNWFTRMF AYFRRNAATW KNAVRHNLSL HKCFVRVENV KGAVWTVDEL
EFQKRRPQKI SGSPALVKNL QTSLSYGTSL TAAFQASMAE NNIPLYTTAS IGSPTLNSLA
NVIREEVNGA MEHANSNGSD SSPGRSPLQA MHHINVKEEP LDPEDHEGPL SLVTTANHSP
DFDHDRDYDD DPGNDDMQ
//
