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Database: UniProt
Entry: W5M3V0_LEPOC
LinkDB: W5M3V0_LEPOC
Original site: W5M3V0_LEPOC 
ID   W5M3V0_LEPOC            Unreviewed;       455 AA.
AC   W5M3V0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Fli-1 proto-oncogene, ETS transcription factor {ECO:0000313|Ensembl:ENSLOCP00000003058.1};
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:ENSLOCP00000003058.1, 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:ENSLOCP00000003058.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU004019}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000256|ARBA:ARBA00005562,
CC       ECO:0000256|RuleBase:RU004019}.
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DR   EMBL; AHAT01024125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01024126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5M3V0; -.
DR   STRING; 7918.ENSLOCP00000003058; -.
DR   Ensembl; ENSLOCT00000003064.1; ENSLOCP00000003058.1; ENSLOCG00000002563.1.
DR   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000158261; -.
DR   InParanoid; W5M3V0; -.
DR   OMA; AXSLLAY; -.
DR   Proteomes; UP000018468; Linkage group LG26.
DR   Bgee; ENSLOCG00000002563; Expressed in heart and 13 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd08541; SAM_PNT-FLI-1; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR046328; ETS_fam.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR035573; SAM_PNT-FLI-1.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11849; ETS; 1.
DR   PANTHER; PTHR11849:SF161; FRIEND LEUKEMIA INTEGRATION 1 TRANSCRIPTION FACTOR; 1.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004019};
KW   Nucleus {ECO:0000256|RuleBase:RU004019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          117..203
FT                   /note="PNT"
FT                   /evidence="ECO:0000259|PROSITE:PS51433"
FT   DOMAIN          284..364
FT                   /note="ETS"
FT                   /evidence="ECO:0000259|PROSITE:PS50061"
FT   REGION          204..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  51077 MW;  0E1AB4B5C2C8F053 CRC64;
     LFSSIEMICK VLSDEALSVV SDDQSLFEPP YAAVPLPKPD MTASGTQDYG PPHKINPLTP
     QQDWINRVNV KREYDHLNGS SRESPVDCSV GKCGKLVGGA EATQINYGSY MDEKNGPPPP
     NMTTNERRVI VPADPSLWSQ DHVRQWLEWA IKEYGLLEID TSLFQSTDGK ELCKMSKEDF
     LRLTSVYNAE VLLSHLNYLR ESSSSLSYNT PHTDQSPRLT TKEDPSYDSA RRTGWSNSMH
     SGKGSPAVTQ NVSKTSEQQR PQPDPYQILG PTSSRLANPG SGQIQLWQFL LELLSDSANA
     GCITWEGTNG EFKMTDPDEV ARRWGERKSK PNMNYDKLSR ALRYYYDKNI MTKVHGKRYA
     YKFDFHGIAQ ALQPHPTESS MYKYPSDLAY VPSYHAHQQK VNFVSPHPPS MPVTSSNFFG
     PPSPYWSSPA GGIYPNPSVP RHPNTHVSSH LGSYY
//
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