ID W5MQE3_LEPOC Unreviewed; 440 AA.
AC W5MQE3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=POU domain protein {ECO:0000256|RuleBase:RU361194};
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:ENSLOCP00000010602.1, 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:ENSLOCP00000010602.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-3
CC subfamily. {ECO:0000256|ARBA:ARBA00010250}.
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DR EMBL; AHAT01003424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006639216.1; XM_006639153.2.
DR AlphaFoldDB; W5MQE3; -.
DR STRING; 7918.ENSLOCP00000010602; -.
DR Ensembl; ENSLOCT00000010617.1; ENSLOCP00000010602.1; ENSLOCG00000008712.1.
DR GeneID; 102696283; -.
DR KEGG; loc:102696283; -.
DR CTD; 5455; -.
DR eggNOG; KOG3802; Eukaryota.
DR GeneTree; ENSGT00940000164385; -.
DR HOGENOM; CLU_013065_1_2_1; -.
DR InParanoid; W5MQE3; -.
DR OMA; PPHQGHW; -.
DR OrthoDB; 4250502at2759; -.
DR Proteomes; UP000018468; Linkage group LG17.
DR Bgee; ENSLOCG00000008712; Expressed in brain and 6 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR InterPro; IPR016362; TF_POU_3.
DR PANTHER; PTHR11636; POU DOMAIN; 1.
DR PANTHER; PTHR11636:SF125; POU DOMAIN, CLASS 3, TRANSCRIPTION FACTOR 3; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PIRSF; PIRSF002629; Transcription_factor_POU; 1.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW ProRule:PRU00108};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transcription {ECO:0000256|RuleBase:RU361194}.
FT DOMAIN 240..314
FT /note="POU-specific"
FT /evidence="ECO:0000259|PROSITE:PS51179"
FT DOMAIN 330..390
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DNA_BIND 332..391
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 101..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 47188 MW; 357E395C30083E11 CRC64;
MATAASNPYL PSNSILSSGS IVHSDSGGGG MQPGSAAVTS VSAGYRGDPT AKMVQSDFMQ
GAMAASNGGH MLSHAHQWVT TLPHAAAAAA AAAVAAAEAG SPWSSSPVGM TGSPQQQQDV
KNNSGRDDLH TGTTLHHRPP HLGPHQSHPG AWGGTTASHI PSIAGGQQQQ SLIYSQPGGF
TVNGMLSPPP GSQSLVHPGL VRGDTPELDH GNHHHHHHHQ HQHHQQHHGG VNSHDPHSDE
DTPTSDDLEQ FAKQFKQRRI KLGFTQADVG LALGTLYGNV FSQTTICRFE ALQLSFKNMC
KLKPLLNKWL EEADSSTGSP TSIDKIAAQG RKRKKRTSIE VSVKGALESH FLKCPKPSAQ
EITTLADSLQ LEKEVVRVWF CNRRQKEKRM TPPGVQQTPD DVYSQVGNGH FLVDYLKDAS
QPSDQRVTTT SSFHQVILAH
//