LEO1_DANRE
ID LEO1_DANRE Reviewed; 696 AA.
AC Q6NYV9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=RNA polymerase-associated protein LEO1;
GN Name=leo1; ORFNames=zgc:77374;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20178782; DOI=10.1016/j.ydbio.2010.02.020;
RA Nguyen C.T., Langenbacher A., Hsieh M., Chen J.N.;
RT "The PAF1 complex component Leo1 is essential for cardiac and neural crest
RT development in zebrafish.";
RL Dev. Biol. 341:167-175(2010).
RN [4]
RP INTERACTION WITH CTR9.
RX PubMed=21338598; DOI=10.1016/j.ydbio.2011.02.011;
RA Langenbacher A.D., Nguyen C.T., Cavanaugh A.M., Huang J., Lu F., Chen J.N.;
RT "The PAF1 complex differentially regulates cardiomyocyte specification.";
RL Dev. Biol. 353:19-28(2011).
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II. PAF1C associates
CC with RNA polymerase II, is involved in transcriptional elongation and
CC in histone modifications including methylation on histone H3 'Lys-4'
CC (H3K4me3) (By similarity). PAF1C seems to be required for multiple
CC steps in cardiac formation. Involved in heart development and required
CC for differentiation of the atrioventricular boundary. Required for
CC neural crest cell development. {ECO:0000250,
CC ECO:0000269|PubMed:20178782}.
CC -!- SUBUNIT: Component of the PAF1 complex, which at least consists of
CC cdc73, paf1, leo1, ctr9 and rtf1 (By similarity). The PAF1 complex
CC interacts with PHF5A (By similarity). Interacts with ctr9
CC (PubMed:21338598). {ECO:0000250|UniProtKB:Q5XJE5,
CC ECO:0000250|UniProtKB:Q8WVC0, ECO:0000269|PubMed:21338598}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20178782}.
CC -!- SIMILARITY: Belongs to the LEO1 family. {ECO:0000305}.
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DR EMBL; CR848839; CAK11210.1; -; Genomic_DNA.
DR EMBL; BC066443; AAH66443.1; -; mRNA.
DR RefSeq; NP_996950.1; NM_207067.1.
DR AlphaFoldDB; Q6NYV9; -.
DR SMR; Q6NYV9; -.
DR IntAct; Q6NYV9; 1.
DR STRING; 7955.ENSDARP00000072160; -.
DR PaxDb; Q6NYV9; -.
DR PRIDE; Q6NYV9; -.
DR Ensembl; ENSDART00000077694; ENSDARP00000072160; ENSDARG00000055357.
DR GeneID; 404599; -.
DR KEGG; dre:404599; -.
DR CTD; 123169; -.
DR ZFIN; ZDB-GENE-040426-2435; leo1.
DR eggNOG; KOG1181; Eukaryota.
DR eggNOG; KOG2428; Eukaryota.
DR GeneTree; ENSGT00550000074952; -.
DR HOGENOM; CLU_021818_1_0_1; -.
DR InParanoid; Q6NYV9; -.
DR OMA; DNDQRES; -.
DR OrthoDB; 666874at2759; -.
DR PhylomeDB; Q6NYV9; -.
DR TreeFam; TF321961; -.
DR Reactome; R-DRE-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-DRE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DRE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-DRE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR PRO; PR:Q6NYV9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000055357; Expressed in tail bud paraxial mesoderm and 31 other tissues.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:ZFIN.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IBA:GO_Central.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:ZFIN.
DR GO; GO:0021782; P:glial cell development; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0016570; P:histone modification; IEA:InterPro.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:ZFIN.
DR GO; GO:0014032; P:neural crest cell development; IMP:ZFIN.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0021529; P:spinal cord oligodendrocyte cell differentiation; IMP:ZFIN.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0050936; P:xanthophore differentiation; IMP:ZFIN.
DR InterPro; IPR007149; Leo1.
DR PANTHER; PTHR23146; PTHR23146; 1.
DR Pfam; PF04004; Leo1; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..696
FT /note="RNA polymerase-associated protein LEO1"
FT /id="PRO_0000247823"
FT REGION 1..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 511..537
FT /evidence="ECO:0000255"
FT COMPBIAS 12..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..696
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 76442 MW; 26C715AD3A275A2B CRC64;
MADMDELFGS DGDSDNEQRD SGSGSGSDSD HERPRSASNA SGSESAQSDR DHDDDEDEDG
GKPSNKELFG DDSEDEHGSQ HSGSQHSGSR HSGSRHSGSR HSGSRHSGSQ HSGSQSERSG
NQSDATMHSD NEHSMSEAHR GEQDDEDDDD RGHRSDVGSP ASGAGSRRSD RGSGSPGSEA
GSPRSEAGSG HSDPGTPHTD GEGSGKDAHS GDEKWGGDGK SDQSEDEDKQ QNSDDERERS
DEEGERQKSE SIKGSDSEDD FTRKKKKKIA SDSDSDSDAE TQGGKKPAAN DLFGEADDIS
SDSDAEKPLT PGQPLDADDG MEGDQPEEEP APETRIEVEI PKVSTDLGSD LYFVKLPNFL
SVEPRPFDPQ YYEDEFEDEE MLDEEGRTRL KLKVENTIRW RSRRDEEGNE VKESNARIVK
WSDGSMSLHL GNEVFDVYKA PLQGDHNHLF IRQGTGLQGQ AVFKTKLTFR PHSTDSATHR
KMTLSLADRC SKTQKIRILP MAGRDPESQR NEMIKKEEER LRASIRRESQ QRRMREKQHQ
RGLNAGYLEP DRYDEDEEGE ESISLAAIKS KYKGGGGLRE ERARIYSSDS DEGSDEDKAQ
RLMKAKRLDS DEEGENSGKR KAEEDEESAS KKPKKYVISD EEDEDGDGER DGDRERGGDM
DGDGDGDMEG DGDVDRDGDM DGDGEGDGEG DGEEDE
