TBP7_CAEEL
ID TBP7_CAEEL Reviewed; 1291 AA.
AC P54816; A7LPG7; A7LPG8; Q21337; Q3YFF5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Tat-binding homolog 7;
DE AltName: Full=Lin-48 expression abnormal protein 1;
GN Name=lex-1; ORFNames=F11A10.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND MUTAGENESIS OF
RP ALA-548 AND GLY-1001.
RC STRAIN=CM3; TISSUE=Embryo;
RX PubMed=17618463; DOI=10.1007/s00438-007-0265-6;
RA Tseng R.-J., Armstrong K.R., Wang X., Chamberlin H.M.;
RT "The bromodomain protein LEX-1 acts with TAM-1 to modulate gene expression
RT in C. elegans.";
RL Mol. Genet. Genomics 278:507-518(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Thought to form a complex that enhances transcription from
CC repetitive DNA sequences by modulating chromatin structure.
CC {ECO:0000269|PubMed:17618463}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a;
CC IsoId=P54816-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P54816-2; Sequence=VSP_032725;
CC Name=c;
CC IsoId=P54816-3; Sequence=VSP_032726;
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; DQ140399; AAZ73761.1; -; mRNA.
DR EMBL; Z68297; CAA92596.2; -; Genomic_DNA.
DR EMBL; Z68316; CAA92596.2; JOINED; Genomic_DNA.
DR EMBL; Z68297; CAO82028.1; -; Genomic_DNA.
DR EMBL; Z68316; CAO82028.1; JOINED; Genomic_DNA.
DR EMBL; Z68297; CAO82029.1; -; Genomic_DNA.
DR EMBL; Z68316; CAO82029.1; JOINED; Genomic_DNA.
DR PIR; T20739; T20739.
DR RefSeq; NP_001122768.1; NM_001129296.2. [P54816-2]
DR RefSeq; NP_502289.2; NM_069888.6. [P54816-1]
DR AlphaFoldDB; P54816; -.
DR SMR; P54816; -.
DR BioGRID; 43240; 4.
DR STRING; 6239.F11A10.1a; -.
DR iPTMnet; P54816; -.
DR EPD; P54816; -.
DR PaxDb; P54816; -.
DR PeptideAtlas; P54816; -.
DR PRIDE; P54816; -.
DR EnsemblMetazoa; F11A10.1a.1; F11A10.1a.1; WBGene00008682. [P54816-1]
DR EnsemblMetazoa; F11A10.1b.1; F11A10.1b.1; WBGene00008682. [P54816-2]
DR GeneID; 178146; -.
DR KEGG; cel:CELE_F11A10.1; -.
DR UCSC; F11A10.1a; c. elegans. [P54816-1]
DR CTD; 178146; -.
DR WormBase; F11A10.1a; CE40608; WBGene00008682; lex-1. [P54816-1]
DR WormBase; F11A10.1b; CE41384; WBGene00008682; lex-1. [P54816-2]
DR eggNOG; KOG0732; Eukaryota.
DR GeneTree; ENSGT00550000074694; -.
DR InParanoid; P54816; -.
DR OMA; RPKYFGR; -.
DR OrthoDB; 184252at2759; -.
DR PhylomeDB; P54816; -.
DR PRO; PR:P54816; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00008682; Expressed in embryo and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031445; P:regulation of heterochromatin assembly; IMP:UniProtKB.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR045199; ATAD2-like.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23069; PTHR23069; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Bromodomain; Nucleotide-binding;
KW Reference proteome; Transcription.
FT CHAIN 1..1291
FT /note="Tat-binding homolog 7"
FT /id="PRO_0000084770"
FT DOMAIN 882..952
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..254
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..307
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 432..439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 160..161
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_032725"
FT VAR_SEQ 880..928
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_032726"
FT MUTAGEN 548
FT /note="A->V: In gu24; reduced lin-48 expression in hindgut
FT cells."
FT /evidence="ECO:0000269|PubMed:17618463"
FT MUTAGEN 1001
FT /note="G->E: In gu48; reduced lin-48 expression in hindgut
FT cells."
FT /evidence="ECO:0000269|PubMed:17618463"
SQ SEQUENCE 1291 AA; 146421 MW; FA5EC4EF72BA73C3 CRC64;
MPRSDGFSPR KNLRRSARDH SRSYAGQCNE DFDDMYAPSS RRRSSGGVDG NGYTRSGRKI
NHNRYYEEEY HEAISSEEDE RRYRTRRSSN SMTYRQQVMQ AIDESKRNQK VPPAKRKRIY
LSDEEEEDFA EAAHVENTVP ERATRRSTRR RSSMHEELGV SEQEESPVRR TRKAAKRLGS
EQPEENLAAD DPLPMEGGGE IVLPIAEIDG MAEQENEDLI EKIGREEEEE GAEEDEQSGE
KDPEEEEDDS SNAESSEEST APRQYSLRRR QPVVQFNASE ARENRRARLE HHRVANQNRH
HRNRNGSRRR RSDSDSDSDD MVLPRPDKRQ SRPHMHNRGE RERGRFMPIN MTEKELQSAQ
HILMDRMRKT DAGQGASDID PMSVDSSVGF DQVGGLGHHI QSLKEVVLFP MLYPEVFEKF
RINPPKGVVF YGPPGTGKTL VARALANECR RGANKVAFFM RKGADCLSKW VGESERQLRL
LFDQAYAMRP SIIFFDEIDG LAPVRSSKQD QIHASIVSTL LALMDGLDGR GEVVVIGATN
RLDTLDPALR RPGRFDRELR FSLPDLNARR QILDIHTSKW EENKPIPETL DAIAERTSGY
CGADLKFLCT EAVLIGLRSR YPHIYMCSER LKLDVATIKI TSEHFGHAMR RITPASRRDL
TIPSRPLDER TSILLGDTVS NLISLRIPQG YRCVENAMAT ASSELEQVVR ALEPNPTVPA
IRLLLCGSEQ LADGGQTSYV LPAILAKLDH LPVFSLSVSS LLTDGRPEEA FSNAIQSAMR
ASATGPCIML LPSIDEWIKV IPVSVQHMLI TCLESMTGFT PILFLSTLDT SFEDAPEYVT
EIFRHANCIT LNPSRRTIRQ KYFEHVIEKI NTPPKVFDPT VYEMPLPDDD SPDSKPSRKL
NDDETRELLK MYTALQRQMR LFFKERLTRL MRDRRFVEFV EPVDPDEAED YYEIIETPIC
MQDIMEKLNN CEYNHADKFV ADLILIQTNA LEYNPSTTKD GKLIRQMANT LRDAIDDLIE
CELDESFVER IETVSRMLQD AGVTPTSDKL LTEIPKGFAR KKAWSMTNSL AKEIEQWTSE
REAENQKMLS KLGVAAPTLE LVVVPVEDMK SEEGTSTSTD GVPASAGNKK KLLKKKKGQK
KSKTGESEEH DEDSTVEDAG EDTIVENLEI KKNQETPNSE HDIEMKDASK DSTPSVQISI
AEKELIVSKP ATCELIQCCV EKSEGWSVSE LERLSSVLSH TIERFRDEWN RENLPAQLTQ
IVREWQTADD SNNTIVNGTL NKSNGNLANG H
