BEL1_FOAMV
ID BEL1_FOAMV Reviewed; 300 AA.
AC P14353; P89872;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 02-JUN-2021, entry version 69.
DE RecName: Full=Protein Bel-1;
DE AltName: Full=Transactivator of spumavirus;
DE Short=Tas;
DE AltName: Full=Transcriptional transactivator;
GN Name=bel1; Synonyms=Taf, tas;
OS Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Spumavirus.
OX NCBI_TaxID=11963;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Fluegel R.M.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-149 AND 152-300.
RX PubMed=2820721; DOI=10.1002/j.1460-2075.1987.tb02473.x;
RA Fluegel R.M., Rethwilm A., Maurer B., Darai G.;
RT "Nucleotide sequence analysis of the env gene and its flanking regions of
RT the human spumaretrovirus reveals two novel genes.";
RL EMBO J. 6:2077-2084(1987).
RN [3]
RP ALTERNATIVE SPLICING.
RX PubMed=1846194; DOI=10.1128/jvi.65.2.727-735.1991;
RA Muranyi W., Fluegel R.M.;
RT "Analysis of splicing patterns of human spumaretrovirus by polymerase chain
RT reaction reveals complex RNA structures.";
RL J. Virol. 65:727-735(1991).
RN [4]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 4-TYR-GLU-5; 24-GLU-LEU-25;
RP 47-ARG--PRO-49; 93-CYS--ARG-95; 119-TRP-GLU-120; 145-PRO-MET-146;
RP 169-SER-ALA-170; 191-SER--GLY-193; 197-ARG--ARG-199; 219-ARG--ARG-221;
RP 247-ASN-PRO-248; 266-LEU-PRO-267; 273-MET-GLY-275; 281-GLU-VAL-282 AND
RP 296-GLU-HIS-297.
RX PubMed=8383217; DOI=10.1128/jvi.67.4.1896-1904.1993;
RA He F., Sun J.D., Garrett E.D., Cullen B.R.;
RT "Functional organization of the Bel-1 trans activator of human foamy
RT virus.";
RL J. Virol. 67:1896-1904(1993).
RN [5]
RP FUNCTION.
RX PubMed=8394017; DOI=10.1073/pnas.90.15.7317;
RA Loechelt M., Muranyi W., Fluegel R.M.;
RT "Human foamy virus genome possesses an internal, Bel-1-dependent and
RT functional promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7317-7321(1993).
RN [6]
RP FUNCTION.
RX PubMed=9420252; DOI=10.1128/jvi.72.1.504-511.1998;
RA Kang Y., Blair W.S., Cullen B.R.;
RT "Identification and functional characterization of a high-affinity Bel-1
RT DNA binding site located in the human foamy virus internal promoter.";
RL J. Virol. 72:504-511(1998).
RN [7]
RP FUNCTION, AND INTERACTION WITH MOUSE NFIA; NFIB; NFIC AND HUMAN NFIX.
RX PubMed=12446690; DOI=10.1074/jbc.m208963200;
RA Kido K., Bannert H., Gronostajski R.M., Fluegel R.M.;
RT "Bel1-mediated transactivation of the spumaretroviral internal promoter is
RT repressed by nuclear factor I.";
RL J. Biol. Chem. 278:11836-11842(2003).
RN [8]
RP REVIEW.
RX PubMed=15358259; DOI=10.1016/j.mib.2004.06.009;
RA Delelis O., Lehmann-Che J., Saib A.;
RT "Foamy viruses-a world apart.";
RL Curr. Opin. Microbiol. 7:400-406(2004).
CC -!- FUNCTION: Transcriptional transactivator that activates the viral
CC internal promoter (IP), thereby enhancing its own expression. This
CC transactivation is repressed by nuclear factor I. Also transactivates
CC the long terminal repeat (LTR) promoter, thereby inducing structural
CC gene expression, initiating the late phase of infection. It is
CC therefore a key regulator of viral gene expression. It directly binds
CC to and activates DNA target sites of viral promoters and those of
CC distinct cellular genes. Required for viral replication.
CC {ECO:0000269|PubMed:12446690, ECO:0000269|PubMed:8394017,
CC ECO:0000269|PubMed:9420252}.
CC -!- SUBUNIT: Homodimer or homomultimer. Forms complexes with the host
CC nuclear factors NFIA, NFIB, NFIC or NFIX.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:8383217}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=The first 88 residues are shared by isoform Bet and isoform
CC Bel-1, the last 396 residues are shared by isoform Bet and isoform
CC Bel-2.;
CC Name=Bel-1; Synonyms=Bel1;
CC IsoId=P14353-1; Sequence=Displayed;
CC Name=Bet;
CC IsoId=P89873-1; Sequence=External;
CC Name=Bel-2; Synonyms=Bel2;
CC IsoId=P89873-2; Sequence=External;
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DR EMBL; U21247; AAB48115.1; -; Genomic_RNA.
DR EMBL; X05591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X05592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Proteomes; UP000138352; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR InterPro; IPR004956; Foamy_BEL.
DR Pfam; PF03274; Foamy_BEL; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Host nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..300
FT /note="Protein Bel-1"
FT /id="PRO_0000125509"
FT DNA_BIND 89..200
FT /evidence="ECO:0000255"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..300
FT /note="Transactivation domain"
FT /evidence="ECO:0000255"
FT MOTIF 214..223
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 4..5
FT /note="YE->RS: No loss of activity, nuclear."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 24..25
FT /note="EL->RS: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 47..49
FT /note="RRP->QIS: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 93..95
FT /note="CKR->LDL: Complete loss of activity, predominantly
FT nuclear."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 119..120
FT /note="WE->RS: Complete loss of activity, predominantly
FT nuclear."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 145..146
FT /note="PM->RS: Complete loss of activity, nuclear."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 169..170
FT /note="SA->DL: Complete loss of activity, nuclear."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 191..193
FT /note="SEG->LRS: No loss of activity, nuclear."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 197..199
FT /note="RPR->DLG: Complete loss of activity, nuclear."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 219..221
FT /note="RPR->QIW: Partial loss of activity, diffuse
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 247..248
FT /note="NP->RS: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 266..267
FT /note="LP->RS: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 273..275
FT /note="MSG->KIC: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 281..282
FT /note="EV->RS: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8383217"
FT MUTAGEN 296..297
FT /note="EH->RS: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8383217"
FT CONFLICT 238
FT /note="A -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 33885 MW; A6571D40648B0D81 CRC64;
MDSYEKEESV ASTSGIQDLQ TLSELVGPEN AGEGELTIAE EPEENPRRPR RYTKREVKCV
SYHAYKEIED KHPQHIKLQD WIPTPEEMSK SLCKRLILCG LYSAEKASEI LRMPFTVSWE
QSDTDPDCFI VSYTCIFCDA VIHDPMPIRW DPEVGIWVKY KPLRGIVGSA VFIMHKHQRN
CSLVKPSTSC SEGPKPRPRH DPVLRCDMFE KHHKPRQKRP RRRSIDNESC ASSSDTMANE
PGSLCTNPLW NPGPLLSGLL EESSNLPNLE VHMSGGPFWE EVYGDSILGP PSGSGEHSVL
