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BET_FOAMV
ID   BET_FOAMV               Reviewed;         482 AA.
AC   P89873; B0LW77; P14354; P90355;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   23-FEB-2022, entry version 70.
DE   RecName: Full=Protein Bet;
GN   Name=bet;
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] (ISOFORM BEL-2).
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] (ISOFORMS BET AND BEL-2).
RA   Fluegel R.M.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH HUMAN APOBEC3C.
RX   PubMed=19074429; DOI=10.1074/jbc.m808853200;
RA   Perkovic M., Schmidt S., Marino D., Russell R.A., Stauch B., Hofmann H.,
RA   Kopietz F., Kloke B.-P., Zielonka J., Stroever H., Hermle J., Lindemann D.,
RA   Pathak V.K., Schneider G., Loechelt M., Cichutek K., Muenk C.;
RT   "Species-specific inhibition of APOBEC3C by the prototype foamy virus
RT   protein bet.";
RL   J. Biol. Chem. 284:5819-5826(2009).
RN   [4]
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   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11884565; DOI=10.1128/jvi.76.7.3388-3394.2002;
RA   Lecellier C.H., Vermeulen W., Bachelerie F., Giron M.L., Saib A.;
RT   "Intra- and intercellular trafficking of the foamy virus auxiliary bet
RT   protein.";
RL   J. Virol. 76:3388-3394(2002).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH HUMAN APOBEC3F AND APOBEC3G.
RX   PubMed=15994766; DOI=10.1128/jvi.79.14.8724-8731.2005;
RA   Russell R.A., Wiegand H.L., Moore M.D., Schaefer A., McClure M.O.,
RA   Cullen B.R.;
RT   "Foamy virus Bet proteins function as novel inhibitors of the APOBEC3
RT   family of innate antiretroviral defense factors.";
RL   J. Virol. 79:8724-8731(2005).
RN   [7]
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: Bet counteracts the innate antiretroviral activity of APOBEC3
CC       family defense factors by inhibiting their incorporation into virions.
CC       May be implicated in the establishment and/or maintenance of viral
CC       persistance. Bet is required for viral replication (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:15994766}.
CC   -!- SUBUNIT: Bet binds to human APOBEC3F and APOBEC3G. Bet interacts with
CC       host APOBEC3C; this interaction does not induce APOBEC3C degradation,
CC       but prevents dimerization and incorporation into virion of the latter.
CC       {ECO:0000269|PubMed:15994766, ECO:0000269|PubMed:19074429}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Bet]: Host cytoplasm
CC       {ECO:0000269|PubMed:11884565}. Host nucleus
CC       {ECO:0000269|PubMed:11884565}. Secreted {ECO:0000269|PubMed:11884565}.
CC       Note=Bet is highly expressed in infected cells, where it localizes to
CC       both cytoplasm and nucleus (PubMed:11884565). Also secreted and
CC       internalized by non-infected surrounding cells (PubMed:11884565).
CC   -!- SUBCELLULAR LOCATION: [Isoform Bel-2]: Host nucleus
CC       {ECO:0000269|PubMed:11884565}.
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=Bet;
CC         IsoId=P89873-1; Sequence=Displayed;
CC       Name=Bel-1; Synonyms=Bel1;
CC         IsoId=P14353-1; Sequence=External;
CC       Name=Bel-2; Synonyms=Bel2;
CC         IsoId=P89873-2; Sequence=VSP_019620;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA29088.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X05591; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; X05592; CAA29088.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U21247; AAB48114.1; -; Genomic_RNA.
DR   EMBL; U21247; AAB48116.1; -; Genomic_RNA.
DR   EMBL; EU381420; ABY84670.1; -; Genomic_DNA.
DR   Proteomes; UP000138352; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Host cytoplasm; Host nucleus; Host-virus interaction;
KW   Reference proteome; Secreted.
FT   CHAIN           1..482
FT                   /note="Protein Bet"
FT                   /id="PRO_0000244972"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..126
FT                   /note="Missing (in isoform Bel-2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_019620"
FT   CONFLICT        105
FT                   /note="D -> A (in Ref. 1; CAA29088)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="P -> S (in Ref. 1; CAA29088)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="Q -> H (in Ref. 1; CAA29088)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="E -> G (in Ref. 3; ABY84670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370
FT                   /note="V -> A (in Ref. 3; ABY84670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        424
FT                   /note="T -> A (in Ref. 3; ABY84670)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   482 AA;  55244 MW;  3655DFC4E4BEB947 CRC64;
     MDSYEKEESV ASTSGIQDLQ TLSELVGPEN AGEGELTIAE EPEENPRRPR RYTKREVKCV
     SYHAYKEIED KHPQHIKLQD WIPTPEEMIA QKVQNQDLGT ILSFDVTCLK SITSLGRNDP
     GDDPSIMSHV LPVVTPWPMS QDHYAPTLFG ILDRYYQGYL KSPATYQTWK FTCQVDPSGK
     RFMETQFWVP PLGQVNIQFY KNYQILTCCQ AVDPFANIFH GTDEEMFDID SGPDVWCSPS
     LCFKVIYEGA MGQKQEQKTW LCRLGHGHRM GACDYRKVDL YAMRQGKENP YGDRGDAALQ
     YAYQVKRGCK AGCLASPVLN YKALQFHRTI MADFTNPRIG EGHLAHGYQA AMEAYGPQRG
     SNEERVWWNV TRNQGKQGGE YYREGGEEPH YPNTPAPHRR TWDERHKVLK LSSFATPSDI
     QRWTTKALPY GWKVVTESGN DYTSRRKIRT LTEMTQDEIR KRWESGYCDP FIDSGSDSDG
     PF
 
 
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