REV_HV1H3
ID REV_HV1H3 Reviewed; 116 AA.
AC P69718; P04617;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 23-FEB-2022, entry version 81.
DE RecName: Full=Protein Rev {ECO:0000255|HAMAP-Rule:MF_04077};
DE AltName: Full=ART/TRS {ECO:0000255|HAMAP-Rule:MF_04077};
DE AltName: Full=Anti-repression transactivator {ECO:0000255|HAMAP-Rule:MF_04077};
DE AltName: Full=Regulator of expression of viral proteins {ECO:0000255|HAMAP-Rule:MF_04077};
GN Name=rev {ECO:0000255|HAMAP-Rule:MF_04077};
OS Human immunodeficiency virus type 1 group M subtype B (isolate HXB3)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11707;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2988795; DOI=10.1016/s0092-8674(85)80078-7;
RA Crowl R., Ganguly K., Gordon M., Conroy R., Schaber M., Kramer R.,
RA Shaw G.M., Wong-Staal F., Reddy E.P.;
RT "HTLV-III env gene products synthesized in E. coli are recognized by
RT antibodies present in the sera of AIDS patients.";
RL Cell 41:979-986(1985).
RN [2]
RP PHOSPHORYLATION.
RX PubMed=2846891; DOI=10.1128/jvi.62.12.4801-4804.1988;
RA Hauber J., Bouvier M., Malim M.H., Cullen B.R.;
RT "Phosphorylation of the rev gene product of human immunodeficiency virus
RT type 1.";
RL J. Virol. 62:4801-4804(1988).
RN [3]
RP PHOSPHORYLATION AT SER-92 AND SER-99, AND MUTAGENESIS OF SER-92; SER-99;
RP SER-106 AND SER-112.
RX PubMed=2550674; DOI=10.1128/jvi.63.10.4438-4440.1989;
RA Cochrane A.W., Golub E., Volsky D., Ruben S., Rosen C.A.;
RT "Functional significance of phosphorylation to the human immunodeficiency
RT virus Rev protein.";
RL J. Virol. 63:4438-4440(1989).
RN [4]
RP FUNCTION.
RX PubMed=2784194; DOI=10.1038/338254a0;
RA Malim M.H., Hauber J., Le S.-Y., Maizel J.V., Cullen B.R.;
RT "The HIV-1 rev trans-activator acts through a structured target sequence to
RT activate nuclear export of unspliced viral mRNA.";
RL Nature 338:254-257(1989).
RN [5]
RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF
RP 4-ARG-SER-5; 8-SER-ASP-9; ARG-17; 23-TYR--ASN-26; 38-ARG-ARG-39;
RP 41-ARG--ARG-44; 54-SER--SER-56; 61-SER-THR-62; 67-SER-THR-68;
RP 78-LEU-GLU-79; 91-THR-SER-92; 99-SER-PRO-100; 106-SER--ILE-109 AND
RP 112-SER-GLY-113.
RX PubMed=2752419; DOI=10.1016/0092-8674(89)90416-9;
RA Malim M.H., Bohnlein S., Hauber J., Cullen B.R.;
RT "Functional dissection of the HIV-1 Rev trans-activator -- derivation of a
RT trans-dominant repressor of Rev function.";
RL Cell 58:205-214(1989).
RN [6]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=2404140; DOI=10.1128/jvi.64.2.881-885.1990;
RA Cochrane A.W., Perkins A., Rosen C.A.;
RT "Identification of sequences important in the nucleolar localization of
RT human immunodeficiency virus Rev: relevance of nucleolar localization to
RT function.";
RL J. Virol. 64:881-885(1990).
RN [7]
RP SUBUNIT, AND RNA-BINDING.
RX PubMed=2015625; DOI=10.1016/0092-8674(91)90158-u;
RA Malim M.H., Cullen B.R.;
RT "HIV-1 structural gene expression requires the binding of multiple Rev
RT monomers to the viral RRE: implications for HIV-1 latency.";
RL Cell 65:241-248(1991).
RN [8]
RP SUBUNIT, AND RNA-BINDING.
RX PubMed=1715576; DOI=10.1073/pnas.88.17.7734;
RA Zapp M.L., Hope T.J., Parslow T.G., Green M.R.;
RT "Oligomerization and RNA binding domains of the type 1 human
RT immunodeficiency virus Rev protein: a dual function for an arginine-rich
RT binding motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7734-7738(1991).
RN [9]
RP RNA-BINDING.
RX PubMed=1942257; DOI=10.1128/jvi.65.12.7051-7055.1991;
RA Boehnlein E., Berger J., Hauber J.;
RT "Functional mapping of the human immunodeficiency virus type 1 Rev RNA
RT binding domain: new insights into the domain structure of Rev and Rex.";
RL J. Virol. 65:7051-7055(1991).
RN [10]
RP RNA-BINDING.
RX PubMed=1547776; DOI=10.1002/j.1460-2075.1992.tb05152.x;
RA Kjems J., Calnan B.J., Frankel A.D., Sharp P.A.;
RT "Specific binding of a basic peptide from HIV-1 Rev.";
RL EMBO J. 11:1119-1129(1992).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=7958838; DOI=10.1101/gad.8.13.1538;
RA Meyer B.E., Malim M.H.;
RT "The HIV-1 Rev trans-activator shuttles between the nucleus and the
RT cytoplasm.";
RL Genes Dev. 8:1538-1547(1994).
RN [12]
RP NUCLEAR EXPORT SIGNAL.
RX PubMed=7634336; DOI=10.1016/0092-8674(95)90435-2;
RA Wen W., Meinkoth J.L., Tsien R.Y., Taylor S.S.;
RT "Identification of a signal for rapid export of proteins from the
RT nucleus.";
RL Cell 82:463-473(1995).
RN [13]
RP FUNCTION.
RX PubMed=8633082; DOI=10.1073/pnas.93.9.4421;
RA Fridell R.A., Bogerd H.P., Cullen B.R.;
RT "Nuclear export of late HIV-1 mRNAs occurs via a cellular protein export
RT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4421-4424(1996).
RN [14]
RP SUBUNIT.
RX PubMed=10219079; DOI=10.1093/nar/27.10.2080;
RA Brice P.C., Kelley A.C., Butler P.J.G.;
RT "Sensitive in vitro analysis of HIV-1 Rev multimerization.";
RL Nucleic Acids Res. 27:2080-2085(1999).
RN [15]
RP NUCLEAR EXPORT SIGNAL.
RX PubMed=10339570; DOI=10.1073/pnas.96.11.6229;
RA Elfgang C., Rosorius O., Hofer L., Jaksche H., Hauber J., Bevec D.;
RT "Evidence for specific nucleocytoplasmic transport pathways used by
RT leucine-rich nuclear export signals.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6229-6234(1999).
RN [16]
RP NUCLEAR LOCALIZATION SIGNAL, AND INTERACTION WITH HOST KPNB1.
RX PubMed=9891055; DOI=10.1128/mcb.19.2.1210;
RA Truant R., Cullen B.R.;
RT "The arginine-rich domains present in human immunodeficiency virus type 1
RT Tat and Rev function as direct importin beta-dependent nuclear localization
RT signals.";
RL Mol. Cell. Biol. 19:1210-1217(1999).
RN [17]
RP INTERACTION WITH HOST KHDRBS1.
RX PubMed=11932418; DOI=10.1128/jvi.76.9.4526-4535.2002;
RA Li J., Liu Y., Park I.W., He J.J.;
RT "Expression of exogenous Sam68, the 68-kilodalton SRC-associated protein in
RT mitosis, is able to alleviate impaired Rev function in astrocytes.";
RL J. Virol. 76:4526-4535(2002).
RN [18]
RP INTERACTION WITH HOST XPO1, AND SUBUNIT.
RX PubMed=12134013; DOI=10.1128/jvi.76.16.8079-8089.2002;
RA Hakata Y., Yamada M., Mabuchi N., Shida H.;
RT "The carboxy-terminal region of the human immunodeficiency virus type 1
RT protein Rev has multiple roles in mediating CRM1-related Rev functions.";
RL J. Virol. 76:8079-8089(2002).
RN [19]
RP INTERACTION WITH HOST DDX3X.
RX PubMed=15507209; DOI=10.1016/j.cell.2004.09.029;
RA Yedavalli V.S., Neuveut C., Chi Y.-H., Kleiman L., Jeang K.-T.;
RT "Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export
RT function.";
RL Cell 119:381-392(2004).
RN [20]
RP FUNCTION.
RX PubMed=14701878; DOI=10.1101/gad.1149704;
RA Sanchez-Velar N., Udofia E.B., Yu Z., Zapp M.L.;
RT "hRIP, a cellular cofactor for Rev function, promotes release of HIV RNAs
RT from the perinuclear region.";
RL Genes Dev. 18:23-34(2004).
RN [21]
RP INTERACTION WITH HOST KPNB1; TNPO1; RANBP5 AND IPO7.
RX PubMed=16704975; DOI=10.1074/jbc.m602189200;
RA Arnold M., Nath A., Hauber J., Kehlenbach R.H.;
RT "Multiple importins function as nuclear transport receptors for the Rev
RT protein of human immunodeficiency virus type 1.";
RL J. Biol. Chem. 281:20883-20890(2006).
RN [22]
RP REVIEW.
RX PubMed=10328811; DOI=10.1006/abbi.1999.1207;
RA Hope T.J.;
RT "The ins and outs of HIV Rev.";
RL Arch. Biochem. Biophys. 365:186-191(1999).
RN [23]
RP INTERACTION WITH INTEGRASE.
RX PubMed=17403681; DOI=10.1074/jbc.m609864200;
RA Rosenbluh J., Hayouka Z., Loya S., Levin A., Armon-Omer A., Britan E.,
RA Hizi A., Kotler M., Friedler A., Loyter A.;
RT "Interaction between HIV-1 Rev and integrase proteins: a basis for the
RT development of anti-HIV peptides.";
RL J. Biol. Chem. 282:15743-15753(2007).
RN [24]
RP INTERACTION WITH HOST DDX24.
RX PubMed=18289627; DOI=10.1016/j.virol.2008.01.025;
RA Ma J., Rong L., Zhou Y., Roy B.B., Lu J., Abrahamyan L., Mouland A.J.,
RA Pan Q., Liang C.;
RT "The requirement of the DEAD-box protein DDX24 for the packaging of human
RT immunodeficiency virus type 1 RNA.";
RL Virology 375:253-264(2008).
RN [25]
RP INTERACTION WITH HOST PSIP1.
RX PubMed=19855849; DOI=10.2119/molmed.2009.00133;
RA Levin A., Rosenbluh J., Hayouka Z., Friedler A., Loyter A.;
RT "Integration of HIV-1 DNA is regulated by interplay between viral rev and
RT cellular LEDGF/p75 proteins.";
RL Mol. Med. 16:34-44(2010).
RN [26]
RP INTERACTION WITH HOST NAP1.
RX PubMed=19339032; DOI=10.1016/j.virol.2009.03.005;
RA Cochrane A., Murley L.L., Gao M., Wong R., Clayton K., Brufatto N.,
RA Canadien V., Mamelak D., Chen T., Richards D., Zeghouf M., Greenblatt J.,
RA Burks C., Frappier L.;
RT "Stable complex formation between HIV Rev and the nucleosome assembly
RT protein, NAP1, affects Rev function.";
RL Virology 388:103-111(2009).
CC -!- FUNCTION: Escorts unspliced or incompletely spliced viral pre-mRNAs
CC (late transcripts) out of the nucleus of infected cells. These pre-
CC mRNAs carry a recognition sequence called Rev responsive element (RRE)
CC located in the env gene, that is not present in fully spliced viral
CC mRNAs (early transcripts). This function is essential since most viral
CC proteins are translated from unspliced or partially spliced pre-mRNAs
CC which cannot exit the nucleus by the pathway used by fully processed
CC cellular mRNAs. Rev itself is translated from a fully spliced mRNA that
CC readily exits the nucleus. Rev's nuclear localization signal (NLS)
CC binds directly to KPNB1/Importin beta-1 without previous binding to
CC KPNA1/Importin alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran-
CC GDP) and targets Rev to the nucleus. In the nucleus, the conversion
CC from Ran-GDP to Ran-GTP dissociates Rev from KPNB1 and allows Rev's
CC binding to the RRE in viral pre-mRNAs. Rev multimerization on the RRE
CC via cooperative assembly exposes its nuclear export signal (NES) to the
CC surface. Rev can then form a complex with XPO1/CRM1 and Ran-GTP,
CC leading to nuclear export of the complex. Conversion from Ran-GTP to
CC Ran-GDP mediates dissociation of the Rev/RRE/XPO1/RAN complex, so that
CC Rev can return to the nucleus for a subsequent round of export. Beside
CC KPNB1, also seems to interact with TNPO1/Transportin-1, RANBP5/IPO5 and
CC IPO7/RANBP7 for nuclear import. The nucleoporin-like HRB/RIP is an
CC essential cofactor that probably indirectly interacts with Rev to
CC release HIV RNAs from the perinuclear region to the cytoplasm.
CC {ECO:0000255|HAMAP-Rule:MF_04077, ECO:0000269|PubMed:14701878,
CC ECO:0000269|PubMed:2784194, ECO:0000269|PubMed:8633082}.
CC -!- SUBUNIT: Homomultimer; when bound to the RRE. Multimeric assembly is
CC essential for activity and may involve XPO1. Binds to human KPNB1,
CC XPO1, TNPO1, RANBP5 and IPO7. Interacts with the viral Integrase.
CC Interacts with human KHDRBS1. Interacts with human NAP1; this
CC interaction decreases Rev multimerization and stimulates its activity.
CC Interacts with human DEAD-box helicases DDX3 and DDX24; these
CC interactions may serve for viral RNA export to the cytoplasm and
CC packaging, respectively. Interacts with human PSIP1; this interaction
CC may inhibit HIV-1 DNA integration by promoting dissociation of the
CC Integrase-LEDGF/p75 complex. {ECO:0000255|HAMAP-Rule:MF_04077,
CC ECO:0000269|PubMed:10219079, ECO:0000269|PubMed:11932418,
CC ECO:0000269|PubMed:12134013, ECO:0000269|PubMed:15507209,
CC ECO:0000269|PubMed:16704975, ECO:0000269|PubMed:1715576,
CC ECO:0000269|PubMed:17403681, ECO:0000269|PubMed:18289627,
CC ECO:0000269|PubMed:19339032, ECO:0000269|PubMed:19855849,
CC ECO:0000269|PubMed:2015625, ECO:0000269|PubMed:9891055}.
CC -!- INTERACTION:
CC P69718; P04585: gag-pol; Xeno; NbExp=8; IntAct=EBI-8540156, EBI-3989067;
CC -!- SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_04077}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04077}.
CC Note=The presence of both nuclear import and nuclear export signals
CC leads to continuous shuttling between the nucleus and cytoplasm.
CC {ECO:0000255|HAMAP-Rule:MF_04077}.
CC -!- DOMAIN: The RNA-binding motif binds to the RRE, a 240 bp stem-and-loop
CC structure present in incompletely spliced viral pre-mRNAs. This region
CC also contains the NLS which mediates nuclear localization via KPNB1
CC binding and, when the N-terminal sequence is present, nucleolar
CC targeting. These overlapping functions prevent Rev bound to RRE from
CC undesirable return to the nucleus. When Rev binds the RRE, the NLS
CC becomes masked while the NES remains accessible. The leucine-rich NES
CC mediates binding to human XPO1. {ECO:0000255|HAMAP-Rule:MF_04077}.
CC -!- PTM: Asymmetrically arginine dimethylated at one site by host PRMT6.
CC Methylation impairs the RNA-binding activity and export of viral RNA
CC from the nucleus to the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04077}.
CC -!- PTM: Phosphorylated by protein kinase CK2. Presence of, and maybe
CC binding to the N-terminus of the regulatory beta subunit of CK2 is
CC necessary for CK2-mediated Rev's phosphorylation. {ECO:0000255|HAMAP-
CC Rule:MF_04077}.
CC -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for
CC Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
CC majority of strains found worldwide belong to the group M. Group O
CC seems to be endemic to and largely confined to Cameroon and neighboring
CC countries in West Central Africa, where these viruses represent a small
CC minority of HIV-1 strains. The group N is represented by a limited
CC number of isolates from Cameroonian persons. The group M is further
CC subdivided in 9 clades or subtypes (A to D, F to H, J and K).
CC {ECO:0000255|HAMAP-Rule:MF_04077}.
CC -!- SIMILARITY: Belongs to the HIV-1 REV protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04077}.
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DR EMBL; M14100; AAA44677.1; -; Genomic_RNA.
DR PIR; S33983; S33983.
DR PDB; 3LPH; X-ray; 2.50 A; A/B/C/D=1-70.
DR PDB; 4PMI; X-ray; 3.20 A; B/C=1-70.
DR PDBsum; 3LPH; -.
DR PDBsum; 4PMI; -.
DR SMR; P69718; -.
DR DIP; DIP-61764N; -.
DR IntAct; P69718; 2.
DR MINT; P69718; -.
DR iPTMnet; P69718; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016032; P:viral process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04077; REV_HIV1; 1.
DR InterPro; IPR000625; REV_protein.
DR Pfam; PF00424; REV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; AIDS; Host cytoplasm; Host nucleus; Host-virus interaction;
KW Methylation; mRNA transport; Phosphoprotein; RNA-binding; Transport.
FT CHAIN 1..116
FT /note="Protein Rev"
FT /id="PRO_0000085262"
FT REGION 18..26
FT /note="Homomultimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04077"
FT REGION 23..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 34..50
FT /note="Nuclear localization signal and RNA-binding (RRE)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04077,
FT ECO:0000269|PubMed:2404140, ECO:0000269|PubMed:2752419,
FT ECO:0000269|PubMed:9891055"
FT MOTIF 73..84
FT /note="Nuclear export signal and binding to XPO1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04077"
FT MOD_RES 5
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04077"
FT MOD_RES 8
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04077"
FT MOD_RES 92
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04077,
FT ECO:0000269|PubMed:2550674"
FT MOD_RES 99
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04077,
FT ECO:0000269|PubMed:2550674"
FT MUTAGEN 4..5
FT /note="RS->DL: Partial loss of expression of unspliced
FT viral transcripts. No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 8..9
FT /note="SD->DL: No effect on expression of unspliced viral
FT transcripts. Decreased phosphorylation. No effect on
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 17
FT /note="R->D: No effect on expression of unspliced viral
FT transcripts. No effect on phosphorylation. Expressed in
FT nucleus and slightly in cytoplasm."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 23..26
FT /note="YQSN->DQDL: Complete loss of expression of unspliced
FT viral transcripts. No effect on phosphorylation. Expressed
FT in nucleus and slightly in cytoplasm."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 38..39
FT /note="RR->DL: Complete loss of expression of unspliced
FT viral transcripts. Decreased phosphorylation. Expressed in
FT cytoplasm and slightly in nucleus."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 41..44
FT /note="RRRR->DL: Complete loss of expression of unspliced
FT viral transcripts. Complete loss of phosphorylation.
FT Expressed in cytoplasm and slightly in nucleus."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 54..56
FT /note="SIS->I: Complete loss of expression of unspliced
FT viral transcripts. No effect on phosphorylation. Expressed
FT in nucleus and slightly in cytoplasm."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 61..62
FT /note="ST->DL: No effect on expression of unspliced viral
FT transcripts. No effect on phosphorylation. Expressed in
FT nucleus and slightly in cytoplasm."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 67..68
FT /note="SA->DL: No effect on expression of unspliced viral
FT transcripts. No effect on phosphorylation. No effect on
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 78..79
FT /note="LE->DL: Complete loss of expression of unspliced
FT viral transcripts. No effect on phosphorylation. No effect
FT on subcellular location."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 91..92
FT /note="TS->DL: No effect on expression of unspliced viral
FT transcripts. No effect on phosphorylation. No effect on
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 92
FT /note="S->R: Decreased phosphorylation."
FT /evidence="ECO:0000269|PubMed:2550674"
FT MUTAGEN 99..100
FT /note="SP->DL: No effect on expression of unspliced viral
FT transcripts. Decreased phosphorylation. No effect on
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 99
FT /note="S->I: Decreased phosphorylation."
FT /evidence="ECO:0000269|PubMed:2550674"
FT MUTAGEN 106..109
FT /note="SPTI->DLTV: No effect on expression of unspliced
FT viral transcripts. No effect on phosphorylation. No effect
FT on subcellular location."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 106
FT /note="S->F: Almost no effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:2550674"
FT MUTAGEN 112..113
FT /note="SG->DL: No effect on expression of unspliced viral
FT transcripts. No effect on phosphorylation. No effect on
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:2752419"
FT MUTAGEN 112
FT /note="S->L: Almost no effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:2550674"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:3LPH"
FT HELIX 35..63
FT /evidence="ECO:0007829|PDB:3LPH"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:3LPH"
SQ SEQUENCE 116 AA; 13051 MW; F3DA2E7AF302FBDF CRC64;
MAGRSGDSDE DLLKAVRLIK FLYQSNPPPN PEGTRQARRN RRRRWRERQR QIHSISERIL
STYLGRSAEP VPLQLPPLER LTLDCNEDCG TSGTQGVGSP QILVESPTIL ESGAKE
