Human immunodeficiency virus 1, complete genome.
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; Lentivirus; Primate lentivirus group.
Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin
Appendix 2: Retroviral taxonomy, protein structure, sequences, and genetic maps
(in) Coffin,J.M. (Ed.); RETROVIRUSES: 757; Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, NY, USA (1997)
Submitted (07-AUG-2002) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA
Submitted (15-MAR-1999) NIH, NLM, Rockville Pike, Bethesda, MD 20894, USA
Submitted (12-NOV-1997) NIH, NLM, Rockville Pike, Bethesda, MD 20894, USA
REVIEWED REFSEQ: This record has been curated by NCBI staff. The\nreference sequence was derived from AF033819.\nThe annotation of this sequence was corrected and updated with the\nkind help of Dr. Colombe Chappey (ViroLogic Inc., South San\nFrancisco, CA USA) and Roger Ptak (Southern Research Institute,\nFrederick, MD USA).\nCOMPLETENESS: full length.
repeat; positions of RNA transcription initialization and polyadenylation; Region: R
both 5' and 3' poly A signals are transcribed into RNA, but the 5' one is suppressed
fusion protein consisting of the viral structural proteins and enzymes; cleaved by the viral protease into individual mature proteins; The processing products of the Gag and Gag-Pol polyproteins were annotated with the help of Pettit et al., 2003 and references therein; Pr160
the Glu-Asp-Leu tripeptide (positions 4-6) is a specific inhibitor of the HIV-1 protease. Involved in regulation of the protease-mediated polyprotein processing; alternative p6 protein; p6*
unprocessed Pol polyprotein; includes part of the transframe peptide, protease, reverse transcriptase and integrase domains.
The proteinase domain of Gag-Pol (in the form of homodimer) mediates all the cleavages in the polyprotein. Cleaves itself from the polyprotein late in particle assembly; protease
transcribes single stranded viral RNA genome into double stranded proviral DNA; HIV-1 reverse transcriptase is composed of the p66 subunit (this protein) and the p51 subunit that lacks the RNAse H domain of the larger subunit
HIV-1 reverse transcriptase is composed of the p66 subunit and the p51 subunit (this protein) that lacks the RNAse H domain of the larger subunit
mediates integration of the viral DNA into the infected cell chromosome
The processing products of the Gag and Gag-Pol polyproteins were annotated with the help of Pettit et al., 2003 and references therein
viral structural protein; forms the outer structural shell of HIV-1 virions; involved in the nuclear import of the HIV-1 preintegration complex; p17
viral structural protein; forms the core of HIV-1 virions; p24
Processing of Gag-Pol by the protease domain dimer starts with cleavage between the p2 and nucleocapsid proteins.
viral structural protein; coats the genomic RNA inside the virion core; binds and delivers full-length viral RNAs into assembling HIV-1 virions; p7
important for virus infectivity, protein processing, and genomic RNA dimer stability
important for incorporation of Vpr into assembling HIV-1 virions; helps mediate efficient virus particle release from infected cells
p23; viral infectivity factor; viral accessory protein important for virus replication in vivo
p15; viral protein R; viral accessory protein important for virus replication in vivo; involved in the nuclear import of the HIV-1 preintegration complex; induces G2 cell cycle arrest; influences mutation rates during viral DNA synthesis; An artificial frameshift eliminating the orf-disrupting nucleotide at position 5320 is introduced to obtain the typical HIV-1 Vpr protein sequence. For this particular HIV-1 strain, HXB2, only a short (78 amino acid long) variant of the Vpr sequence can be obtained by translation of nucleotides 5105 through 5341 without the frameshift
p14; transcriptional activator; viral regulatory protein required for virus replication; transactivates the viral LTR promoter through interactions with cellular transcription factors; associated with pathogenic effects of the virus; the length of Tat varies depending on virus strain or clade
p19; regulator of expression of virion proteins; prevents splicing of viral RNA; shuttles unspliced viral RNA to the cytoplasm for expression of viral proteins and incorporation of full length viral genomic RNA into virions
p16; viral protein U; viral accessory protein important for virus replication in vivo; promotes degradation of CD4 and down-regulates cell surface expression of MHC class I proteins; helps mediate efficient virus particle release from infected cells; reported to induce apoptosis by suppressing the nuclear factor kappaB-dependent expression of antiapoptotic factors; may attenuate the level of Env precursor(gp160) biosynthesis; Vpu and gp160 are translated from different reading frames of the same bicistronic mRNA
gp160; envelope glycoprotein; envelope polyprotein; cleaved by cellular proteases into mature proteins gp120 and gp41
Envelope surface glycoprotein gp160, precursor
mediates binding of HIV-1 to CD4 and cellular co-receptors; cooperates with gp41 to mediate fusion of viral membrane with cellular membrane during virus entry into cells; Envelope surface unit; SU
cooperates with gp120 to mediate fusion of viral membrane with cellular membrane during virus entry into cells; Envelope transmembrane glycoprotein gp41; TM
minus-strand-encoded antisense protein of unknown function; region is highly conserved and likely analogous to the HTLV-1 encoded, HBZ, a nuclear basic region leucine zipper (b-ZIP) protein
p27; negative factor; viral accessory protein; important for virus replication in vivo; determinant of HIV-1 pathogenesis; down-regulates cell surface CD4 and MHC class I molecules; enhances virus infectivity through; interactions with multiple cellular signaling proteins; This particular nucleotide sequence has a premature stop codon in place of a well-conserved tryptophan codon at position 8712-8714 that truncates the HIV1 Nef protein sequence to a 123 amino acids-long N-terminal portion (not shown)