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P12451

- POL_HV2SB

UniProt

P12451 - POL_HV2SB

Protein

Gag-Pol polyprotein

Gene

gag-pol

Organism
Human immunodeficiency virus type 2 subtype A (isolate SBLISY) (HIV-2)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation By similarity.By similarity
    Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to play a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. The myristoylation signal and the NLS exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu By similarity.By similarity
    Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV to the human species By similarity.By similarity
    Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity By similarity.By similarity
    The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell.PROSITE-ProRule annotation
    Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H can probably proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends By similarity.By similarity
    Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration By similarity.By similarity

    Catalytic activityi

    Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
    3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation
    Endopeptidase for which the P1 residue is preferably hydrophobic.PROSITE-ProRule annotation

    Cofactori

    Binds 2 magnesium ions for reverse transcriptase polymerase activity.By similarity
    Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is a precondition for magnesium binding By similarity.By similarity
    Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei135 – 1362Cleavage; by viral proteaseBy similarity
    Sitei222 – 2232Cis/trans isomerization of proline peptide bond; by human PPIA/CYPABy similarity
    Sitei364 – 3652Cleavage; by viral proteaseBy similarity
    Sitei381 – 3822Cleavage; by viral proteaseBy similarity
    Sitei430 – 4312Cleavage; by viral proteaseSequence Analysis
    Sitei444 – 4452Cleavage; by viral proteaseBy similarity
    Sitei511 – 5122Cleavage; by viral proteaseBy similarity
    Active sitei536 – 5361For protease activity; shared with dimeric partnerPROSITE-ProRule annotation
    Sitei610 – 6112Cleavage; by viral proteaseBy similarity
    Metal bindingi720 – 7201Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi795 – 7951Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi796 – 7961Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Sitei1010 – 10101Essential for RT p66/p51 heterodimerizationBy similarity
    Sitei1023 – 10231Essential for RT p66/p51 heterodimerizationBy similarity
    Sitei1049 – 10502Cleavage; by viral protease; partialBy similarity
    Metal bindingi1052 – 10521Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi1087 – 10871Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi1107 – 11071Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi1158 – 11581Magnesium; catalytic; for RNase H activityBy similarity
    Sitei1169 – 11702Cleavage; by viral proteaseBy similarity
    Metal bindingi1233 – 12331Magnesium; catalytic; for integrase activityBy similarity
    Metal bindingi1285 – 12851Magnesium; catalytic; for integrase activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri388 – 40518CCHC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri409 – 42618CCHC-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1172 – 121342Integrase-typePROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi1392 – 143948Integrase-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. DNA-directed DNA polymerase activity Source: UniProtKB-KW
    4. exoribonuclease H activity Source: UniProtKB-EC
    5. RNA binding Source: UniProtKB-KW
    6. RNA-directed DNA polymerase activity Source: UniProtKB-KW
    7. RNA-DNA hybrid ribonuclease activity Source: InterPro
    8. structural molecule activity Source: InterPro
    9. zinc ion binding Source: InterPro

    GO - Biological processi

    1. DNA integration Source: UniProtKB-KW
    2. DNA recombination Source: UniProtKB-KW
    3. establishment of integrated proviral latency Source: UniProtKB-KW
    4. suppression by virus of host gene expression Source: UniProtKB-KW
    5. viral entry into host cell Source: UniProtKB-KW
    6. viral penetration into host nucleus Source: UniProtKB-KW
    7. viral release from host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

    Keywords - Biological processi

    DNA integration, DNA recombination, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Viral genome integration, Viral penetration into host nucleus, Virion maturation, Virus entry into host cell, Virus exit from host cell

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, RNA-binding, Viral nucleoprotein, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gag-Pol polyprotein
    Alternative name(s):
    Pr160Gag-Pol
    Cleaved into the following 11 chains:
    Matrix protein p17
    Short name:
    MA
    Capsid protein p24
    Short name:
    CA
    Transframe peptide
    Short name:
    TF
    p6-pol
    Short name:
    p6*
    Alternative name(s):
    PR
    Retropepsin
    Alternative name(s):
    Exoribonuclease H (EC:3.1.13.2)
    p66 RT
    Integrase
    Short name:
    IN
    Gene namesi
    Name:gag-pol
    OrganismiHuman immunodeficiency virus type 2 subtype A (isolate SBLISY) (HIV-2)
    Taxonomic identifieri11718 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007427: Genome

    Subcellular locationi

    Chain Matrix protein p17 : Virion Curated. Host nucleus By similarity. Host cytoplasm By similarity. Host cell membrane Curated; Lipid-anchor Curated
    Note: Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localization of the viral genome. During virus production, the nuclear export activity of the matrix protein counteracts the NLS to maintain the Gag and Gag-Pol polyproteins in the cytoplasm, thereby directing unspliced RNA to the plasma membrane By similarity.By similarity
    Chain Integrase : Virion Curated. Host nucleus Curated. Host cytoplasm Curated
    Note: Nuclear at initial phase, cytoplasmic at assembly.Curated

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell
    2. host cell nucleus Source: UniProtKB-SubCell
    3. host cell plasma membrane Source: UniProtKB-SubCell
    4. intracellular Source: GOC
    5. membrane Source: UniProtKB-KW
    6. viral nucleocapsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, Host nucleus, Membrane, Virion

    Pathology & Biotechi

    Keywords - Diseasei

    AIDS

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 14621461Gag-Pol polyproteinPRO_0000261299Add
    BLAST
    Chaini2 – 135134Matrix protein p17By similarityPRO_0000042515Add
    BLAST
    Chaini136 – 364229Capsid protein p24By similarityPRO_0000042516Add
    BLAST
    Peptidei365 – 38117Spacer peptide p2By similarityPRO_0000042517Add
    BLAST
    Chaini382 – 43049Nucleocapsid protein p7By similarityPRO_0000042519Add
    BLAST
    Peptidei431 – 44414Transframe peptideSequence AnalysisPRO_0000246748Add
    BLAST
    Chaini445 – 51167p6-polSequence AnalysisPRO_0000042521Add
    BLAST
    Chaini512 – 61099ProteaseBy similarityPRO_0000038672Add
    BLAST
    Chaini611 – 1169559Reverse transcriptase/ribonuclease HBy similarityPRO_0000042522Add
    BLAST
    Chaini611 – 1049439p51 RTBy similarityPRO_0000042523Add
    BLAST
    Chaini1050 – 1169120p15By similarityPRO_0000042524Add
    BLAST
    Chaini1170 – 1462293IntegraseBy similarityPRO_0000042525Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit.PROSITE-ProRule annotation

    Keywords - PTMi

    Lipoprotein, Myristate

    Interactioni

    Subunit structurei

    Matrix protein p17 is a trimer. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a heterodimer of p66 RT and p51 RT (RT p66/p51). Heterodimerization of RT is essential for DNA polymerase activity. Despite the sequence identities, p66 RT and p51 RT have distinct folding. The integrase is a homodimer and possibly a homotetramer By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP12451.
    SMRiP12451. Positions 2-135, 145-380, 384-429, 512-610, 613-1165, 1170-1215, 1224-1381, 1385-1439.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini531 – 60070Peptidase A2PROSITE-ProRule annotationAdd
    BLAST
    Domaini654 – 844191Reverse transcriptasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1043 – 1166124RNase HPROSITE-ProRule annotationAdd
    BLAST
    Domaini1222 – 1373152Integrase catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni837 – 8459RT 'primer grip'By similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi16 – 227Nuclear export signalBy similarity
    Motifi26 – 327Nuclear localization signalBy similarity
    Motifi1007 – 102317Tryptophan repeat motifBy similarityAdd
    BLAST

    Domaini

    The p66 RT is structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RNase H domain stabilizes the association of RT with primer-template By similarity.By similarity
    The tryptophan repeat motif is involved in RT p66/p51 dimerization.By similarity

    Sequence similaritiesi

    Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
    Contains 1 integrase-type DNA-binding domain.PROSITE-ProRule annotation
    Contains 1 integrase-type zinc finger.PROSITE-ProRule annotation
    Contains 1 peptidase A2 domain.PROSITE-ProRule annotation
    Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation
    Contains 1 RNase H domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri388 – 40518CCHC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri409 – 42618CCHC-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1172 – 121342Integrase-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Family and domain databases

    Gene3Di1.10.10.200. 1 hit.
    1.10.1200.30. 1 hit.
    1.10.150.90. 1 hit.
    1.10.375.10. 1 hit.
    2.30.30.10. 1 hit.
    2.40.70.10. 1 hit.
    3.30.420.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProiIPR001969. Aspartic_peptidase_AS.
    IPR000721. Gag_p24.
    IPR001037. Integrase_C_retrovir.
    IPR001584. Integrase_cat-core.
    IPR017856. Integrase_Zn-bd_dom-like_N.
    IPR003308. Integrase_Zn-bd_dom_N.
    IPR000071. Lentvrl_matrix_N.
    IPR012344. Matrix_N_HIV/RSV.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR008916. Retrov_capsid_C.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR010659. RVT_connect.
    IPR010661. RVT_thumb.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF00540. Gag_p17. 1 hit.
    PF00607. Gag_p24. 1 hit.
    PF00552. IN_DBD_C. 1 hit.
    PF02022. Integrase_Zn. 1 hit.
    PF00075. RNase_H. 1 hit.
    PF00665. rve. 1 hit.
    PF00077. RVP. 1 hit.
    PF00078. RVT_1. 1 hit.
    PF06815. RVT_connect. 1 hit.
    PF06817. RVT_thumb. 1 hit.
    PF00098. zf-CCHC. 2 hits.
    [Graphical view]
    PRINTSiPR00234. HIV1MATRIX.
    SMARTiSM00343. ZnF_C2HC. 2 hits.
    [Graphical view]
    SUPFAMiSSF46919. SSF46919. 1 hit.
    SSF47353. SSF47353. 1 hit.
    SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF50122. SSF50122. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF53098. SSF53098. 2 hits.
    SSF57756. SSF57756. 1 hit.
    PROSITEiPS50175. ASP_PROT_RETROV. 1 hit.
    PS00141. ASP_PROTEASE. 1 hit.
    PS50994. INTEGRASE. 1 hit.
    PS51027. INTEGRASE_DBD. 1 hit.
    PS50879. RNASE_H. 1 hit.
    PS50878. RT_POL. 1 hit.
    PS50158. ZF_CCHC. 2 hits.
    PS50876. ZF_INTEGRASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

    Note: Translation results in the formation of the Gag polyprotein most of the time. Ribosomal frameshifting at the gag-pol genes boundary occurs at low frequency and produces the Gag-Pol polyprotein. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. Maintenance of a correct Gag to Gag-Pol ratio is essential for RNA dimerization and viral infectivity.

    Isoform Gag-Pol polyprotein (identifier: P12451-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGAKNSVLRG KKADELEKIR LRPGGKKKYR LKHIVWAANE LDRFGLTESL     50
    LESKEGCQKI ISVLEPLVPT GSENLKSLYN TTCVIWCLHA EEKVKDTEEA 100
    KRIVGRHLVA ETETAEKMPN ISRPTAPPSG KGGNFPVQQI GGNYVHLPLS 150
    PRTLNAWVKL VEEKKFGAEV VPGFQALSEG CTPYDINQML NCVGDHQAAM 200
    QIIREIINEE AADWDVQHPI PGPLPAGQLR DPRGSDIAGT TSTVEEQIEW 250
    MYRQENPVPV GNIYRRWIQI GLQKCVRMYN PTNILDIKQG PKESFQSYVD 300
    RFYKSLRAEQ TDAAVKNWMT QTLLVQSNPD CKLVLKGLGM NPTLEEMLTA 350
    CQGIGGPGQK ARLMAEALKE AMRPAPIPFA AAQQKRAIKC WNCGKEGHSA 400
    RQCRAPRRQG CWKCGKSGHI MANCPDRQAG FLRAWTMGKE APQLPRGPKF 450
    AGANTNSTPN GSSSGPTGEV HAAREKTERA ETKTIQRSDR GLAASRARRD 500
    TTQRDDRGLA APQFSLWKRP VVTAYIEDQP VEVLLDTGAD DSIVAGIELG 550
    SNYSPKIVGG IGGFINTKEY KDVEIRVLNK KVRATIMTGD TPINIFGRNI 600
    LTALGMSLNL PVAKIEPVKV TLKPGKDGPK QRQWPLTREK IEALREICEK 650
    MEREGQLEEA PPTNPYNTPT FAIKKKDKNK WRMLIDFREL NKVTQDFTEV 700
    QLGIPHPAGL AKKRRITVLD VGDAYFSIPL YEDFRQYTAF TLPSVNNAEP 750
    GKRYIYKVLP QGWKGSPAIF QYTMRQVLEP FRKANPDVII VQYMDDILIA 800
    SDRTDLEHDK VVLQLKELLN GLGFSTPDEK FQKDPPYQWM GYELWPTKWK 850
    LQKIQLPQKE VWTVNDIQKL VGVLNWAAQI YPGIKTKHLC KLIRGKMTPT 900
    EEVQWTELAE AELEENKIIL SQEQEGHYYQ EEKELEATVQ KDQDNQWTYK 950
    VHQGEKILKV GKYAKIKNTH TNGVRLLAQV VQKIGKEALV IWGRIPKFHL 1000
    PVERETWEQW WDNYWQVTWI PDWDFVSTPP LVRLAFNLVK DPIPGAETFY 1050
    TDGSCNRQSK EGKAGYITDR GKDKVRILEQ TTNQQAELEA FAMAVTDSGP 1100
    KVNIVVDSQY VMGIVTGQPA ESESRIVNKI IEEMIKKEAI YVAWVPAHKG 1150
    IGGNQEIDHL VSQGIRQVLF LERIEPAQEE HGKYHSNVKE LAHKFGLPNL 1200
    VARQIVNTCA QCQQKGEAIH GQVNAELGTW QMDCTHLEGK IIIVAVHVAS 1250
    GFIEAEVIPQ ESGRQTALFL LKLASRWPIT HLHTDNGANF TSQEVKMVAW 1300
    WVGIEQSFGV PYNPQSQGVV EAMNHHLKNQ IERIREQANT METIVLMAVH 1350
    CMNFKRRGGI GDMTPVERLV NMITTEQEIQ FLQAKNSKLK NFRVYFREGR 1400
    NQLWQGPGEL LWKGDGAVIV KVGTDIKVIP RRKAKIIRDY GPRQEMDSGS 1450
    HLEGAREDGE MA 1462

    Note: Produced by -1 ribosomal frameshifting.

    Length:1,462
    Mass (Da):165,014
    Last modified:January 23, 2007 - v3
    Checksum:iDBA366324EA0167E
    GO
    Isoform Gag polyprotein (identifier: P12450-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P12450.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:520
    Mass (Da):58,175
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04498 Genomic DNA. Translation: AAB00746.1. Sequence problems.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04498 Genomic DNA. Translation: AAB00746.1 . Sequence problems.

    3D structure databases

    ProteinModelPortali P12451.
    SMRi P12451. Positions 2-135, 145-380, 384-429, 512-610, 613-1165, 1170-1215, 1224-1381, 1385-1439.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.10.10.200. 1 hit.
    1.10.1200.30. 1 hit.
    1.10.150.90. 1 hit.
    1.10.375.10. 1 hit.
    2.30.30.10. 1 hit.
    2.40.70.10. 1 hit.
    3.30.420.10. 2 hits.
    4.10.60.10. 1 hit.
    InterProi IPR001969. Aspartic_peptidase_AS.
    IPR000721. Gag_p24.
    IPR001037. Integrase_C_retrovir.
    IPR001584. Integrase_cat-core.
    IPR017856. Integrase_Zn-bd_dom-like_N.
    IPR003308. Integrase_Zn-bd_dom_N.
    IPR000071. Lentvrl_matrix_N.
    IPR012344. Matrix_N_HIV/RSV.
    IPR018061. Pept_A2A_retrovirus_sg.
    IPR001995. Peptidase_A2_cat.
    IPR021109. Peptidase_aspartic_dom.
    IPR008916. Retrov_capsid_C.
    IPR008919. Retrov_capsid_N.
    IPR010999. Retrovr_matrix_N.
    IPR012337. RNaseH-like_dom.
    IPR002156. RNaseH_domain.
    IPR000477. RT_dom.
    IPR010659. RVT_connect.
    IPR010661. RVT_thumb.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF00540. Gag_p17. 1 hit.
    PF00607. Gag_p24. 1 hit.
    PF00552. IN_DBD_C. 1 hit.
    PF02022. Integrase_Zn. 1 hit.
    PF00075. RNase_H. 1 hit.
    PF00665. rve. 1 hit.
    PF00077. RVP. 1 hit.
    PF00078. RVT_1. 1 hit.
    PF06815. RVT_connect. 1 hit.
    PF06817. RVT_thumb. 1 hit.
    PF00098. zf-CCHC. 2 hits.
    [Graphical view ]
    PRINTSi PR00234. HIV1MATRIX.
    SMARTi SM00343. ZnF_C2HC. 2 hits.
    [Graphical view ]
    SUPFAMi SSF46919. SSF46919. 1 hit.
    SSF47353. SSF47353. 1 hit.
    SSF47836. SSF47836. 1 hit.
    SSF47943. SSF47943. 1 hit.
    SSF50122. SSF50122. 1 hit.
    SSF50630. SSF50630. 1 hit.
    SSF53098. SSF53098. 2 hits.
    SSF57756. SSF57756. 1 hit.
    PROSITEi PS50175. ASP_PROT_RETROV. 1 hit.
    PS00141. ASP_PROTEASE. 1 hit.
    PS50994. INTEGRASE. 1 hit.
    PS51027. INTEGRASE_DBD. 1 hit.
    PS50879. RNASE_H. 1 hit.
    PS50878. RT_POL. 1 hit.
    PS50158. ZF_CCHC. 2 hits.
    PS50876. ZF_INTEGRASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular and biological characterization of a replication competent human immunodeficiency type 2 (HIV-2) proviral clone."
      Franchini G., Fargnoli K.A., Giombini F., Jagodzinski L.L., de Rossi A., Bosch M., Biberfeld G., Fenyo A.M., Albert J., Gallo R.C., Wong-Staal F.
      Proc. Natl. Acad. Sci. U.S.A. 86:2433-2437(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Proteolytic processing and particle maturation."
      Vogt V.M.
      Curr. Top. Microbiol. Immunol. 214:95-131(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    3. Cited for: REVIEW.
    4. "Mechanisms of retroviral recombination."
      Negroni M., Buc H.
      Annu. Rev. Genet. 35:275-302(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    5. Cited for: REVIEW.

    Entry informationi

    Entry nameiPOL_HV2SB
    AccessioniPrimary (citable) accession number: P12451
    Secondary accession number(s): Q85570
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template switching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs.

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3