ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P04593


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GAG_HV1B5
Primary accession number P04593
Secondary accession numbers None
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 94)
Name and origin of the protein
Protein name Gag polyprotein
Synonym Pr55Gag
Contains Matrix protein p17
     (MA)
Capsid protein p24
     (CA)
Spacer peptide p2
Nucleocapsid protein p7
     (NC)
Spacer peptide p1
p6-gag
Gene name
Name: gag
From
Human immunodeficiency virus type 1 (isolate BH5 group M subtype B) (HIV-1) [TaxID: 11682] 
Taxonomy Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; Lentivirus; Primate lentivirus group.
Virus host Homo sapiens (Human) [TaxID: 9606]
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1038/313277a0; PubMed=2578615 [NCBI, ExPASy, EBI, Israel, Japan]
Ratner L., Haseltine W.A., Patarca R., Livak K.J., Starcich B.R., Josephs S.F., Doran E.R., Rafalski J.A., Whitehorn E.A., Baumeister K., Ivanoff L., Petteway S.R. Jr., Pearson M.L., Lautenberger J.A., Papas T.S., Ghrayeb J., Chang N.T., Gallo R.C., Wong-Staal F.;
"Complete nucleotide sequence of the AIDS virus, HTLV-III.";
Nature 313:277-284(1985).
[2]
REVIEW.
DOI=10.1016/S0005-2736(03)00163-9; PubMed=12873766 [NCBI, ExPASy, EBI, Israel, Japan]
Scarlata S., Carter C.;
"Role of HIV-1 Gag domains in viral assembly.";
Biochim. Biophys. Acta 1614:62-72(2003).
Comments
  • FUNCTION: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu.
  • FUNCTION: Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.
  • FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers.
  • FUNCTION: p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1 (By similarity).
  • SUBUNIT: Matrix protein p17 is a trimer. Interacts with gp120. p6-gag interacts with human TSG101 and PDCD6IP/AIP1 (By similarity).
  • SUBCELLULAR LOCATION: Matrix protein p17: Virion (Potential). Host nucleus (By similarity). Host cytoplasm (By similarity). Host cell membrane; Lipid-anchor (Potential). 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).
  • SUBCELLULAR LOCATION: Capsid protein p24: Virion (Potential).
  • SUBCELLULAR LOCATION: Nucleocapsid protein p7: Virion (Potential).
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by ribosomal frameshifting. 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.
    NameGag polyprotein
    Isoform IDP04593-1
    Note: Produced by conventional translation.
    This is the isoform sequence displayed in this entry.
    NameGag-Pol polyprotein
    Isoform IDP04587-1
    Note: Produced by -1 ribosomal frameshifting.
    This isoform is stored in UniProtKB/Swiss-Prot entry P04587.
  • DOMAIN: Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. p6-gag contains two L domains: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 and a LXXLF motif which interacts with PDCD6IP/AIP1 (By similarity).
  • PTM: Capsid protein p24 is phosphorylated.
  • PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity).
  • PTM: Nucleocapsid protein p7 is methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription (By similarity).
  • MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K).
  • SIMILARITY: Belongs to the primate lentivirus group gag polyprotein family.
  • SIMILARITY: Contains 2 CCHC-type zinc fingers.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
K02012; AAA44652.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P04591; 1E6J. [HSSP ENTRY / PDB]
SMR P04593; 2-283, 143-351, 378-432, 461-512.
ModBase P04593.
Enzyme and pathway databases
Reactome REACT_6185; HIV Infection.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0030430; Cellular component: host cell cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0042025; Cellular component: host cell nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0020002; Cellular component: host cell plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0019028; Cellular component: viral capsid (inferred from electronic annotation from UniProtKB-KW).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005198; Molecular function: structural molecule activity (inferred from electronic annotation from UniProtKB-KW).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019059; Biological process: initiation of viral infection (inferred from experiment from Reactome).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0019047; Biological process: provirus integration (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR000721; Gag_p24.
IPR014817; Gag_p6.
IPR000071; Lentvrl_matrix_N.
IPR008916; Retrov_capsid_C.
IPR008919; Retrov_capsid_N.
IPR013084; Znf_CCH_retrovir.
IPR001878; Znf_CCHC.
Graphical view of domain structure.
Gene3D G3DSA:1.10.1200.30; Retrov_capsid_C; 1.
G3DSA:1.10.375.10; Retrov_capsid_N; 1.
G3DSA:4.10.60.10; Znf_CCH_retrovir; 1.
Pfam PF00540; Gag_p17; 1.
PF00607; Gag_p24; 1.
PF08705; Gag_p6; 2.
PF00098; zf-CCHC; 2.
Pfam graphical view of domain structure.
PRINTS PR00234; HIV1MATRIX.
SMART SM00343; ZnF_C2HC; 2.
SMART graphical view of domain structure.
PROSITE PS50158; ZF_CCHC; 2.
PROSITE graphical view of domain structure (profiles).
Other
ProtoNet P04593.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
AIDS; Capsid protein; Cell membrane; Cytoplasm; Host-virus interaction; Lipoprotein; Membrane; Metal-binding; Methylation; Myristate; Nucleus; Phosphoprotein; Repeat; Ribosomal frameshifting; RNA-binding; Viral nucleoprotein; Virion; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed; by host (By similarity). 
CHAIN   2   512  511     Gag polyprotein. PRO_0000261210
CHAIN   2   132  131     Matrix protein p17 (By similarity). PRO_0000038481
CHAIN   133   363  231     Capsid protein p24 (By similarity). PRO_0000038482
PEPTIDE   364   377  14     Spacer peptide p2 (By similarity). PRO_0000038483
CHAIN   378   432  55     Nucleocapsid protein p7 (By similarity). PRO_0000038484
PEPTIDE   433   448  16     Spacer peptide p1 (By similarity). PRO_0000038485
CHAIN   449   512  64     p6-gag (By similarity). PRO_0000038486
ZN_FING   390   407  18     CCHC-type 1. 
ZN_FING   411   428  18     CCHC-type 2. 
MOTIF   16    22  7     Nuclear export signal (By similarity). 
MOTIF   26    32  7     Nuclear localization signal (By similarity). 
MOTIF   455   458  4     PTAP motif 1 (By similarity). 
MOTIF   467   470  4     PTAP motif 2 (By similarity). 
MOTIF   501   505  5     LXXLF motif (By similarity). 
SITE   132   133  2     Cleavage; by viral protease (By similarity). 
SITE   363   364  2     Cleavage; by viral protease (By similarity). 
SITE   377   378  2     Cleavage; by viral protease (By similarity). 
SITE   432   433  2     Cleavage; by viral protease (By similarity). 
SITE   448   449  2     Cleavage; by viral protease (By similarity). 
MOD_RES   387   387        Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 (By similarity). 
MOD_RES   409   409        Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 (By similarity). 
LIPID   2     2        N-myristoyl glycine; by host (By similarity). 
Sequence information
Length: 512 AA [This is the length of the unprocessed precursor] Molecular weight: 57238 Da [This is the MW of the unprocessed precursor] CRC64: 243A82D3CBBE7A9C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGARASVLSG GELDRWEKIR LRPGGKKKYK LKHIVWASRE LERFAVNPGL LETSEGCRQI 

        70         80         90        100        110        120 
LGQLQPSLQT GSEELRSLYN TVATLYCVHQ RIEIKDTKEA LDKIEEEQNK SKKKAQQAAA 

       130        140        150        160        170        180 
DTGHSSQVSQ NYPIVQNIQG QMVHQAISPR TLNAWVKVVE EKAFSPEVIP MFSALSEGAT 

       190        200        210        220        230        240 
PQDLNTMLNT VGGHQAAMQM LKETINEEAA EWDRVHPVHA GPIAPGQMRE PRGSDIAGTT 

       250        260        270        280        290        300 
STLQEQIGWM TNNPPIPVGE IYKRWIILGL NKIVRMYSPT SILDIRQGPK EPFRDYVDRF 

       310        320        330        340        350        360 
YKTLRAEQAS QEVKNWMTET LLVQNANPDC KTILKALGPA ATLEEMMTAC QGVGGPGHKA 

       370        380        390        400        410        420 
RVLAEAMSQV TNSTTIMMQR GNFRNQRKIV KCFNCGKEGH IARNCKAPRK KGCWKCGKEG 

       430        440        450        460        470        480 
HQMKDCTERQ ANFLGKIWPS YKGRPGNFLQ SRPEPTAPPF LQSRPEPTAP PEESFRSGVE 

       490        500        510 
TTTPPQKQEP IDKELYPLTS LRSLFGNDPS SQ 

P04593 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!