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 P27978


[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_SIVVG
Primary accession number P27978
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 64)
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
Simian immunodeficiency virus agm.vervet (isolate AGM3) (SIV-agm.ver) (Simian immunodeficiency virus African green monkey vervet) [TaxID: 11730] 
Taxonomy Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; Lentivirus; Primate lentivirus group.
Virus host Cercopithecidae (Old World monkeys) [TaxID: 9527]
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1016/0042-6822(90)90246-N; PubMed=2158689 [NCBI, ExPASy, EBI, Israel, Japan]
Baier M., Garber C., Mueller C., Cichutek K., Kurth R.;
"Complete nucleotide sequence of a simian immunodeficiency virus from African green monkeys: a novel type of intragroup divergence.";
Virology 176:216-221(1990).
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 (By similarity).
  • FUNCTION: Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).
  • FUNCTION: Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).
  • 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 host TSG101 and PDCD6IP/AIP1 (By similarity).
  • SUBCELLULAR LOCATION: Matrix protein p17: Virion (Potential). Nucleus (By similarity). Cytoplasm (By similarity). 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 IDP27978-1
    Note: Produced by conventional translation.
    This is the isoform sequence displayed in this entry.
    NameGag-Pol polyprotein
    Isoform IDP27980-1
    Note: Produced by -1 ribosomal frameshifting.
    This isoform is stored in UniProtKB/Swiss-Prot entry P27980.
  • 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 (By similarity).
  • 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).
  • MISCELLANEOUS: This is an African green monkey isolate.
  • 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
M30931; AAA91913.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP Q03859; 1ED1. [HSSP ENTRY / PDB]
SMR P27978; 155-364.
ModBase P27978.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0019028; Cellular component: viral capsid (inferred from electronic annotation from InterPro).
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 InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0016032; Biological process: viral reproduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000721; Gag_p24.
IPR000071; Lentvrl_matrix_N.
IPR012344; Matrix_HIV/RSV_N.
IPR008916; Retrov_capsid_C.
IPR008919; Retrov_capsid_N.
IPR013084; Znf_CCH_retrovir.
IPR001878; Znf_CCHC.
Graphical view of domain structure.
Gene3D G3DSA:1.10.150.90; Matrix_HIV/RSV_N; 1.
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.
PF00098; zf-CCHC; 2.
Pfam graphical view of domain structure.
PRINTS PR00939; C2HCZNFINGER.
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 P27978.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Capsid protein; Cytoplasm; Host-virus interaction; Lipoprotein; Metal-binding; 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   521  520     Gag polyprotein (By similarity). PRO_0000316109
CHAIN   2   145  144     Matrix protein p17 (By similarity). PRO_0000038622
CHAIN   146   376  231     Capsid protein p24 (By similarity). PRO_0000038623
PEPTIDE   377   390  14     Spacer peptide p2 (By similarity). PRO_0000316110
CHAIN   391   443  53     Nucleocapsid protein p7 (By similarity). PRO_0000038624
PEPTIDE   444   458  15     Spacer peptide p1 (By similarity). PRO_0000316111
CHAIN   483   521  39     p6-gag (By similarity). PRO_0000316112
ZN_FING   402   419  18     CCHC-type 1. 
ZN_FING   423   440  18     CCHC-type 2. 
MOTIF   16    22  7     Nuclear export signal (By similarity). 
MOTIF   26    32  7     Nuclear localization signal (By similarity). 
MOTIF   490   492  3     PTAP motif (By similarity). 
MOTIF   513   517  5     LXXLF motif (By similarity). 
SITE   443   444  2     Cleavage; by viral protease (By similarity). 
LIPID   2     2        N-myristoyl glycine; by host (By similarity). 
Sequence information
Length: 521 AA [This is the length of the unprocessed precursor] Molecular weight: 58409 Da [This is the MW of the unprocessed precursor] CRC64: 1F111BD2F2EDF4F5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGAATSALNR RQLDKFEHIR LRPTGKKKYQ IKHLIWAGKE MERFGLHERL LESEEGCKKI 

        70         80         90        100        110        120 
IEVLYPLEPT GSEGLKSLFN LVCVLFCVHK DKEVKDTEEA VAIVRQCCHL VEKERNAERN 

       130        140        150        160        170        180 
TTETSSGQKK NDKGVTVPPG GSQNFPAQQQ GNAWIHVPLS PRTLNAWVKA VEEKKFGAEI 

       190        200        210        220        230        240 
VPMFQALSEG CTPYDINQML NVLGDHQGAL QIVKEIINEE AAQWDIAHPP PAGPLPAGQL 

       250        260        270        280        290        300 
RDPRGSDIAG TTSTVQEQLE WIYTANPRVD VGAIYRRWII LGLQKCVKMY NPVSVLDIRQ 

       310        320        330        340        350        360 
GPKEAFKDYV DRFYKAIRAE QASGEVKQWM TESLLIQNAN PDCKVILKGL GMHPTLEEML 

       370        380        390        400        410        420 
TACQGVGGPS YKAKVMAEMM QNMQSQNMMQ QGGQRGRPRP PVKCYNCGKF GHMQRQCPEP 

       430        440        450        460        470        480 
RKMRCLKCGK PGHLAKDCRG QVNFLGYGRW MGAKPRNFPA ATLGVEPTAP PPPSPYDPAK 

       490        500        510        520 
KLLQQYADKG KQLREQRKKP PAVNPDWTEG YSLNSLFGED Q 

P27978 in FASTA format

View entry in original UniProtKB/Swiss-Prot 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!