P29168 · GAG_MLVDE

Function

function

Gag polyprotein

Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release.

Matrix protein p15

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 pre-integration complex.

RNA-binding phosphoprotein p12

Constituent of the pre-integration complex (PIC) which tethers the latter to mitotic chromosomes.

Capsid protein p30

Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex.

Nucleocapsid protein p10-gag

Involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization.

Features

Showing features for site.

TypeIDPosition(s)Description
Site129-130Cleavage; by viral protease p14
Site213-214Cleavage; by viral protease p14
Site476-477Cleavage; by viral protease p14

GO annotations

AspectTerm
Cellular Componenthost cell plasma membrane
Cellular Componentmembrane
Cellular Componentviral nucleocapsid
Molecular FunctionRNA binding
Molecular Functionstructural constituent of virion
Molecular Functionzinc ion binding
Biological Processvirion assembly

Keywords

Names & Taxonomy

Protein names

Gene names

    • Name
      gag

Organism names

Accessions

  • Primary accession
    P29168

Subcellular Location

Gag polyprotein

Virion
Host cell membrane
; Lipid-anchor

Matrix protein p15

Virion

Capsid protein p30

Virion

Nucleocapsid protein p10-gag

Virion

Keywords

PTM/Processing

Features

Showing features for initiator methionine, lipidation, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed; by host
Lipidation2N-myristoyl glycine; by host
ChainPRO_00000408882-129Matrix protein p15
ChainPRO_00003908092-536Gag polyprotein
ChainPRO_0000040889130-213RNA-binding phosphoprotein p12
ChainPRO_0000040890214-476Capsid protein p30
ChainPRO_0000040891477-536Nucleocapsid protein p10-gag

Post-translational modification

Gag polyprotein

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.

Keywords

Interaction

Subunit

Gag polyprotein

Interacts (via PPXY motif) with host NEDD4.

Capsid protein p30

Homohexamer. Further associates as homomultimer (By similarity).
The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers (By similarity).

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, motif, coiled coil, zinc finger.

TypeIDPosition(s)Description
Region139-216Disordered
Compositional bias165-190Pro residues
Motif183-186PPXY motif
Compositional bias432-474Basic and acidic residues
Region432-536Disordered
Coiled coil436-474
Compositional bias486-521Basic and acidic residues
Zinc finger500-517CCHC-type

Domain

Gag polyprotein

Late-budding domains (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus egress.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    536
  • Mass (Da)
    60,891
  • Last updated
    2007-01-23 v3
  • Checksum
    4D990FD5C5AEF39B
MGQTITTPLSLTLEHWRDVQCIASNQSVDVKRRRWVTFCSVEWPSFDVGWPLDGTFNLDIILQVKSKVFCPGPHGHPDQVPYIVTWEALAYHPPPWVKPFVSPKPFPLSTLPFSPPGPSAHPPSRSDLYTALIPSIKTKPPKSRVLPTNGGPLIDLLTENPPNLGEQGPPLPKGPVKKRRPPPPRYSPPGPMVSRLRGNRDPPAADSTTSRAFPLRLGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLTTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLPNEVNSAFPLERPDWDYTTPEGRNHLVLYRQLLLAGLQNAGRSPTNLAKVKGITQGPSESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLKSKTLGDLVREAEKIFNKRETPEEREERIRRETEEKEERRRAEDEQREKERDRRRHREMSKFLATVVTGQRQDRQGGERRRPQLDKDQCAYCKEKGHWAKDCPKKPRGPRGPRPQTSLLTLGD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias165-190Pro residues
Compositional bias432-474Basic and acidic residues
Compositional bias486-521Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M64096
EMBL· GenBank· DDBJ
AAA46509.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.

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