P03322 · GAG_RSVP

Function

function

Gag polyprotein

The p10 domain folds back and interacts with the capsid protein domain during Gag polyprotein assembly in the immature particle (before the maturation cleavage that splits the 2 domains).

Capsid protein p27, alternate cleaved 1

Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro (PubMed:10873863, PubMed:28588198).
Binds to inositol hexakisphosphate (IP6), which allows the assembly of the polyhedral capsid (PubMed:34050170).

Capsid protein p27, alternate cleaved 2

Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro (PubMed:10873863, PubMed:28588198).
Binds to inositol hexakisphosphate (IP6), which allows the assembly of the polyhedral capsid (PubMed:34050170).

Nucleocapsid protein p12

Binds strongly to viral nucleic acids and promotes their packaging (PubMed:17070546).
Plays a role in the maturation-stabilization of the viral dimeric RNA via highly structured zinc-binding motifs (By similarity).

Spacer peptide

Plays a role in the oligomerization of the Gag polyprotein and in the stabilization of the immature particle (PubMed:28588198).
Essential layering element during tube assembly that is progressively removed as capsid assembly proceeds (PubMed:28588198).
Allows the cooperative binging of Gag to the host plasma membrane (PubMed:26676779).

Protease p15

Aspartyl protease that 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.

Features

Showing features for site, active site.

TypeIDPosition(s)Description
Site155-156Cleavage; by viral protease p15
Site166-167Cleavage; by viral protease p15
Site177-178Cleavage; by viral protease p15
Site239-240Cleavage; by viral protease p15
Site418Involved in capsid protein dimerization upon acidification
Site430Involved in capsid protein dimerization upon acidification
Site476-477Cleavage; by viral protease p15
Site479-480Cleavage; by viral protease p15
Site488-489Cleavage; by viral protease p15
Site577-578Cleavage; by viral protease p15
Active site614For protease activity; shared with dimeric partner

GO annotations

AspectTerm
Cellular Componenthost cell nucleolus
Cellular Componenthost cell nucleoplasm
Cellular Componenthost cell plasma membrane
Cellular Componentmembrane
Cellular Componentviral capsid
Molecular Functionaspartic-type endopeptidase activity
Molecular Functionnucleic acid binding
Molecular Functionstructural constituent of virion
Molecular Functionzinc ion binding
Biological Processproteolysis
Biological Processviral procapsid maturation
Biological Processviral translational frameshifting

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      gag

Organism names

Accessions

  • Primary accession
    P03322
  • Secondary accessions
    • Q77YH0

Proteomes

Subcellular Location

Matrix protein p19

Virion

Capsid protein p27, alternate cleaved 1

Virion

Capsid protein p27, alternate cleaved 2

Virion

Nucleocapsid protein p12

Virion

Gag polyprotein

Host cell membrane
Note: Shuttles between nucleoplasm and nucleolus.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis17275% loss of budding.
Mutagenesis180-18440% loss of budding.
Mutagenesis219Reduced nucleolar localization of Gag polyprotein.
Mutagenesis524-527Complete loss of nuclear and nucleolar localization.
Mutagenesis549-551Reduced localization in nucleolus; no effect on nuclear localization.

PTM/Processing

Features

Showing features for chain, peptide.

TypeIDPosition(s)Description
ChainPRO_00000261131-155Matrix protein p19
ChainPRO_00004421141-701Gag polyprotein
ChainPRO_0000026114156-166p2A
ChainPRO_0000026115167-177p2B
ChainPRO_0000026116178-239p10
ChainPRO_0000442115240-476Capsid protein p27, alternate cleaved 1
ChainPRO_0000026117240-479Capsid protein p27, alternate cleaved 2
PeptidePRO_0000026118477-488Spacer peptide
ChainPRO_0000026119489-577Nucleocapsid protein p12
ChainPRO_0000026120578-701Protease p15

Post-translational modification

Gag polyprotein

Specific enzymatic cleavages in vivo yield mature proteins (PubMed:8627817, PubMed:8636100).
The cleavage at the C-terminus of the Capsid protein p27 is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid protein C-terminally extended by 3 amino acids in a ratio of 2:1 (PubMed:7666544).

Interaction

Subunit

Protease p15

Active as a homodimer (PubMed:2166563, PubMed:2536902).

Capsid protein p27, alternate cleaved 1

Homodimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062).
Homomultimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062).
Homohexamer (PubMed:28588198).

Capsid protein p27, alternate cleaved 2

Homodimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062).
Homomultimer (PubMed:10873863, PubMed:14659756, PubMed:19446529, PubMed:20228062).
Homohexamer (PubMed:28588198).

Gag polyprotein

Homohexamer (PubMed:26223638).
Interacts (via p2B domain) with host PACSIN2; this interaction probably allows PACSIN2 recruitment to viral assembly sites (By similarity).

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, motif, zinc finger, domain.

TypeIDPosition(s)Description
Region128-150Disordered
Motif172-175PPXY motif
Motif180-184LYPX(n)L motif
Region181-217Disordered
Region217-259Involved in capsid protein dimerization
Motif219-229Nuclear export signal
Region290-298Involved in capsid protein dimerization
Region351-362Involved in capsid protein dimerization
Zinc finger507-524CCHC-type 1
Motif524-527Nuclear/nucleolar localization signal
Zinc finger533-550CCHC-type 2
Region543-575Disordered
Domain609-690Peptidase A2

Domain

Gag polyprotein

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. P2B contains two L domains: a PPXY motif which probably binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases and a LYPX(n)L domain which is known to bind the Alix adaptator protein.

Gag polyprotein

Contains a nuclear export signal in p10 and a nucleolar localization signal in nucleocapsid protein p12.
Capsid protein p27: Proton-driven dimerization of the C-terminus facilitates capsid assembly.

Keywords

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Ribosomal frameshifting. Translation results in the formation of the Gag polyprotein. Ribosomal frameshifting at the gag/pol genes boundary produces the Gag-Pol polyprotein.

P03322-1

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.

  • Name
    Gag polyprotein
  • Note
    Produced by conventional translation.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    701
  • Mass (Da)
    74,527
  • Last updated
    1986-07-21 v1
  • Checksum
    5FD365D9CFEF37F1
MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMILGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPPGAEQSRAEPGHAGQAPGPALTDWARVREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVIAAATRDPRHPANGQGRGERTNLNRLKGLADGMVGNPQGQAALLRPGELVAITASALQAFREVARLAEPAGPWADIMQGPSESFVDFANRLIKAVEGSDLPPSARAPVIIDCFRQKSQPDIQQLIRTAPSTLTTPGEIIKYVLDRQKTAPLTDQGIAAAMSSAIQPLIMAVVNRERDGQTGSGGRARGLCYTCGSPGHYQAQCPKKRKSGNSRERCQLCNGMGHNAKQCRKRDGNQGQRPGKGLSSGPWPGPEPPAVSLAMTMEHKDRPLVRVILTNTGSHPVKQRSVYITALLDSGADITIISEEDWPTDWPVMEAANPQIHGIGGGIPMRKSRDMIELGVINRDGSLERPLLLFPAVAMVRGSILGRDCLQGLGLRLTNL

P03354-1

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

View isoform
  • Name
    Gag-Pol polyprotein
  • See also
    sequence in UniParc or sequence clusters in UniRef

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict505in Ref. 2; AA sequence
Sequence conflict536in Ref. 2; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF033808
EMBL· GenBank· DDBJ
AAC82560.1
EMBL· GenBank· DDBJ
Genomic RNA
J02342
EMBL· GenBank· DDBJ
AAB59932.1
EMBL· GenBank· DDBJ
Genomic RNA
V01197
EMBL· GenBank· DDBJ
CAA24512.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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