P03353 · PRO_HTLV2

Function

function

Gag-Pro polyprotein

The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus.

Matrix protein p19

Matrix protein.

Capsid protein p24

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

Nucleocapsid protein p15-pro

Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs.

Protease

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 (Potential). Cleaves the translation initiation factor eIF4G leading to the inhibition of host cap-dependent translation (By similarity).

Miscellaneous

HTLV-1 lineages are divided in four clades, A (Cosmopolitan), B (Central African group), C (Melanesian group) and D (New Central African group).

Features

Showing features for site, active site.

TypeIDPosition(s)Description
Site136-137Cleavage; by viral protease
Site350-351Cleavage; by viral protease
Site446-447Cleavage; by viral protease
Active site478Protease; shared with dimeric partner
Site571-572Cleavage; by viral protease
Site579-580Cleavage; by viral protease

GO annotations

AspectTerm
Cellular Componentviral nucleocapsid
Molecular Functionaspartic-type endopeptidase activity
Molecular Functionnucleic acid binding
Molecular Functionstructural molecule activity
Molecular Functionzinc ion binding
Biological Processproteolysis
Biological Processsymbiont-mediated suppression of host gene expression
Biological Processviral translational frameshifting

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      gag-pro

Organism names

Accessions

  • Primary accession
    P03353

Proteomes

Subcellular Location

Matrix protein p19

Virion

Capsid protein p24

Virion

Nucleocapsid protein p15-pro

Virion

Keywords

PTM/Processing

Features

Showing features for initiator methionine, lipidation, chain, peptide.

TypeIDPosition(s)Description
Initiator methionine1Removed; by host
Lipidation2N-myristoyl glycine; by host
ChainPRO_00002598102-136Matrix protein p19
ChainPRO_00002598092-602Gag-Pro polyprotein
ChainPRO_0000259811137-350Capsid protein p24
ChainPRO_0000259812351-446Nucleocapsid protein p15-pro
ChainPRO_0000199535447-571Protease
PeptidePRO_0000259813572-579p1
ChainPRO_0000259814580-602Transframe peptide

Post-translational modification

Gag-Pro polyprotein

Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini.

Matrix protein p19

Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in budding.

Gag-Pro polyprotein

Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles.

Keywords

Interaction

Subunit

Gag-Pro polyprotein

Homodimer; the homodimers are part of the immature particles. Interacts with human TSG101 and NEDD4; these interactions are essential for budding and release of viral particles.

Matrix protein p19

Homodimer; further assembles as homohexamers.

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Motif94-97PTAP/PSAP motif
Region94-121Disordered
Compositional bias97-121Pro residues
Motif124-127PPXY motif
Zinc finger361-378CCHC-type 1
Zinc finger384-401CCHC-type 2
Region399-425Disordered
Domain473-551Peptidase A2
Region582-602Disordered

Domain

Capsid protein p24

The capsid protein N-terminus seems to be involved in Gag-Gag interactions.

Gag-Pro 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. Matrix protein p19 contains two L domains: a PTAP/PSAP motif which interacts with the UEV domain of TSG101, and a PPXY motif which binds to the WW domains of the ubiquitin ligase NEDD4.

Keywords

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Ribosomal frameshifting. This strategy of translation probably allows the virus to modulate the quantity of each viral protein.

P03353-1

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-Pro polyprotein
  • Note
    Produced by -1 ribosomal frameshifting at the gag-pro genes boundary.
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    602
  • Mass (Da)
    66,435
  • Last updated
    2007-01-23 v3
  • Checksum
    15627B078EFAC16E
MGQIHGLSPTPIPKAPRGLSTHHWLNFLQAAYRLQPRPSDFDFQQLRRFLKLALKTPIWLNPIDYSLLASLIPKGYPGRVVEIINILVKNQVSPSAPAAPVPTPICPTTTPPPPPPPSPEAHVPPPYVEPTTTQCFPILHPPGAPSAHRPWQMKDLQAIKQEVSSSALGSPQFMQTLRLAVQQFDPTAKDLQDLLQYLCSSLVVSLHHQQLNTLITEAETRGMTGYNPMAGPLRMQANNPAQQGLRREYQNLWLAAFSTLPGNTRDPSWAAILQGLEEPYCAFVERLNVALDNGLPEGTPKEPILRSLAYSNANKECQKILQARGHTNSPLGEMLRTCQAWTPKDKTKVLVVQPRRPPPTQPCFRCGKVGHWSRDCTQPRPPPGPCPLCQDPSHWKRDCPQLKPPQEEGEPLLLDLPSTSGTTEEKNLLKGGDLISPHPDQDISILPLIPLRQQQQPILGVRISVMGQTPQPTQALLDTGADLTVIPQTLVPGPVKLHDTLILGASGQTNTQFKLLQTPLHIFLPFRRSPVILSSCLLDTHNKWTIIGRDALQQCQGLLYLPDDPSPHQLLPIATPNTIGLEHLPPPPQVDQFPLNLSASRP

P03346-1

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 polyprotein
  • See also
    sequence in UniParc or sequence clusters in UniRef

P03363-1

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-Pro-Pol polyprotein
  • See also
    sequence in UniParc or sequence clusters in UniRef

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias97-121Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M10060
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Similar Proteins

Disclaimer

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