P12495 (GAG_HV1Z2) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 129. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Human immunodeficiency virus type 1 group M subtype D (isolate Z2/CDC-Z34) (HIV-1)|
|Taxonomic identifier||11683 [NCBI]|
|Taxonomic lineage||Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group ›|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
|Sequence length||501 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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.
Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex.
Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers.
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.
Matrix protein p17, and probably Pr55Gag form hexamer rings of trimers. Oligomerization possibly creates a central hole into which the cytoplasmic tail of the gp41 envelope protein may be inserted. Pr55Gag interacts with host TRIM22; this interaction seems to disrupt proper trafficking of Gag polyprotein and may interfere with budding. p6-gag interacts with Vpr. p6-gag interacts with host TSG101. p6-gag interacts with host PDCD6IP/AIP1 By similarity. Pr55Gag interacts with host PDZD8 By similarity.
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.
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. p6-gag contains two L domains: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 and a LYPX(n)L motif which interacts with PDCD6IP/AIP1 By similarity.
Capsid protein p24 is phosphorylated.
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.
Nucleocapsid protein p7 is methylated by host PRMT6, impairing its function by reducing RNA annealing and the initiation of reverse transcription By similarity.
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).
Belongs to the primate lentivirus group gag polyprotein family.
Contains 2 CCHC-type zinc fingers.
|This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]|
Note: 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.
|Isoform Gag polyprotein (identifier: P12495-1) |
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.
|Note: Produced by conventional translation.|
|Isoform Gag-Pol polyprotein (identifier: P12499-1) |
The sequence of this isoform can be found in the external entry P12499.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
|Note: Produced by -1 ribosomal frameshifting.|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed; by host By similarity|
|Chain||2 – 501||500||Gag polyprotein||PRO_0000261239|
|Chain||2 – 133||132||Matrix protein p17 By similarity||PRO_0000038499|
|Chain||134 – 364||231||Capsid protein p24 By similarity||PRO_0000038500|
|Peptide||365 – 379||15||Spacer peptide p2 By similarity||PRO_0000038501|
|Chain||380 – 434||55||Nucleocapsid protein p7 By similarity||PRO_0000038502|
|Peptide||435 – 450||16||Spacer peptide p1 By similarity||PRO_0000038503|
|Chain||451 – 501||51||p6-gag By similarity||PRO_0000038504|
|Zinc finger||392 – 409||18||CCHC-type 1|
|Zinc finger||413 – 430||18||CCHC-type 2|
|Motif||16 – 22||7||Nuclear export signal By similarity|
|Motif||26 – 32||7||Nuclear localization signal By similarity|
|Motif||457 – 460||4||PTAP/PSAP motif|
|Motif||484 – 493||10||LYPX(n)L motif|
|Site||133 – 134||2||Cleavage; by viral protease By similarity|
|Site||364 – 365||2||Cleavage; by viral protease By similarity|
|Site||379 – 380||2||Cleavage; by viral protease By similarity|
|Site||434 – 435||2||Cleavage; by viral protease By similarity|
|Site||450 – 451||2||Cleavage; by viral protease By similarity|
Amino acid modifications
|Modified residue||389||1||Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 By similarity|
|Modified residue||411||1||Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 By similarity|
|Lipidation||2||1||N-myristoyl glycine; by host By similarity|
Helix Strand Turn
|Turn||178 – 180||3|
|||Theodore T., Buckler-White A.J.|
Submitted (JUL-1989) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"Role of HIV-1 Gag domains in viral assembly."|
Scarlata S., Carter C.
Biochim. Biophys. Acta 1614:62-72(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
|+||Additional computationally mapped references.|
|M22639 Genomic RNA. Translation: AAA45365.1.|
3D structure databases
|SMR||P12495. Positions 2-434, 451-501. |
Protocols and materials databases
Family and domain databases
|Gene3D||1.10.1200.30. 1 hit. |
126.96.36.199. 1 hit.
1.10.375.10. 1 hit.
188.8.131.52. 1 hit.
|InterPro||IPR000721. Gag_p24. |
|Pfam||PF00540. Gag_p17. 1 hit. |
PF00607. Gag_p24. 1 hit.
PF08705. Gag_p6. 1 hit.
PF00098. zf-CCHC. 2 hits.
|PRINTS||PR00234. HIV1MATRIX. |
|SMART||SM00343. ZnF_C2HC. 2 hits. |
|SUPFAM||SSF47353. SSF47353. 1 hit. |
SSF47836. SSF47836. 1 hit.
SSF47943. SSF47943. 1 hit.
SSF57756. SSF57756. 1 hit.
|PROSITE||PS50158. ZF_CCHC. 2 hits. |
|Accession||Primary (citable) accession number: P12495|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|