P17282 (GAG_SIVCZ) Reviewed, UniProtKB/Swiss-Prot
Last modified October 16, 2013. Version 89. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Simian immunodeficiency virus (isolate CPZ GAB1) (SIV-cpz) (Chimpanzee immunodeficiency virus) [Complete proteome]|
|Taxonomic identifier||402771 [NCBI]|
|Taxonomic lineage||Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group ›|
|Virus host||Pan (chimpanzees) [TaxID: 9596]|
|Sequence length||508 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Inferred from homology|
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 By similarity.
Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex By similarity.
Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers By similarity.
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 is a trimer. Interacts with gp120. p6-gag interacts with host TSG101 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 By similarity.
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.
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: P17282-1) |
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: P17283-1) |
The sequence of this isoform can be found in the external entry P17283.
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|
|Chain||2 – 508||507||Gag polyprotein By similarity||PRO_0000316150|
|Chain||2 – 140||139||Matrix protein p17 By similarity||PRO_0000038644|
|Chain||141 – 371||231||Capsid protein p24 By similarity||PRO_0000038645|
|Peptide||372 – 387||16||Spacer peptide p2 By similarity||PRO_0000316151|
|Chain||388 – 442||55||Nucleocapsid protein p7 By similarity||PRO_0000038646|
|Peptide||443 – 458||16||Spacer peptide p1 By similarity||PRO_0000316152|
|Chain||459 – 508||50||p6-gag By similarity||PRO_0000316153|
|Zinc finger||400 – 417||18||CCHC-type 1|
|Zinc finger||421 – 438||18||CCHC-type 2|
|Motif||16 – 22||7||Nuclear export signal By similarity|
|Motif||26 – 32||7||Nuclear localization signal By similarity|
|Motif||465 – 468||4||PTAP/PSAP motif|
|Motif||491 – 500||10||LYPX(n)L motif|
|Site||140 – 141||2||Cleavage; by viral protease By similarity|
|Site||371 – 372||2||Cleavage; by viral protease By similarity|
|Site||387 – 388||2||Cleavage; by viral protease By similarity|
|Site||442 – 443||2||Cleavage; by viral protease By similarity|
|Site||458 – 459||2||Cleavage; by viral protease By similarity|
Amino acid modifications
|Lipidation||2||1||N-myristoyl glycine; by host By similarity|
|X52154 Genomic RNA. Translation: CAA36401.1.|
|PIR||FOLJSI. S09983. |
3D structure databases
|SMR||P17282. Positions 2-442, 459-508. |
Protocols and materials databases
Family and domain databases
|Gene3D||1.10.1200.30. 1 hit. |
184.108.40.206. 1 hit.
1.10.375.10. 1 hit.
220.127.116.11. 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: P17282|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families