P63131 · VPK7_HUMAN
- ProteinEndogenous retrovirus group K member 7 Pro protein
- GeneERVK-7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids156 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Retroviral proteases have roles in processing of the primary translation products and the maturation of the viral particle. Endogenous Pro proteins may have kept, lost or modified their original function during evolution. This endogenous protein has retained most of the characteristics of retroviral proteases.
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 26 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | aspartic-type endopeptidase activity | |
Molecular Function | nucleic acid binding | |
Biological Process | proteolysis | |
Biological Process | viral translational frameshifting |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameEndogenous retrovirus group K member 7 Pro protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP63131
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000199546 | 1-156 | Endogenous retrovirus group K member 7 Pro protein | |||
Sequence: WASQVSENRPVCKAIIQGKQFEGLVDTGADVSIIALNQWPKNWPKQKAVTGLVGIGTASEVYQSTEILHCLGPDNQESTVQPMITSIPLNLWGRDLLQQWGAEITMPAPLYSPTSQKIMTKMGYIPGKGLGKNEDGIKVPVEAKINQEREGIGYPF |
Post-translational modification
Autoproteolytically processed at the N-terminus. Expected C-terminal autoprocessing not detected. The sequence shown is that of the processed Pro protein (By similarity).
Keywords
- PTM
PTM databases
Interaction
Subunit
Active as a homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-96 | Peptidase A2 | ||||
Sequence: FEGLVDTGADVSIIALNQWPKNWPKQKAVTGLVGIGTASEVYQSTEILHCLGPDNQESTVQPMITSIPLNLWGRDL | ||||||
Domain | 111-156 | G-patch | ||||
Sequence: YSPTSQKIMTKMGYIPGKGLGKNEDGIKVPVEAKINQEREGIGYPF |
Sequence similarities
Belongs to the peptidase A2 family. HERV class-II K(HML-2) subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
This entry describes 1 isoforms produced by Ribosomal frameshifting. This protein is synthesized as Gag-Pro and Gag-Pro-Pol polyprotein. These polyproteins are thought, by similarity with type-B retroviruses, to be generated by -1 frameshifts occurring at the Gag-Pro and Pro-Pol genes boundaries.
P63131-1
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.
- Name1
- Length156
- Mass (Da)17,078
- Last updated2004-09-13 v1
- ChecksumC49D721F2B056702
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 6 | in Ref. 1 | ||||
Sequence: S → T |
Keywords
- Coding sequence diversity
- Technical term