Aliases for ERVK-6 Gene
- Endogenous Retrovirus Group K Member 6, Envelope 2 3
- HERV-K_7p22.1 Provirus Ancestral Env Polyprotein 2 3 4
- HERV-K_7p22.1 Provirus Ancestral Pol Protein 2 3 4
- HERV-K_7p22.1 Provirus Ancestral Pro Protein 2 3 4
- HERV-K_7p22.1 Provirus Rec Protein 2 3 4
- HERV-K(C7) Envelope Protein 2 3 4
- HERV-K108 Envelope Protein 2 3 4
- Endogenous Retrovirus Group K, Member 6 2 3
- Endogenous Retroviral Sequence K, 6 2 3
- HERV-K(HML-2.HOM) Envelope Protein 3 4
- Envelope Polyprotein 3 4
- HERV-K (HML-2.HOM) 2 3
- Rev-Like Protein 3 4
- Rev/Rex Homolog 3 4
- EnvK2 Protein 3 4
- ERVK6 3 4
- K-Rev 3 4
- C-Orf 3 4
- CORF 3 4
- Endogenous Retrovirus Group K Member 6 Env Polyprotein 3
- HERV-K_7p22.1 Provirus Ancestral Gag Polyprotein 4
- Endogenous Retrovirus Group K Member 6 2
- Endogenous Retrovirus K Protein 6 4
- HERV-K(HML-2.HOM) Gag Protein 4
- HERV-K(HML-2.HOM) Pol Protein 4
- HERV-K(HML-2.HOM) Pro Protein 4
- HERV-K(HML-2.HOM) Rec Protein 4
- Central Open Reading Frame 4
- HERV-K(C7) Gag Protein 4
- HERV-K(C7) Pol Protein 4
- HERV-K(C7) Pro Protein 4
- HERV-K(C7) Rec Protein 4
- Envelope Glycoprotein 3
- HERV-K108 Gag Protein 4
- HERV-K108 Pol Protein 4
- HERV-K108 Pro Protein 4
- HERV-K108 Rec Protein 4
- Envelope Protein 3
- Gag Polyprotein 4
- EC 188.8.131.52 4
- Proteinase 4
- HERV-K(C7) 3
- HERV-K108 3
- EC 3.4.23 56
- Protease 4
- EnvK2 3
- PR 4
External Ids for ERVK-6 Gene
Previous HGNC Symbols for ERVK-6 Gene
GeneCards Summary for ERVK-6 Gene
ERVK-6 (Endogenous Retrovirus Group K Member 6, Envelope) is a Protein Coding gene. Diseases associated with ERVK-6 include Human Immunodeficiency Virus Type 1. Among its related pathways are Gastric Cancer Network 1. Gene Ontology (GO) annotations related to this gene include nucleic acid binding and structural molecule activity.
UniProtKB/Swiss-Prot for ERVK-6 Gene
Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties.
SU mediates receptor recognition.
TM anchors the envelope heterodimer to the viral membrane through one transmembrane domain. The other hydrophobic domain, called fusion peptide, mediates fusion of the viral membrane with the target cell membrane (By similarity).
The products of the Gag polyproteins of infectious retroviruses perform highly complex orchestrated tasks during the assembly, budding, maturation, and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. Endogenous Gag proteins may have kept, lost or modified their original function during evolution.
Early post-infection, the reverse transcriptase converts the viral RNA genome into double-stranded viral DNA. The RNase H domain of the reverse transcriptase performs two functions. It degrades the RNA template and specifically removes the RNA primer from the RNA/DNA hybrid. Following nuclear import, the integrase catalyzes the insertion of the linear, double-stranded viral DNA into the host cell chromosome. Endogenous Pol proteins may have kept, lost or modified their original function during evolution.
Retroviral replication requires the nuclear export and translation of unspliced, singly-spliced and multiply-spliced derivatives of the initial genomic transcript. Rec interacts with a highly structured RNA element (RcRE) present in the viral 3LTR and recruits the cellular nuclear export machinery. This permits export to the cytoplasm of unspliced genomic or incompletely spliced subgenomic viral transcripts.
Retroviral proteases have roles in the 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.