P31791 · ENV_FENV1
- ProteinEnvelope glycoprotein
- Geneenv
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids671 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).
The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 470-471 | Cleavage; by host | ||||
Sequence: RD | ||||||
Site | 650-651 | Cleavage; by viral protease | ||||
Sequence: LV |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | host cell plasma membrane | |
Cellular Component | membrane | |
Cellular Component | viral envelope | |
Cellular Component | virion membrane | |
Biological Process | fusion of virus membrane with host plasma membrane | |
Biological Process | symbiont entry into host cell | |
Biological Process | virion attachment to host cell |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameEnvelope glycoprotein
- Alternative names
- Cleaved into 3 chains
Gene names
Organism names
- Organism
- Taxonomic lineageViruses > Riboviria > Pararnavirae > Artverviricota > Revtraviricetes > Ortervirales > Retroviridae > Orthoretrovirinae > Gammaretrovirus > Feline endogenous virus
- Virus hosts
Accessions
- Primary accessionP31791
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Transmembrane protein
Virion membrane ; Single-pass type I membrane protein
Host cell membrane ; Single-pass type I membrane protein
Surface protein
Virion membrane ; Peripheral membrane protein
Host cell membrane ; Peripheral membrane protein
Note: The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity).
R-peptide
Host cell membrane ; Peripheral membrane protein
Note: The R-peptide is membrane-associated through its palmitate.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-611 | Extracellular | ||||
Sequence: KIVKEGNPHQVYTLTWQIYSQSGEVVWEVQGNHALNTWWPALTPDFCQLAAGLDTWDIPDRSPKNLETSMEGTSQQLTPQGCSKPWKRCALTERDFYVCPRDNRDRATAHRCGGYEEYFCSAWGCETTGDAYWQPTSTWDLITITRNYTKPDSCDDRVERERKTSRHWRDPLSLPLKITFTDSGKRALGWQTGYTWGLRWYLPGKDRGIILKIKLKIDTITQTVGPNLVLADQKTPVQLAIPVQPPRAPTQTPRVNPVNSTLSPSLGYPAPAPGPRPPYPTSPSRPGTGDRLLNLVQGVYLTLNLTAPNQTQDCWLCLTAKPPYYQGVAIIGNFTNHTNAPLRCSTTPRHGLTLTEVTGYGLCIGKIPPSHQNLCSQTVPSVGQGPYYLTAPNGTYWVCNTGLTPCISLQILNDTADYCILIELWPKIFYHDSEYIYGHYEPGGRFRRDPVSLTVALLLGGLTMGSLAAGIGTGTAALIETNQFKQLQIAMHSDIQALEESISALERSLISLSEVVLQNRRGLDLLFLQEGGLCAALKEECCFYADHTGIVRDSMAKLRERFKQRQKLFESQQGWFEGWYNKSPWFTTL | ||||||
Transmembrane | 612-632 | Helical | ||||
Sequence: VSSLMVPLILLLLILMFGPCI | ||||||
Topological domain | 633-671 | Cytoplasmic | ||||
Sequence: LNHLLQFIRERLSVIQALVLTQQYHQLRQFDAERPDAIE |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, lipidation, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MKPPAGMVFLWVLTSLGAGIGA | ||||||
Chain | PRO_0000040703 | 23-470 | Surface protein | |||
Sequence: KIVKEGNPHQVYTLTWQIYSQSGEVVWEVQGNHALNTWWPALTPDFCQLAAGLDTWDIPDRSPKNLETSMEGTSQQLTPQGCSKPWKRCALTERDFYVCPRDNRDRATAHRCGGYEEYFCSAWGCETTGDAYWQPTSTWDLITITRNYTKPDSCDDRVERERKTSRHWRDPLSLPLKITFTDSGKRALGWQTGYTWGLRWYLPGKDRGIILKIKLKIDTITQTVGPNLVLADQKTPVQLAIPVQPPRAPTQTPRVNPVNSTLSPSLGYPAPAPGPRPPYPTSPSRPGTGDRLLNLVQGVYLTLNLTAPNQTQDCWLCLTAKPPYYQGVAIIGNFTNHTNAPLRCSTTPRHGLTLTEVTGYGLCIGKIPPSHQNLCSQTVPSVGQGPYYLTAPNGTYWVCNTGLTPCISLQILNDTADYCILIELWPKIFYHDSEYIYGHYEPGGRFRR | ||||||
Chain | PRO_0000239558 | 23-671 | Envelope glycoprotein | |||
Sequence: KIVKEGNPHQVYTLTWQIYSQSGEVVWEVQGNHALNTWWPALTPDFCQLAAGLDTWDIPDRSPKNLETSMEGTSQQLTPQGCSKPWKRCALTERDFYVCPRDNRDRATAHRCGGYEEYFCSAWGCETTGDAYWQPTSTWDLITITRNYTKPDSCDDRVERERKTSRHWRDPLSLPLKITFTDSGKRALGWQTGYTWGLRWYLPGKDRGIILKIKLKIDTITQTVGPNLVLADQKTPVQLAIPVQPPRAPTQTPRVNPVNSTLSPSLGYPAPAPGPRPPYPTSPSRPGTGDRLLNLVQGVYLTLNLTAPNQTQDCWLCLTAKPPYYQGVAIIGNFTNHTNAPLRCSTTPRHGLTLTEVTGYGLCIGKIPPSHQNLCSQTVPSVGQGPYYLTAPNGTYWVCNTGLTPCISLQILNDTADYCILIELWPKIFYHDSEYIYGHYEPGGRFRRDPVSLTVALLLGGLTMGSLAAGIGTGTAALIETNQFKQLQIAMHSDIQALEESISALERSLISLSEVVLQNRRGLDLLFLQEGGLCAALKEECCFYADHTGIVRDSMAKLRERFKQRQKLFESQQGWFEGWYNKSPWFTTLVSSLMVPLILLLLILMFGPCILNHLLQFIRERLSVIQALVLTQQYHQLRQFDAERPDAIE | ||||||
Disulfide bond | 121↔142 | |||||
Sequence: CPRDNRDRATAHRCGGYEEYFC | ||||||
Disulfide bond | 134↔147 | |||||
Sequence: CGGYEEYFCSAWGC | ||||||
Glycosylation | 169 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 281 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 326 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 331 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 355 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 358 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 415 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 435 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Chain | PRO_0000040704 | 471-650 | Transmembrane protein | |||
Sequence: DPVSLTVALLLGGLTMGSLAAGIGTGTAALIETNQFKQLQIAMHSDIQALEESISALERSLISLSEVVLQNRRGLDLLFLQEGGLCAALKEECCFYADHTGIVRDSMAKLRERFKQRQKLFESQQGWFEGWYNKSPWFTTLVSSLMVPLILLLLILMFGPCILNHLLQFIRERLSVIQAL | ||||||
Lipidation | 631 | S-palmitoyl cysteine; by host | ||||
Sequence: C | ||||||
Peptide | PRO_0000239559 | 651-671 | R-peptide | |||
Sequence: VLTQQYHQLRQFDAERPDAIE |
Post-translational modification
Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. The R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic (By similarity).
The transmembrane protein is palmitoylated.
The R-peptide is palmitoylated.
Keywords
- PTM
PTM databases
Interaction
Subunit
The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by noncovalent interactions or by a labile interchain disulfide bond.
Family & Domains
Features
Showing features for region, compositional bias, motif, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 265-310 | Disordered | ||||
Sequence: VQPPRAPTQTPRVNPVNSTLSPSLGYPAPAPGPRPPYPTSPSRPGT | ||||||
Compositional bias | 290-306 | Pro residues | ||||
Sequence: YPAPAPGPRPPYPTSPS | ||||||
Motif | 336-339 | CXXC | ||||
Sequence: CWLC | ||||||
Region | 473-493 | Fusion peptide | ||||
Sequence: VSLTVALLLGGLTMGSLAAGI | ||||||
Coiled coil | 501-550 | |||||
Sequence: IETNQFKQLQIAMHSDIQALEESISALERSLISLSEVVLQNRRGLDLLFL | ||||||
Region | 539-555 | Immunosuppression | ||||
Sequence: LQNRRGLDLLFLQEGGL | ||||||
Motif | 556-564 | CX6CC | ||||
Sequence: CAALKEECC | ||||||
Coiled coil | 560-596 | |||||
Sequence: KEECCFYADHTGIVRDSMAKLRERFKQRQKLFESQQG | ||||||
Motif | 656-659 | YXXL motif; contains endocytosis signal | ||||
Sequence: YHQL |
Domain
The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo (By similarity).
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length671
- Mass (Da)75,152
- Last updated1993-07-01 v1
- ChecksumEA9847024EF794A0
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 290-306 | Pro residues | ||||
Sequence: YPAPAPGPRPPYPTSPS |