UniProtKB - P35954 (ENV_VILVK)
Envelope glycoprotein gp160
env
Functioni
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).
By similarityThe 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).
By similarityGO - Biological processi
- viral entry into host cell Source: UniProtKB-KW
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Biological process | Host-virus interaction, Viral attachment to host cell, Virus entry into host cell |
Names & Taxonomyi
Protein namesi | Recommended name: Envelope glycoprotein gp160Alternative name(s): Env polyprotein Cleaved into the following 2 chains: Alternative name(s): Glycoprotein 135 Short name: gp135 Alternative name(s): Glycoprotein 46 Short name: gp46 |
Gene namesi | Name:env |
Organismi | Maedi visna virus (strain KV1772) (MVV) (Visna lentivirus) |
Taxonomic identifieri | 36374 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Pararnavirae › Artverviricota › Revtraviricetes › Ortervirales › Retroviridae › Orthoretrovirinae › Lentivirus › |
Virus hosti | Ovis aries (Sheep) [TaxID: 9940] |
Subcellular locationi
- Virion membrane By similarity; Single-pass type I membrane protein By similarity
- Host cell membrane By similarity; Single-pass type I membrane protein By similarity Note: It is probably 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
- Virion membrane By similarity; Peripheral membrane protein By similarity
- Host cell membrane By similarity; Peripheral membrane protein By similarity Note: The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably 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).By similarity
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 107 – 832 | ExtracellularSequence analysisAdd BLAST | 726 | |
Transmembranei | 833 – 853 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 854 – 983 | CytoplasmicSequence analysisAdd BLAST | 130 |
Keywords - Cellular componenti
Host cell membrane, Host membrane, Membrane, Viral envelope protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 106 | Sequence analysisAdd BLAST | 106 | |
ChainiPRO_0000239543 | 107 – 983 | Envelope glycoprotein gp160Add BLAST | 877 | |
ChainiPRO_0000038744 | 107 – 656 | Surface proteinBy similarityAdd BLAST | 550 | |
ChainiPRO_0000038745 | 657 – 983 | Transmembrane proteinBy similarityAdd BLAST | 327 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 140 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 161 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 206 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 258 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 298 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 364 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 381 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 387 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 403 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 414 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 435 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 439 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 470 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 475 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 481 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 491 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 501 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 515 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 527 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 537 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 542 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 543 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 568 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 697 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 765 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 772 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 788 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Glycosylationi | 822 | N-linked (GlcNAc...) asparagine; by hostSequence analysis | 1 | |
Lipidationi | 856 | S-palmitoyl cysteine; by hostBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 656 – 657 | Cleavage; by hostBy similarity | 2 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, PalmitateInteractioni
Subunit structurei
The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by noncovalent interactions or by a labile interchain disulfide bond.
By similarityStructurei
Secondary structure
3D structure databases
SMRi | P35954 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P35954 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 22 | DisorderedSequence analysisAdd BLAST | 22 | |
Regioni | 657 – 677 | Fusion peptideAdd BLAST | 21 | |
Regioni | 723 – 739 | ImmunosuppressionBy similarityAdd BLAST | 17 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 689 – 739 | Sequence analysisAdd BLAST | 51 | |
Coiled coili | 780 – 815 | Sequence analysisAdd BLAST | 36 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1 – 17 | Basic and acidic residuesSequence analysisAdd BLAST | 17 |
Keywords - Domaini
Coiled coil, Signal, Transmembrane, Transmembrane helixi Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MASKESKPSR TTRRGMEPPL RETWNQVLQE LVKRQQQEEE EQQGLVSGKK
60 70 80 90 100
KSWVSIDLLG TEGKDIKKVN IWEPCEKWFA QVVWGVLWVL QIVLWGCLMW
110 120 130 140 150
EVRKGNQCQA EEVIALVSDP GGFQRVQHVE TVPVTCVTKN FTQWGCQPEG
160 170 180 190 200
AYPDPELEYR NISREILEEV YKQDWPWNTY HWPLWQMENM RQWMKENEKE
210 220 230 240 250
YKERTNKTKE DIDDLVAGRI RGRFCVPYPY ALLRCEEWCW YPESINQETG
260 270 280 290 300
HAEKIKINCT KAKAVSCTEK MSLAAVQRVY WEKEDEESMK FLNIKACNIS
310 320 330 340 350
LRCQDEGKSP GGCVQGYPIP KGAEIIPEAM KYLRGKKSRY GGIKDKNGEL
360 370 380 390 400
KLPLSVRVWV RMANLSGWVN GTPPYWSARI NGSTGINGTR WYGIGTLHHL
410 420 430 440 450
GCNISSNPER GICNFTGELW IGGDKFPYYY TPSWNCSQNW TGHPVWHVFR
460 470 480 490 500
YLDMTEHMTS RCIQRPKRHN ITVGNGTITG NCSVTNWDGC NCTRSGNHLY
510 520 530 540 550
NSTSGGLLVI ICRQNSTITG IMGTNTNWTT MWNIYQNCSR CNNSSLDRTG
560 570 580 590 600
SGTLGTVNNL KCSLPHRNES NKWTCKSQRD SYIAGRDFWG KVKAKYSCES
610 620 630 640 650
NLGGLDSMMH QQMLLQRYQV IRVRAYTYGV VEMPQSYMEA QGENKRSRRN
660 670 680 690 700
LQRKKRGIGL VIVLAIMAII AAAGAGLGVA NAVQQSYTRT AVQSLANATA
710 720 730 740 750
AQQEVLEASY AMVQHIAKGI RILEARVARV EALVDRMMVY QELDCWHYQH
760 770 780 790 800
YCVTSTRSEV ANYVNWTRFK DNCTWQQWEE EIEQHEGNLS LLLREAALQV
810 820 830 840 850
HIAQRDARRI PDAWKAIQEA FNWSSWFSWL KYIPWIIMGI VGLMCFRILM
860 870 880 890 900
CVISMCLQAY KQVKQIRYTQ VTVVIEAPVE LEEKQKRNGD GTNGCASLER
910 920 930 940 950
ERRTSHRSFI QIWRATWWAW KTSPWRHNWR TMPYITLLPI LVIWQWMEEN
960 970 980
GWNGENQHKK KKERVDCQDR EQMPTLENDY VEL
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 900 | R → H in AAA48362 (PubMed:8382414).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | S55323 Genomic DNA Translation: AAB25463.1 L06906 Genomic RNA Translation: AAA48362.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | S55323 Genomic DNA Translation: AAB25463.1 L06906 Genomic RNA Translation: AAA48362.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1JEK | X-ray | 1.50 | A | 693-732 | [»] | |
B | 775-808 | [»] | ||||
SMRi | P35954 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P35954 |
Family and domain databases
MobiDBi | Search... |
Entry informationi
Entry namei | ENV_VILVK | |
Accessioni | P35954Primary (citable) accession number: P35954 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
Last sequence update: | June 1, 1994 | |
Last modified: | June 2, 2021 | |
This is version 120 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references