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P03399

- ENV_AVIRE

UniProt

P03399 - ENV_AVIRE

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Protein

Envelope glycoprotein

Gene

env

Organism
Avian reticuloendotheliosis virus
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

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 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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei392 – 3932Cleavage; by hostBy similarity

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Fusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein
Alternative name(s):
Env polyprotein
Cleaved into the following 2 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 73
Short name:
gp73
Transmembrane protein
Short name:
TM
Alternative name(s):
Glycoprotein 22
Short name:
gp22
Gene namesi
Name:env
OrganismiAvian reticuloendotheliosis virus
Taxonomic identifieri11636 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostiGalliformes [TaxID: 8976]

Subcellular locationi

Chain Transmembrane protein : 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
Chain Surface protein : 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 519484ExtracellularSequence AnalysisAdd
BLAST
Transmembranei520 – 54021HelicalSequence AnalysisAdd
BLAST
Topological domaini541 – 58242CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 582547Envelope glycoproteinPRO_0000239546Add
BLAST
Chaini36 – 392357Surface proteinBy similarityPRO_0000040683Add
BLAST
Chaini393 – 582190Transmembrane proteinBy similarityPRO_0000040684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi241 – 2411N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi251 ↔ 481Interchain (between SU and TM chains, or C-254 with C-481); in linked formBy similarity
Disulfide bondi251 ↔ 254By similarity
Glycosylationi301 – 3011N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi314 – 3141N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi473 ↔ 480By similarity
Glycosylationi485 – 4851N-linked (GlcNAc...); by hostSequence Analysis
Lipidationi543 – 5431S-palmitoyl cysteine; by hostBy similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as a 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 (By similarity).By similarity
The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion (By similarity).By similarity
The transmembrane protein is palmitoylated.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by a labile interchain disulfide bond.By similarity

Structurei

3D structure databases

ProteinModelPortaliP03399.
SMRiP03399. Positions 433-485.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni396 – 41621Fusion peptideSequence AnalysisAdd
BLAST
Regioni456 – 47217ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili417 – 46751Sequence AnalysisAdd
BLAST
Coiled coili477 – 51337Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi251 – 2544CXXC
Motifi473 – 4819CX6CC

Domaini

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).By similarity

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03399-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDCLTDLRST EGKVDQAGKT LILLVVWWGF GTTAEGHPLQ QLWELPCDCS
60 70 80 90 100
GGYVSPDLPI TPTPSIAVAS PLPDLRVWLQ GSWGWGGGFR QQWECVFKPK
110 120 130 140 150
IIPSVQEQPG PCECLTIATQ MHSTCYEKAQ ECTLLGKTYF TAILQKTKLG
160 170 180 190 200
SYEDGPNKLL QASCTGIWET SMLGPRCPCV CLDGGGPTDR FGRICAEGLE
210 220 230 240 250
EIIRHSYPSV QYHPLALPRP RGVDLDPQTS DILEATHQVL NATNPQLAEN
260 270 280 290 300
CWLCMTLGTQ SPQPSRRMAM SLSMEIAVLA SLSGATHRVN RCQLLCREAD
310 320 330 340 350
NRTGIPVGYV HFTNCTSIQE SLTRRVIYEI LRDYVLHRVM YLCVEQHAYT
360 370 380 390 400
ALPNKWIGLC ILASIVPDMS IIPGEEPIPL PSIEYTAGRH KRAVQFIPLL
410 420 430 440 450
VGLGITGATL AGGTGLGVSV HTYHKLSNQL IEDVQALSGT INDLQDQIDS
460 470 480 490 500
LAEVVLQNRR GLDLLTAEQG GICLALQEKC CFYANKSGIV RDKIRKLQED
510 520 530 540 550
LLARKRALYD NPLWNGLNGF LPYLLPSLGP LFGLILFLTL GPCIRKTLTR
560 570 580
IIHDKIQGSK NPRISPAVQA TPNRDGYPRS MV
Length:582
Mass (Da):64,138
Last modified:July 21, 1986 - v1
Checksum:iCD2560ADFC026D32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01455 Genomic RNA. Translation: CAA25686.1.
PIRiA03999. VCVDAR.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01455 Genomic RNA. Translation: CAA25686.1 .
PIRi A03999. VCVDAR.

3D structure databases

ProteinModelPortali P03399.
SMRi P03399. Positions 433-485.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view ]
PANTHERi PTHR10424. PTHR10424. 1 hit.
Pfami PF00429. TLV_coat. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleic acid sequences of the oncogene v-rel in reticuloendotheliosis virus strain T and its cellular homolog, the proto-oncogene c-rel."
    Wilhelmsen K.C., Eggleton K., Temin H.M.
    J. Virol. 52:172-182(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: A.

Entry informationi

Entry nameiENV_AVIRE
AccessioniPrimary (citable) accession number: P03399
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Strain A is a helper virus of the strain T.

External Data

Dasty 3