Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P03399

- ENV_AVIRE

UniProt

P03399 - ENV_AVIRE

Protein

Envelope glycoprotein

Gene

env

Organism
Avian reticuloendotheliosis virus
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. viral envelope Source: UniProtKB-KW
    4. virion membrane Source: UniProtKB-SubCell

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini36 – 519484ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini541 – 58242CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei520 – 54021HelicalSequence AnalysisAdd
    BLAST

    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

    MDCLTDLRST EGKVDQAGKT LILLVVWWGF GTTAEGHPLQ QLWELPCDCS    50
    GGYVSPDLPI TPTPSIAVAS PLPDLRVWLQ GSWGWGGGFR QQWECVFKPK 100
    IIPSVQEQPG PCECLTIATQ MHSTCYEKAQ ECTLLGKTYF TAILQKTKLG 150
    SYEDGPNKLL QASCTGIWET SMLGPRCPCV CLDGGGPTDR FGRICAEGLE 200
    EIIRHSYPSV QYHPLALPRP RGVDLDPQTS DILEATHQVL NATNPQLAEN 250
    CWLCMTLGTQ SPQPSRRMAM SLSMEIAVLA SLSGATHRVN RCQLLCREAD 300
    NRTGIPVGYV HFTNCTSIQE SLTRRVIYEI LRDYVLHRVM YLCVEQHAYT 350
    ALPNKWIGLC ILASIVPDMS IIPGEEPIPL PSIEYTAGRH KRAVQFIPLL 400
    VGLGITGATL AGGTGLGVSV HTYHKLSNQL IEDVQALSGT INDLQDQIDS 450
    LAEVVLQNRR GLDLLTAEQG GICLALQEKC CFYANKSGIV RDKIRKLQED 500
    LLARKRALYD NPLWNGLNGF LPYLLPSLGP LFGLILFLTL GPCIRKTLTR 550
    IIHDKIQGSK NPRISPAVQA TPNRDGYPRS MV 582
    Length:582
    Mass (Da):64,138
    Last modified:July 21, 1986 - v1
    Checksum:iCD2560ADFC026D32
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01455 Genomic RNA. Translation: CAA25686.1.
    PIRiA03999. VCVDAR.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 1, 2014
    This is version 88 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