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)

P03386

- ENV_MLVAV

UniProt

P03386 - ENV_MLVAV

Protein

Envelope glycoprotein

Gene

env

Organism
AKV murine leukemia virus (AKR (endogenous) murine leukemia virus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 100 (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
    Metal bindingi117 – 1171ZincBy similarity
    Sitei470 – 4712Cleavage; by hostBy similarity
    Sitei650 – 6512Cleavage; by viral protease p14By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. structural molecule activity Source: InterPro

    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

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Envelope glycoprotein
    Alternative name(s):
    Env polyprotein
    Cleaved into the following 3 chains:
    Surface protein
    Short name:
    SU
    Alternative name(s):
    Glycoprotein 70
    Short name:
    gp70
    Transmembrane protein
    Short name:
    TM
    Alternative name(s):
    Envelope protein p15E
    Alternative name(s):
    p2E
    Gene namesi
    Name:env
    OrganismiAKV murine leukemia virus (AKR (endogenous) murine leukemia virus)
    Taxonomic identifieri11791 [NCBI]
    Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000008875: Genome

    Subcellular locationi

    Chain Surface protein : Virion membrane; Peripheral membrane protein. 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 virion 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.By similarity
    R-peptide : Host cell membrane By similarity; Peripheral membrane protein By similarity
    Note: The R-peptide is membrane-associated through its palmitate.By similarity

    GO - Cellular componenti

    1. host cell plasma membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. viral capsid Source: InterPro
    4. viral envelope Source: UniProtKB-KW
    5. 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 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 669638Envelope glycoproteinPRO_0000239579Add
    BLAST
    Chaini32 – 470439Surface proteinBy similarityPRO_0000040745Add
    BLAST
    Chaini471 – 650180Transmembrane proteinBy similarityPRO_0000040746Add
    BLAST
    Peptidei651 – 66919R-peptideBy similarityPRO_0000040747Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi43 – 431N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi77 ↔ 129By similarity
    Disulfide bondi103 ↔ 118By similarity
    Disulfide bondi104 ↔ 114By similarity
    Disulfide bondi152 ↔ 172By similarity
    Disulfide bondi164 ↔ 177By similarity
    Glycosylationi199 – 1991N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi209 ↔ 215By similarity
    Glycosylationi293 – 2931N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi327 – 3271N-linked (GlcNAc...); by hostBy similarity
    Disulfide bondi337 ↔ 564Interchain (between SU and TM chains, or C-340 with C-564); in linked form
    Disulfide bondi337 ↔ 340
    Glycosylationi359 – 3591N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi366 – 3661N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi367 ↔ 421By similarity
    Disulfide bondi386 ↔ 398By similarity
    Glycosylationi399 – 3991N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi428 ↔ 441By similarity
    Disulfide bondi556 ↔ 563By similarity
    Lipidationi631 – 6311S-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. 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.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
    The R-peptide 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

    ProteinModelPortaliP03386.
    SMRiP03386. Positions 40-266, 516-568.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 611580ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini633 – 66937CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei612 – 63221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni32 – 267236Receptor-binding domain (RBD)Sequence AnalysisAdd
    BLAST
    Regioni473 – 49321Fusion peptideBy similarityAdd
    BLAST
    Regioni539 – 55517ImmunosuppressionBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili502 – 53837Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi337 – 3404CXXC
    Motifi556 – 5649CX6CC
    Motifi656 – 6594YXXL motif; contains endocytosis signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi264 – 30845Pro-richAdd
    BLAST

    Domaini

    The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis.
    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

    Gene3Di3.90.310.10. 1 hit.
    InterProiIPR008981. FMuLV_rcpt-bd.
    IPR018154. TLV/ENV_coat_polyprotein.
    [Graphical view]
    PANTHERiPTHR10424. PTHR10424. 1 hit.
    PfamiPF00429. TLV_coat. 1 hit.
    [Graphical view]
    SUPFAMiSSF49830. SSF49830. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P03386-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESTTLSKPF KNQVNPWGPL IVLLILGGVN PVTLGNSPHQ VFNLTWEVTN    50
    GDRETVWAIT GNHPLWTWWP DLTPDLCMLA LHGPSYWGLE YRAPFSPPPG 100
    PPCCSGSSDS TPGCSRDCEE PLTSYTPRCN TAWNRLKLSK VTHAHNGGFY 150
    VCPGPHRPRW ARSCGGPESF YCASWGCETT GRASWKPSSS WDYITVSNNL 200
    TSDQATPVCK GNEWCNSLTI RFTSFGKQAT SWVTGHWWGL RLYVSGHDPG 250
    LIFGIRLKIT DSGPRVPIGP NPVLSDRRPP SRPRPTRSPP PSNSTPTETP 300
    LTLPEPPPAG VENRLLNLVK GAYQALNLTS PDKTQECWLC LVSGPPYYEG 350
    VAVLGTYSNH TSAPANCSVA SQHKLTLSEV TGQGLCIGAV PKTHQVLCNT 400
    TQKTSDGSYY LAAPTGTTWA CSTGLTPCIS TTILDLTTDY CVLVELWPRV 450
    TYHSPSYVYH QFERRAKYKR EPVSLTLALL LGGLTMGGIA AGVGTGTTAL 500
    VATQQFQQLQ AAMHDDLKEV EKSITNLEKS LTSLSEVVLQ NRRGLDLLFL 550
    KEGGLCAALK EECCFYADHT GLVRDSMAKL RERLSQRQKL FESQQGWFEG 600
    LFNKSPWFTT LISTIMGPLI ILLLILLFGP CILNRLVQFI KDRISVVQAL 650
    VLTQQYHQLK TIEDCKSRE 669
    Length:669
    Mass (Da):73,756
    Last modified:July 21, 1986 - v1
    Checksum:i3A6C3845208A13F2
    GO

    Sequence cautioni

    The sequence CAA24493.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351G → R(PubMed:6294621)Curated
    Sequence conflicti463 – 4631E → K(PubMed:6294621)Curated
    Sequence conflicti592 – 5921E → K(PubMed:6294621)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01998 Genomic RNA. Translation: AAB03092.1.
    V01164 Genomic DNA. Translation: CAA24493.1. Different initiation.
    PIRiA92995. VCVWEK.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01998 Genomic RNA. Translation: AAB03092.1 .
    V01164 Genomic DNA. Translation: CAA24493.1 . Different initiation.
    PIRi A92995. VCVWEK.

    3D structure databases

    ProteinModelPortali P03386.
    SMRi P03386. Positions 40-266, 516-568.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.90.310.10. 1 hit.
    InterProi IPR008981. FMuLV_rcpt-bd.
    IPR018154. TLV/ENV_coat_polyprotein.
    [Graphical view ]
    PANTHERi PTHR10424. PTHR10424. 1 hit.
    Pfami PF00429. TLV_coat. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49830. SSF49830. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of AKV murine leukemia virus."
      Herr W.
      J. Virol. 49:471-478(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Nucleotide sequence of the Akv env gene."
      Lenz J., Crowther R., Straceski A., Haseltine W.
      J. Virol. 42:519-529(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiENV_MLVAV
    AccessioniPrimary (citable) accession number: P03386
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome

    External Data

    Dasty 3