ENV_MLVAV
ID ENV_MLVAV Reviewed; 669 AA.
AC P03386;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 70;
DE Short=gp70;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Envelope protein p15E;
DE Contains:
DE RecName: Full=R-peptide;
DE AltName: Full=p2E;
DE Flags: Precursor;
GN Name=env;
OS AKV murine leukemia virus (AKR (endogenous) murine leukemia virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11791;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6319746; DOI=10.1128/jvi.49.2.471-478.1984;
RA Herr W.;
RT "Nucleotide sequence of AKV murine leukemia virus.";
RL J. Virol. 49:471-478(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6294621; DOI=10.1093/nar/10.21.6931;
RA Herr W., Corbin V., Gilbert W.;
RT "Nucleotide sequence of the 3' half of AKV.";
RL Nucleic Acids Res. 10:6931-6944(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6283170; DOI=10.1128/jvi.42.2.519-529.1982;
RA Lenz J., Crowther R., Straceski A., Haseltine W.;
RT "Nucleotide sequence of the Akv env gene.";
RL J. Virol. 42:519-529(1982).
CC -!- FUNCTION: The surface protein (SU) attaches the virus to the host cell
CC by binding to its receptor. This interaction triggers the refolding of
CC the transmembrane protein (TM) and is thought to activate its fusogenic
CC potential by unmasking its fusion peptide. Fusion occurs at the host
CC cell plasma membrane (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During viral and
CC target cell membrane fusion, the coiled coil regions (heptad repeats)
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and target cell membranes. Membranes fusion leads to
CC delivery of the nucleocapsid into the cytoplasm (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-
CC TM heterodimers attached by a labile interchain disulfide bond.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC cell membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral
CC membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=The surface protein is not anchored to the
CC viral envelope, but associates with the virion surface through its
CC binding to TM. Both proteins are thought to be concentrated at the site
CC of budding and incorporated into the virions possibly by contacts
CC between the cytoplasmic tail of Env and the N-terminus of Gag (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [R-peptide]: Host cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=The R-peptide is
CC membrane-associated through its palmitate. {ECO:0000250}.
CC -!- DOMAIN: The YXXL motif is involved in determining the exact site of
CC viral release at the surface of infected mononuclear cells and promotes
CC endocytosis.
CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC many retroviral envelope proteins. Synthetic peptides derived from this
CC relatively conserved sequence inhibit immune function in vitro and in
CC vivo (By similarity). {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as an inactive precursor that is
CC N-glycosylated and processed likely by host cell furin or by a furin-
CC like protease in the Golgi to yield the mature SU and TM proteins. The
CC cleavage site between SU and TM requires the minimal sequence [KR]-X-
CC [KR]-R. The R-peptide is released from the C-terminus of the
CC cytoplasmic tail of the TM protein upon particle formation as a result
CC of proteolytic cleavage by the viral protease. Cleavage of this peptide
CC is required for TM to become fusogenic (By similarity). {ECO:0000250}.
CC -!- PTM: The CXXC motif is highly conserved across a broad range of
CC retroviral envelope proteins. It is thought to participate in the
CC formation of a labile disulfide bond possibly with the CX6CC motif
CC present in the transmembrane protein. Isomerization of the intersubunit
CC disulfide bond to an SU intrachain disulfide bond is thought to occur
CC upon receptor recognition in order to allow membrane fusion (By
CC similarity). {ECO:0000250}.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
CC -!- PTM: The R-peptide is palmitoylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24493.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J01998; AAB03092.1; -; Genomic_RNA.
DR EMBL; V01164; CAA24493.1; ALT_INIT; Genomic_DNA.
DR PIR; A92995; VCVWEK.
DR SMR; P03386; -.
DR Proteomes; UP000008875; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 3.90.310.10; -; 1.
DR InterPro; IPR008981; FMuLV_rcpt-bd.
DR InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR PANTHER; PTHR10424; PTHR10424; 1.
DR Pfam; PF00429; TLV_coat; 1.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell;
KW Zinc.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..669
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239579"
FT CHAIN 32..470
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040745"
FT CHAIN 471..650
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040746"
FT PEPTIDE 651..669
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040747"
FT TOPO_DOM 32..611
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 32..267
FT /note="Receptor-binding domain (RBD)"
FT /evidence="ECO:0000255"
FT REGION 266..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..493
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 539..555
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 502..538
FT /evidence="ECO:0000255"
FT MOTIF 337..340
FT /note="CXXC"
FT MOTIF 556..564
FT /note="CX6CC"
FT MOTIF 656..659
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 273..307
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 470..471
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 650..651
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT LIPID 631
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 77..129
FT /evidence="ECO:0000250"
FT DISULFID 103..118
FT /evidence="ECO:0000250"
FT DISULFID 104..114
FT /evidence="ECO:0000250"
FT DISULFID 152..172
FT /evidence="ECO:0000250"
FT DISULFID 164..177
FT /evidence="ECO:0000250"
FT DISULFID 209..215
FT /evidence="ECO:0000250"
FT DISULFID 337..564
FT /note="Interchain (between SU and TM chains, or C-340 with
FT C-564); in linked form"
FT DISULFID 337..340
FT DISULFID 367..421
FT /evidence="ECO:0000250"
FT DISULFID 386..398
FT /evidence="ECO:0000250"
FT DISULFID 428..441
FT /evidence="ECO:0000250"
FT DISULFID 556..563
FT /evidence="ECO:0000250"
FT CONFLICT 35
FT /note="G -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="E -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="E -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 73756 MW; 3A6C3845208A13F2 CRC64;
MESTTLSKPF KNQVNPWGPL IVLLILGGVN PVTLGNSPHQ VFNLTWEVTN GDRETVWAIT
GNHPLWTWWP DLTPDLCMLA LHGPSYWGLE YRAPFSPPPG PPCCSGSSDS TPGCSRDCEE
PLTSYTPRCN TAWNRLKLSK VTHAHNGGFY VCPGPHRPRW ARSCGGPESF YCASWGCETT
GRASWKPSSS WDYITVSNNL TSDQATPVCK GNEWCNSLTI RFTSFGKQAT SWVTGHWWGL
RLYVSGHDPG LIFGIRLKIT DSGPRVPIGP NPVLSDRRPP SRPRPTRSPP PSNSTPTETP
LTLPEPPPAG VENRLLNLVK GAYQALNLTS PDKTQECWLC LVSGPPYYEG VAVLGTYSNH
TSAPANCSVA SQHKLTLSEV TGQGLCIGAV PKTHQVLCNT TQKTSDGSYY LAAPTGTTWA
CSTGLTPCIS TTILDLTTDY CVLVELWPRV TYHSPSYVYH QFERRAKYKR EPVSLTLALL
LGGLTMGGIA AGVGTGTTAL VATQQFQQLQ AAMHDDLKEV EKSITNLEKS LTSLSEVVLQ
NRRGLDLLFL KEGGLCAALK EECCFYADHT GLVRDSMAKL RERLSQRQKL FESQQGWFEG
LFNKSPWFTT LISTIMGPLI ILLLILLFGP CILNRLVQFI KDRISVVQAL VLTQQYHQLK
TIEDCKSRE
