ENV_MCFF
ID ENV_MCFF Reviewed; 636 AA.
AC P15073;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 107.
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 Mink cell focus-forming murine leukemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC Murine leukemia virus.
OX NCBI_TaxID=11935;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2535909; DOI=10.1016/0042-6822(89)90407-8;
RA Chattopadhyay S.K., Baroudy B.M., Holmes K.L., Fredrickson T.N.,
RA Lander M.R., Morse H.C. III, Hartley J.W.;
RT "Biologic and molecular genetic characteristics of a unique MCF virus that
RT is highly leukemogenic in ecotropic virus-negative mice.";
RL Virology 168:90-100(1989).
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 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 -!- 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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M23029; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P15073; -.
DR SwissPalm; P15073; -.
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: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; 2.
DR SUPFAM; SSF49830; SSF49830; 1.
PE 3: Inferred from homology;
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; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..636
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239577"
FT CHAIN 33..440
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040739"
FT CHAIN 441..620
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040740"
FT PEPTIDE 621..636
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040741"
FT TOPO_DOM 33..581
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 32..233
FT /note="Receptor-binding domain (RBD)"
FT /evidence="ECO:0000255"
FT REGION 254..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..463
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 509..525
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 472..508
FT /evidence="ECO:0000255"
FT MOTIF 307..310
FT /note="CXXC"
FT MOTIF 526..534
FT /note="CX6CC"
FT MOTIF 626..629
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 254..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 440..441
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 620..621
FT /note="Cleavage; by viral protease p14"
FT /evidence="ECO:0000250"
FT LIPID 601
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 58
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 109..126
FT /evidence="ECO:0000250"
FT DISULFID 118..131
FT /evidence="ECO:0000250"
FT DISULFID 307..534
FT /note="Interchain (between SU and TM chains, or C-310 with
FT C-534); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 307..310
FT /evidence="ECO:0000250"
FT DISULFID 337..391
FT /evidence="ECO:0000250"
FT DISULFID 356..368
FT /evidence="ECO:0000250"
FT DISULFID 398..411
FT /evidence="ECO:0000250"
FT DISULFID 526..533
FT /evidence="ECO:0000250"
SQ SEQUENCE 636 AA; 69113 MW; DF6208F7EA968E2A CRC64;
MEGPAFSKPL KDKINPWGPL IILGILIRAG VSVQHDSPHQ VFNVTWRVTN LMTGQTANAT
SLLGTMTDAF PKLYFDLCDL IGDDWDETGL GCRTPGGRKR ARTFDFYVCP GHTVPTGCGG
PREGYCGKWG CETTGQAYWK PSSSWDLISL KRGNTPRNQG PCYDSSVVSS GIQGATPGGR
CNPLVLEFTD AGKKASWDGP KVWGLRLYRS TGIDPVTRFS LTRQVLNIGP RLPIGPNPVI
TGQLPPSRPV QIRLPRPPQP PPPGAASIVP ETAPPSQQPG TGDRLLNLVD GAYQALNLTS
PDKTQECWLC LVAGPPYYEG VAVLGTYSNH TSAPANCSVA SQHKLTLSEV TGQGLCVGAV
PKTHQALCNT TQKTSDGSYY LAAPAGTIWA CNTGLTPCLS TTVLNLTTDY CVLVELWPKV
TYHSPDYVYT QFEPGARFRR EPVSLTLALL LGGLTMGGIA AGVGTGTTAL VATQQFQQLQ
AAVHNDLKEV EKSITNLEKS LTSLSEVALQ NRRGLDLLFL KEGGLCAALK EECCFYADHT
GLVRDSMAKL RERLNQRQKL FESGQGWFEG LFNRSPWFTT LISTIMGPLI VLLLILLFGP
CILNRLVQFV KDRISVVQAL VLTQQYHQLK PIEYEP
