ENV_FLVSA
ID ENV_FLVSA Reviewed; 639 AA.
AC P06752;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 106.
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 Feline leukemia virus (strain C/Sarma).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=103919;
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3018287; DOI=10.1128/jvi.60.1.242-250.1986;
RA Riedel N., Hoover E.A., Gasper P.W., Nicolson M.O., Mullins J.I.;
RT "Molecular analysis and pathogenesis of the feline aplastic anemia
RT retrovirus, feline leukemia virus C-Sarma.";
RL J. Virol. 60:242-250(1986).
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 extravirion 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 -!- 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}.
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DR EMBL; M14331; AAA43049.1; -; Genomic_DNA.
DR PIR; A29013; VCMVSA.
DR PIR; A46165; A46165.
DR SMR; P06752; -.
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; 1.
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..34
FT /evidence="ECO:0000255"
FT CHAIN 35..639
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239568"
FT CHAIN 35..442
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040716"
FT CHAIN 443..622
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040717"
FT PEPTIDE 623..639
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239569"
FT TOPO_DOM 35..583
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 232..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..465
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 511..527
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 473..522
FT /evidence="ECO:0000255"
FT COILED 532..568
FT /evidence="ECO:0000255"
FT MOTIF 309..312
FT /note="CXXC"
FT MOTIF 528..536
FT /note="CX6CC"
FT COMPBIAS 243..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 442..443
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 622..623
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 603
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:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 122..144
FT /evidence="ECO:0000250"
FT DISULFID 136..149
FT /evidence="ECO:0000250"
FT DISULFID 309..536
FT /note="Interchain (between SU and TM chains, or C-312 with
FT C-536); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 309..312
FT /evidence="ECO:0000250"
FT DISULFID 528..535
FT /evidence="ECO:0000250"
SQ SEQUENCE 639 AA; 71162 MW; A309B64AC8EC74E4 CRC64;
MESPTHPKPS KDKTFPWNLV FLVGILFQID MGMANPSPHQ VYNVTWVITN VQTNSRANAT
SMLGTLTDAY PTLYVDLCDL VGDTWEPIAP DPRSWARYSS STHGCKTTDR KKQQQTYPFY
VCPGHAPSMG PKGTYCGGAQ DGFCAAWGCE TTGEAWWKPT SSWDYITVKR GSNQDNSCKG
KCNPLVLQFT QKGRQASWDR PKMWGLRLYR SGYDPIALFS VSRQVMTITP PQAMGPNLVL
PDQKPPSRQS QTKSKVTTQR PQITSSTPRS VASATMGPKR IGTGDRLINL VQGTYLALNA
TDPNKTKDCW LCLVSRPPYY EGIAVLGNYS NQTNPPPSCL STPQHKLTIS EVSGQGLCIG
TVPKTHQALC KKTQKGHKGT HYLAAPNGTY WACNTGLTPC ISMAVLNWTS DFCVLIELWP
RVTYHQPEYI YTHFDKAVRF RREPISLTVA LMLGGLTVGG IAAGVGTGTK ALLETAQFRQ
LQIAMHTDIQ ALEESISALE KSLTSLSEVV LQNRRGLDIL FLQEGGLCAA LKEECCFYAD
HTGLVRDNMA KLRERLKQRQ QLFDSQQGWF EGWFNKSPWF TTLISSIMGP LLILLLILLL
GPCILNRLVQ FVKDRISVVQ ALILTQQYQQ IQQYDSDRP
