ENV_FSVSM
ID ENV_FSVSM Reviewed; 645 AA.
AC P21445;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 104.
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 sarcoma virus (strain SM) (Sm-FeSV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=11779;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2823466; DOI=10.1016/0042-6822(87)90194-2;
RA Guilhot S., Hampe A., D'Auriol L., Galibert F.;
RT "Nucleotide sequence analysis of the LTRs and env genes of SM-FeSV and GA-
RT FeSV.";
RL Virology 161:252-258(1987).
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; M23025; AAA74004.1; -; Genomic_DNA.
DR PIR; A33741; VCMVSS.
DR SMR; P21445; -.
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..36
FT /evidence="ECO:0000255"
FT CHAIN 37..645
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239572"
FT CHAIN 37..448
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040727"
FT CHAIN 449..628
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040728"
FT PEPTIDE 629..645
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239573"
FT TOPO_DOM 37..589
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 238..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..471
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 517..533
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 479..528
FT /evidence="ECO:0000255"
FT COILED 538..574
FT /evidence="ECO:0000255"
FT MOTIF 315..318
FT /note="CXXC"
FT MOTIF 534..542
FT /note="CX6CC"
FT COMPBIAS 249..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 448..449
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 628..629
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 609
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 128..150
FT /evidence="ECO:0000250"
FT DISULFID 142..155
FT /evidence="ECO:0000250"
FT DISULFID 315..542
FT /note="Interchain (between SU and TM chains, or C-318 with
FT C-542); in linked form"
FT /evidence="ECO:0000250"
FT DISULFID 315..318
FT /evidence="ECO:0000250"
FT DISULFID 534..541
FT /evidence="ECO:0000250"
SQ SEQUENCE 645 AA; 71594 MW; 4E6DB90A00A43B21 CRC64;
MEGPTHPKPF KDKTFSWDLI ILVGVVRVLL RLDVGMANPS PHQVYNVTWV ITNVQTNSQA
NATSMLGTLT DAYPTLHVDL CDLVGDTWEP IVLDPSNVKH GARYSSSKYG CKTTDRKKQQ
QTYPFYVCPG HAPSMGPKGT HCGGAHDGFC AAWGCETTGE AWWKPTSSWD YITVKRGSSQ
DTSCDKNCNP LVLQFTQKGR QASWDGPKLW GLRLYRTGYD PIALFSVSRQ VSTIMPPQAM
GPNLVLPEQK PPSRQSQTKS KVATQKPQTN GTTPRSVAPA TMSPKRIGTR DRLINLVQGT
YLALNATDPN KTKDCWLCLV SRPPYYEGIA ILGNYSNQTN PPPSCLSTPQ HKLTISEVSG
QGLCIGTVPR THQALCNKTQ QGHTGAHYLA APNGTYWACN TGLTPCISMA VLNWTSDFCV
LIELWPRVTY HQPEYIYTHF DKAVRFRREP ISLTVALMLG GLTVGGIAAG VGTGTKALLE
TAQFRQLQIA MHTDIQALEE SISALEKSLT SLSEVVLQNR RGLDILFLQG GGLCAALKEE
CCFYADHTGL VRDNMAKLRE RLKQRQQLFD SQQGWFEGWF NKSPWFTTLI SSIMGPLLIL
LLILLFGPCI LNRLVQFVKD RISVVQALIL TQQYQQIQQY DPDRP
