ENV_FLVCA
ID ENV_FLVCA Reviewed; 410 AA.
AC Q02076;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 96.
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 Flags: Fragment;
GN Name=env;
OS Feline leukemia virus (strain C/FA27).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX NCBI_TaxID=103917;
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1326757; DOI=10.1073/pnas.89.18.8457;
RA Brojatsch J., Kristal B.S., Viglianti G.A., Khiroya R., Hoover E.A.,
RA Mullins J.I.;
RT "Feline leukemia virus subgroup C phenotype evolves through distinct
RT alterations near the N-terminus of the envelope surface glycoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8457-8461(1992).
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 -!- 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 (By similarity). {ECO:0000250}.
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DR EMBL; M89998; AAA43057.1; -; Genomic_DNA.
DR SMR; Q02076; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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; 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; Membrane;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT CHAIN <1..>410
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239563"
FT CHAIN <1..405
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040708"
FT CHAIN 406..>410
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040709"
FT TOPO_DOM <1..>410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 193..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 272..275
FT /note="CXXC"
FT COMPBIAS 207..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 405..406
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
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 350
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 85..107
FT /evidence="ECO:0000250"
FT DISULFID 99..112
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 410
SQ SEQUENCE 410 AA; 45218 MW; C6115A36CEF2905B CRC64;
PHQIYNVTWV ITNVQTNTQA NATSMLGTLT DAYPTLHVDL CDLVGNTWEP IVPDLRGWAS
YSSSKYGCKT ADRKKQQQTY PFYVCPGHAP SLGPKGTHCG GAQDGFCAAW GCETTGEAWW
KPTSSWDYIT VKRGSSQDNS CEGKCNPLVL QFTQKGRQAS WDGPKMWGLR LYRTGYDPIA
LFTVSRQVST ITPPQAMGPN LVLPDRKPPS RQSQTGSKVA TQRPQTNESA PRSIAPTTMG
PKRIGTGDRL INLVQGTYLA LNATDPNKTK DCWLCLVSRP PYYEGIAILG NYSNQTNPPP
SCLSIPQHKL TISEVSGQGL CIGTVPKTHQ ALCNETQQGH TGAHYLAAPN GTYWACNTGL
TPCISMAVLN WTSDFCVLIE LWPRVTYHQP EYVYTHFAKA VRFRREPISL
