ENV_FENV1
ID ENV_FENV1 Reviewed; 671 AA.
AC P31791; Q28416;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 98.
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 endogenous virus ECE1.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC unclassified Gammaretrovirus.
OX NCBI_TaxID=11766;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Moehring R., Drescher B., Riedel H., Bauer D., Rohde K., Beyer W.,
RA Rosenthal S.;
RT "The exogenous RD-114 and the related endogenous proviral element ECE1 of
RT domestic cat differ in their env genes.";
RL Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases.
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 noncovalent interactions or by a labile
CC interchain disulfide bond. {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 transmembrane protein is palmitoylated. {ECO:0000250}.
CC -!- PTM: The R-peptide is palmitoylated. {ECO:0000250}.
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DR EMBL; X51929; CAB38567.1; -; Genomic_DNA.
DR PIR; S12815; VCMVCE.
DR SMR; P31791; -.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..671
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239558"
FT CHAIN 23..470
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040703"
FT CHAIN 471..650
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000040704"
FT PEPTIDE 651..671
FT /note="R-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000239559"
FT TOPO_DOM 23..611
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..671
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 265..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..493
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 539..555
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 501..550
FT /evidence="ECO:0000255"
FT COILED 560..596
FT /evidence="ECO:0000255"
FT MOTIF 336..339
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 290..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 470..471
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 650..651
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000250"
FT LIPID 631
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
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 355
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 121..142
FT /evidence="ECO:0000250"
FT DISULFID 134..147
FT /evidence="ECO:0000250"
SQ SEQUENCE 671 AA; 75152 MW; EA9847024EF794A0 CRC64;
MKPPAGMVFL WVLTSLGAGI GAKIVKEGNP HQVYTLTWQI YSQSGEVVWE VQGNHALNTW
WPALTPDFCQ LAAGLDTWDI PDRSPKNLET SMEGTSQQLT PQGCSKPWKR CALTERDFYV
CPRDNRDRAT AHRCGGYEEY FCSAWGCETT GDAYWQPTST WDLITITRNY TKPDSCDDRV
ERERKTSRHW RDPLSLPLKI TFTDSGKRAL GWQTGYTWGL RWYLPGKDRG IILKIKLKID
TITQTVGPNL VLADQKTPVQ LAIPVQPPRA PTQTPRVNPV NSTLSPSLGY PAPAPGPRPP
YPTSPSRPGT GDRLLNLVQG VYLTLNLTAP NQTQDCWLCL TAKPPYYQGV AIIGNFTNHT
NAPLRCSTTP RHGLTLTEVT GYGLCIGKIP PSHQNLCSQT VPSVGQGPYY LTAPNGTYWV
CNTGLTPCIS LQILNDTADY CILIELWPKI FYHDSEYIYG HYEPGGRFRR DPVSLTVALL
LGGLTMGSLA AGIGTGTAAL IETNQFKQLQ IAMHSDIQAL EESISALERS LISLSEVVLQ
NRRGLDLLFL QEGGLCAALK EECCFYADHT GIVRDSMAKL RERFKQRQKL FESQQGWFEG
WYNKSPWFTT LVSSLMVPLI LLLLILMFGP CILNHLLQFI RERLSVIQAL VLTQQYHQLR
QFDAERPDAI E
