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}. 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; 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 //