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 19-JAN-2010, entry version 63. 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; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; OC Gammaretrovirus; 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 RT of 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 CC cell by binding to its receptor. This interaction triggers the CC refolding of the transmembrane protein (TM) and is thought to CC activate its fusogenic potential by unmasking its fusion peptide. CC Fusion occurs at the host cell plasma membrane (By similarity). CC -!- FUNCTION: The transmembrane protein (TM) acts as a class I viral CC fusion protein. Under the current model, the protein has at least CC 3 conformational states: pre-fusion native state, pre-hairpin CC intermediate state, and post-fusion hairpin state. During viral CC and target cell membrane fusion, the coiled coil regions (heptad CC repeats) assume a trimer-of-hairpins structure, positioning the CC fusion peptide in close proximity to the C-terminal region of the CC ectodomain. The formation of this structure appears to drive CC apposition and subsequent fusion of viral and target cell CC membranes. Membranes fusion leads to delivery of the nucleocapsid CC into the cytoplasm (By similarity). CC -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of CC SU-TM heterodimers attached by noncovalent interactions or by a CC labile interchain disulfide bond (By similarity). CC -!- SUBCELLULAR LOCATION: Transmembrane protein: Virion membrane; CC Single-pass type I membrane protein (By similarity). Host cell CC membrane; Single-pass type I membrane protein (By similarity). CC -!- SUBCELLULAR LOCATION: Surface protein: Virion membrane; Peripheral CC membrane protein. Host cell membrane; Peripheral membrane protein CC (By similarity). Note=The surface protein is not anchored to the CC viral envelope, but associates with the extravirion surface CC through its binding to TM. Both proteins are thought to be CC concentrated at the site of budding and incorporated into the CC virions possibly by contacts between the cytoplasmic tail of Env CC and the N-terminus of Gag (By similarity). CC -!- SUBCELLULAR LOCATION: R-peptide: Host cell membrane; Peripheral CC membrane protein (By similarity). Note=The R-peptide is membrane- CC associated through its palmitate (By similarity). CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is CC present in many retroviral envelope proteins. Synthetic peptides CC derived from this relatively conserved sequence inhibit immune CC function in vitro and in vivo (By similarity). CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. CC Envelope glycoproteins are synthesized as a inactive precursor CC that is N-glycosylated and processed likely by host cell furin or CC by a furin-like protease in the Golgi to yield the mature SU and CC TM proteins. The cleavage site between SU and TM requires the CC minimal sequence [KR]-X-[KR]-R. The R-peptide is released from the CC C-terminus of the cytoplasmic tail of the TM protein upon particle CC formation as a result of proteolytic cleavage by the viral CC protease. Cleavage of this peptide is required for TM to become CC fusogenic (By similarity). CC -!- PTM: The transmembrane protein is palmitoylated (By similarity). CC -!- PTM: The R-peptide is palmitoylated (By similarity). 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; 499-587. DR GO; GO:0019898; C:extrinsic to membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C:viral capsid; IEA:InterPro. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0019058; P:viral infectious cycle; IEA:InterPro. DR InterPro; IPR002050; Env_polyprotein. DR InterPro; IPR008981; FMuLV_rcpt_bd. DR InterPro; IPR018154; TLV/ENV_coat_polyprotein. DR Gene3D; G3DSA:3.90.310.10; FMuLV_rcpt_bd; 1. DR PANTHER; PTHR10424; Env_polyprotein; 1. DR Pfam; PF00429; TLV_coat; 1. PE 3: Inferred from homology; KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond; KW Envelope protein; Fusion protein; Glycoprotein; Host cell membrane; KW Host membrane; Lipoprotein; Membrane; Palmitate; Signal; KW Transmembrane; Virion. FT SIGNAL 1 22 Potential. FT CHAIN 23 671 Envelope glycoprotein. FT /FTId=PRO_0000239558. FT CHAIN 23 470 Surface protein (By similarity). FT /FTId=PRO_0000040703. FT CHAIN 471 650 Transmembrane protein (By similarity). FT /FTId=PRO_0000040704. FT PEPTIDE 651 671 R-peptide (By similarity). FT /FTId=PRO_0000239559. FT TOPO_DOM 23 611 Extracellular (Potential). FT TRANSMEM 612 632 Potential. FT TOPO_DOM 633 671 Cytoplasmic (Potential). FT REGION 473 493 Fusion peptide (Potential). FT REGION 539 555 Immunosuppression (By similarity). FT COILED 501 550 Potential. FT COILED 560 596 Potential. FT MOTIF 336 339 CXXC. FT MOTIF 556 564 CX6CC. FT MOTIF 656 659 YXXL motif; contains endocytosis signal FT (By similarity). FT SITE 470 471 Cleavage; by host (By similarity). FT SITE 650 651 Cleavage; by viral protease (By FT similarity). FT LIPID 631 631 S-palmitoyl cysteine; by host (By FT similarity). FT CARBOHYD 169 169 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 281 281 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 326 326 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 331 331 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 355 355 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 358 358 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 415 415 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 435 435 N-linked (GlcNAc...); by host FT (Potential). FT DISULFID 121 142 By similarity. FT DISULFID 134 147 By similarity. 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 //