ID A0A1W7HC61_9DELA Unreviewed; 488 AA. AC A0A1W7HC61; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 27-MAR-2024, entry version 25. DE RecName: Full=Envelope glycoprotein gp62 {ECO:0000256|ARBA:ARBA00040868}; DE AltName: Full=Env polyprotein {ECO:0000256|ARBA:ARBA00029888}; GN Name=env {ECO:0000313|EMBL:BAX34835.1}; OS Human T-cell leukemia virus type I. OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Deltaretrovirus; OC Primate T-lymphotropic virus 1. OX NCBI_TaxID=11908 {ECO:0000313|EMBL:BAX34835.1}; RN [1] {ECO:0000313|EMBL:BAX34835.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FHAM005 {ECO:0000313|EMBL:BAX34835.1}, and FHAM006 RC {ECO:0000313|EMBL:BAX34844.1}; RX PubMed=28420387; DOI=10.1186/s12977-017-0350-9; RA Nozuma S., Matsuura E., Kodama D., Tashiro Y., Matsuzaki T., Kubota R., RA Izumo S., Takashima H.; RT "Effects of host restriction factors and the HTLV-1 subtype on RT susceptibility to HTLV-1-associated myelopathy/tropical spastic RT paraparesis."; RL Retrovirology 14:26-26(2017). 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. {ECO:0000256|ARBA:ARBA00025621}. 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. CC {ECO:0000256|ARBA:ARBA00024648}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell CC membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane CC protein {ECO:0000256|ARBA:ARBA00004251}. Host cell membrane CC {ECO:0000256|ARBA:ARBA00004505}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004505}. Host cell membrane CC {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004402}. Membrane CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004650}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004650}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004563}. 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; LC192508; BAX34835.1; -; Genomic_DNA. DR EMBL; LC192509; BAX34844.1; -; Genomic_DNA. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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 CDD; cd09851; HTLV-1-like_HR1-HR2; 1. DR Gene3D; 1.10.287.210; -; 1. DR InterPro; IPR018154; TLV/ENV_coat_polyprotein. DR PANTHER; PTHR10424:SF77; BC035947 PROTEIN-RELATED; 1. DR PANTHER; PTHR10424; VIRAL ENVELOPE PROTEIN; 1. DR Pfam; PF00429; TLV_coat; 2. DR SUPFAM; SSF58069; Virus ectodomain; 1. PE 4: Predicted; KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Fusion of virus membrane with host cell membrane KW {ECO:0000256|ARBA:ARBA00022521}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|ARBA:ARBA00022521}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023139}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804}; KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022521}; KW Virion {ECO:0000256|ARBA:ARBA00022844}; KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00022521}. FT TRANSMEM 442..464 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 488 AA; 53810 MW; E492F406AF5A222E CRC64; MGKFLATLIL FFQFCPLILG DYSPSCCTLT IGVSSYHSKP CNPAQPVCSW TLDLPALSAD QALQPPCPNL VGYSSYHATY SLYLFPHWIK KPNRNGGGYY SASYSDPCSL KCPYLGCQSW TCPYTGAVSS PYWKFQQDVN FTQEVSRLNI NLHFSKCGFP FSLLVDAPGY DPIWFLNTEP SQLPPTAPPL LPHSNLDHIL EPSIPWKSKL LTLVQLTLQS TNYTCIVCID RASLSTWHVL YSPNVSVPSS SSTPLLYPSL ALPAPHLTLP FNWTHCFDPQ IQAIVSSPCH NSLILPPFSL SPVPTLGSRS RRAVPVAVWL VSALAMGAGV AGGITGSMSL ASGKSLLHEV DKDISQLTQA IVKNHKNLLK IAQYAAQNRR GLDLLFWEQG GLCKALQEQC CFLNITNSHV SILQERPPLE NRVLTGWGLN WDLGLSQWAR EALQTGITLV ALLLLVILAG PCILRQLRHL PSRVRYPHYS LINPESSL //