ID D0UGX9_9RETR Unreviewed; 864 AA.
AC D0UGX9;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Envelope glycoprotein {ECO:0000256|ARBA:ARBA00014571};
DE AltName: Full=Env polyprotein {ECO:0000256|ARBA:ARBA00029888};
GN Name=env {ECO:0000313|EMBL:ACY07749.1};
OS Equine infectious anemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11665 {ECO:0000313|EMBL:ACY07749.1};
RN [1] {ECO:0000313|EMBL:ACY07749.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19843328; DOI=10.1186/1742-4690-6-95;
RA Craigo J.K., Barnes S., Zhang B., Cook S.J., Howe L., Issel C.J.,
RA Montelaro R.C.;
RT "An EIAV field isolate reveals much higher levels of subtype variability
RT than currently reported for the equine lentivirus family.";
RL Retrovirology 6:95-95(2009).
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 -!- 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:0000256|ARBA:ARBA00011327}.
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}.
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DR EMBL; GQ855748; ACY07749.1; -; 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:0005198; F:structural molecule activity; IEA:InterPro.
DR CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR InterPro; IPR000328; GP41-like.
DR InterPro; IPR001361; Gp90_EIAV.
DR Pfam; PF00971; EIAV_GP90; 1.
PE 4: Predicted;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Viral envelope protein {ECO:0000313|EMBL:ACY07749.1};
KW Virion {ECO:0000313|EMBL:ACY07749.1}.
FT TRANSMEM 452..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..642
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 648..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 799..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 49..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 97763 MW; 026222A3014841E8 CRC64;
MVSIAFYGGI PGGISTPIAQ QHQEINTRDE DNAVFQPYCY IDGNKGKMAE GRDPRYSEDK
NLKEESKEDY DEEKGKKDWW KIGMLLLCLV GTTGSILWWY EGVTHTSFIG LVAMGGRLNG
SDLTNAIECW GSFPGCRPFT NYFRYGTNRT IYYDNDTATL LHAYQREVTY IYKTSCDDSD
HCQDYQCGQV YITGNNTLTI NKTENSTTFW DFEWLECNQT GNTKTILVPK DEMVNWGNDT
WRPKGCNETW ARVKHCPADL LYGIHPIRLC VQPPFFLTNF NNDSDSNNTV ISNCGPLIRL
GILEENKGVI SEYSNNNCSV AKKSFQRPDY SGTYQVPILY ECHLKLSSCE ENSTVSIIRY
EQNNVQYLLC RRNDTKTNYS CVVQTFGVIG QAHLELPRKN KRIENPRFTY YNCSINNKTE
LKSWKLVKTS GITPVPVSSE AKTGLIRHKR DFGISAIIAA IVAATAIAAS GTMAYIALTE
ANKLADVQNH TFEVENNTLN GMEIIEKQIH ILYAMVLQTH ADVQILKEKQ HIEETFNLIG
CIEQTHTFCH TGHPWNDSWG QLNDTTQWDE WVSRMESYNQ DILTTLHVAR NNLAQAMITF
NTPDSVAQFG KNIWDHIANW IPGLGASITK YIVMFLLIYL LLTSAPKILR ALLTTISGAG
SSASHFLKKR YHRRHVWQED NLDQGQYSIH LADVTAGLED EYKGRKYFRS NWNGESEGSN
KNMRSSKGLM REYGGSYTSL RTKKETIHPG GVTNTKKKVT GENPHQGSLN LEIQNDGGNI
YDCCIKAQEG TIAIPCCGFL LWLFWGLLII LGRLIGYVLR GLAKILMNVG KGLSMLLEVI
RRVLDYIGKA LNPASQHVSM PQYV
//
