ID K7WSH4_9RETR Unreviewed; 258 AA.
AC K7WSH4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Envelope glycoprotein {ECO:0000256|ARBA:ARBA00014571};
DE AltName: Full=Env polyprotein {ECO:0000256|ARBA:ARBA00029888};
DE Flags: Fragment;
GN Name=env {ECO:0000313|EMBL:AFW99490.1};
OS Equine infectious anemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11665 {ECO:0000313|EMBL:AFW99490.1};
RN [1] {ECO:0000313|EMBL:AFW99490.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H3 {ECO:0000313|EMBL:AFW99490.1};
RX PubMed=23175240; DOI=10.1099/vir.0.047191-0;
RA Quinlivan M., Cook F., Kenna R., Callinan J.J., Cullinane A.;
RT "Genetic characterization by composite sequence analysis of a new
RT pathogenic field strain of equine infectious anemia virus from the 2006
RT outbreak in Ireland.";
RL J. Gen. Virol. 94:612-622(2013).
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}.
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; JX480809; AFW99490.1; -; 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.
DR Pfam; PF00517; GP41; 1.
DR SUPFAM; SSF58069; Virus ectodomain; 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:AFW99490.1};
KW Virion {ECO:0000313|EMBL:AFW99490.1}.
FT TRANSMEM 52..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..251
FT /note="Retroviral envelope protein GP41-like"
FT /evidence="ECO:0000259|Pfam:PF00517"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFW99490.1"
FT NON_TER 258
FT /evidence="ECO:0000313|EMBL:AFW99490.1"
SQ SEQUENCE 258 AA; 29079 MW; FA7A7DBD5C271E08 CRC64;
KRIATPNFSH YNCTVNNKTE MQEWQLVKTS GITPIPISSR NEKGLIRHKR DFGLSAIVAA
IVAATAIAAS TTMSYIALTE ASKIQDVVNH TLNVENNTLS ATEMIEKQVS ILYAMILQTH
ADVQLLKEKQ QVEETFNLIG CIEKTHTFCH TGHPWNNSWG LLNDTTQWDT WVGEMEKYNQ
DILTTLHVAR NNLEQAMITF NTPDSIAQFG KNIWDHIANW IPGLGASIIK YIVLFLIIYV
VLTSMPKLLR HLLTTMTG
//
