ID E2E2G0_9RETR Unreviewed; 709 AA.
AC E2E2G0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Envelope glycoprotein {ECO:0000256|ARBA:ARBA00014571};
DE AltName: Full=Env polyprotein {ECO:0000256|ARBA:ARBA00029888};
GN Name=env {ECO:0000313|EMBL:ADK35795.1};
OS Equine infectious anemia virus.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11665 {ECO:0000313|EMBL:ADK35795.1};
RN [1] {ECO:0000313|EMBL:ADK35795.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDDV-5 {ECO:0000313|EMBL:ADK35795.1};
RX PubMed=21136127; DOI=10.1007/s00705-010-0877-8;
RA Wang X., Wang S., Lin Y., Jiang C., Ma J., Zhao L., Lv X., Wang F.,
RA Shen R., Kong X., Zhou J.;
RT "Genomic comparison between attenuated Chinese equine infectious anemia
RT virus vaccine strains and their parental virulent strains.";
RL Arch. Virol. 156:353-357(2011).
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; GU385353; ADK35795.1; -; 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.
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:ADK35795.1};
KW Virion {ECO:0000313|EMBL:ADK35795.1}.
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 618..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 472..650
FT /note="Retroviral envelope protein GP41-like"
FT /evidence="ECO:0000259|Pfam:PF00517"
SQ SEQUENCE 709 AA; 80415 MW; 94E21E4D7381DBC2 CRC64;
MVSIAFYGGI PGGISTPITQ QTESTDTQKG DHMVYQPYCY NDSYKEEMAE ARDTRYQEEM
NRKEDKEDKR RNNWWKIGMF LLCLLGTTGG FLWWYERQQH SYYIGLVTIG GRLNGSGMTS
AIECWGSFPG CRSFTNYFSY ETNRTVSRDN NTATLLDAYQ REVTNIYRTS CVDSDHCQEY
KCKQVQLEKN SNNIIMNNCS NNSCEEFWGF SWLECNQTEN AITILVPEVE MQQSKNTWIP
KGCKKTWARV KHCPMDLLYG INRIRMCVQP PFFCFKQNDT SNNTGILSNC GPLVFLGILE
DNKAAIQNGS CTVHRTNINR PDYSGFYQVP IFYICNLTGL QSCNNGSIIS IIMSEPNNVQ
YLLCNTSNTN STSNANVSCV VQSFGVIGQA HVALPRKNKR LQSPKFAQYN CTINNKTELR
QWQLVKTSGI TPLPISSTAN TGLVRHKRDF GISAIIAAIV AATAIAASAT MSYIALTEVN
KLDSVQNHTF KVENNTINSM ELTEEQIHIL YAMVLQTHAD VQLLKEQQKI EETFNLIGCI
ERSHTFCHTG HPWNESWGQL NDSTQWDDWV NKMENLNHDI LTTLHTARNN LEQSMITFNT
PDSIAQFGKN IWSHVANWIP GLGASIIKYI VLLLLVYVLL TSAPKILRGL LATMSGAGSS
ASRYLRKRYH HRHASRGDIW AQVQYHAYLA DETHGSGDKS NMRKFSRNN
//
