ID   ENV_BAEVM               Reviewed;         563 AA.
AC   P10269;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 111.
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=Glycoprotein p20E;
DE   Contains:
DE     RecName: Full=R-peptide;
DE     AltName: Full=p2E;
DE   Flags: Precursor;
GN   Name=env;
OS   Baboon endogenous virus (strain M7).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Baboon endogenous virus.
OX   NCBI_TaxID=11764;
OH   NCBI_TaxID=9554; Papio (baboons).
OH   NCBI_TaxID=9565; Theropithecus gelada (Gelada baboon).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kato S., Matsuo K., Nishimura N., Takahashi N., Takano T.;
RT   "The entire nucleotide sequence of baboon endogenous virus DNA: a chimeric
RT   genome structure of murine type C and simian type D retroviruses.";
RL   Jpn. J. Genet. 62:127-137(1987).
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of SU-
CC       TM heterodimers attached by a labile interchain disulfide bond.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC       cell membrane {ECO:0000250}; Single-pass type I membrane protein
CC       {ECO:0000250}. Note=It is probably concentrated at the site of budding
CC       and incorporated into the virions possibly by contacts between the
CC       cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Host cell membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The
CC       surface protein is not anchored to the viral envelope, but associates
CC       with the extravirion surface through its binding to TM. It is probably
CC       concentrated at the site of budding and incorporated into the virions
CC       possibly by contacts between the cytoplasmic tail of Env and the N-
CC       terminus of Gag (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [R-peptide]: Host cell membrane; Peripheral
CC       membrane protein. Note=The R-peptide is membrane-associated through its
CC       palmitate. {ECO:0000250}.
CC   -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC       many retroviral envelope proteins. Synthetic peptides derived from this
CC       relatively conserved sequence inhibit immune function in vitro and in
CC       vivo (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The YXXL motif is involved in determining the exact site of
CC       viral release at the surface of infected mononuclear cells and promotes
CC       endocytosis.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC       Envelope glycoproteins are synthesized as an inactive precursor that is
CC       N-glycosylated and processed likely by host cell furin or by a furin-
CC       like protease in the Golgi to yield the mature SU and TM proteins. The
CC       cleavage site between SU and TM requires the minimal sequence [KR]-X-
CC       [KR]-R. The R-peptide is released from the C-terminus of the
CC       cytoplasmic tail of the TM protein upon particle formation as a result
CC       of proteolytic cleavage by the viral protease. Cleavage of this peptide
CC       is required for TM to become fusogenic (By similarity). {ECO:0000250}.
CC   -!- PTM: The CXXC motif is highly conserved across a broad range of
CC       retroviral envelope proteins. It is thought to participate in the
CC       formation of a labile disulfide bond possibly with the CX6CC motif
CC       present in the transmembrane protein. Isomerization of the intersubunit
CC       disulfide bond to an SU intrachain disulfide bond is thought to occur
CC       upon receptor recognition in order to allow membrane fusion (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
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DR   EMBL; D10032; BAA00924.1; -; Genomic_DNA.
DR   EMBL; X05470; CAA29028.1; -; Genomic_DNA.
DR   PIR; JT0262; VCMVM7.
DR   RefSeq; YP_009109691.1; NC_022517.1.
DR   SMR; P10269; -.
DR   GlyCosmos; P10269; 11 sites, No reported glycans.
DR   GeneID; 22318530; -.
DR   KEGG; vg:22318530; -.
DR   Proteomes; UP000007443; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF75; ENDOGENOUS RETROVIRUS GROUP S71 MEMBER 1 ENV POLYPROTEIN-RELATED; 1.
DR   PANTHER; PTHR10424; VIRAL ENVELOPE PROTEIN; 1.
DR   Pfam; PF00429; TLV_coat; 1.
DR   SUPFAM; SSF58069; Virus ectodomain; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW   Fusion of virus membrane with host cell membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW   Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..563
FT                   /note="Envelope glycoprotein"
FT                   /id="PRO_0000239549"
FT   CHAIN           19..376
FT                   /note="Surface protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040687"
FT   CHAIN           377..546
FT                   /note="Transmembrane protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000040688"
FT   PEPTIDE         547..563
FT                   /note="R-peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000239550"
FT   TOPO_DOM        19..503
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        504..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        525..563
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          380..400
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000255"
FT   REGION          440..456
FT                   /note="Immunosuppression"
FT                   /evidence="ECO:0000250"
FT   COILED          401..451
FT                   /evidence="ECO:0000255"
FT   COILED          461..497
FT                   /evidence="ECO:0000255"
FT   MOTIF           236..239
FT                   /note="CXXC"
FT   MOTIF           457..465
FT                   /note="CX6CC"
FT   MOTIF           552..555
FT                   /note="YXXL motif; contains endocytosis signal"
FT                   /evidence="ECO:0000250"
FT   SITE            376..377
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250"
FT   SITE            546..547
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250"
FT   LIPID           527
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        236..465
FT                   /note="Interchain (between SU and TM chains, or C-239 with
FT                   C-465); in linked form"
FT                   /evidence="ECO:0000250"
FT   DISULFID        236..239
FT                   /evidence="ECO:0000250"
FT   DISULFID        457..464
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   563 AA;  61879 MW;  9573137DC4620BB7 CRC64;
     MGFTTKIIFL YNLVLVYAGF DDPRKAIELV QKRYGRPCDC SGGQVSEPPS DRVSQVTCSG
     KTAYLMPDQR WKCKSIPKDT SPSGPLQECP CNSYQSSVHS SCYTSYQQCR SGNKTYYTAT
     LLKTQTGGTS DVQVLGSTNK LIQSPCNGIK GQSICWSTTA PIHVSDGGGP LDTTRIKSVQ
     RKLEEIHKAL YPELQYHPLA IPKVRDNLMV DAQTLNILNA TYNLLLMSNT SLVDDCWLCL
     KLGPPTPLAI PNFLLSYVTR SSDNISCLII PPLLVQPMQF SNSSCLFSPS YNSTEEIDLG
     HVAFSNCTSI TNVTGPICAV NGSVFLCGNN MAYTYLPTNW TGLCVLATLL PDIDIIPGDE
     PVPIPAIDHF IYRPKRAIQF IPLLAGLGIT AAFTTGATGL GVSVTQYTKL SNQLISDVQI
     LSSTIQDLQD QVDSLAEVVL QNRRGLDLLT AEQGGICLAL QEKCCFYVNK SGIVRDKIKT
     LQEELERRRK DLASNPLWTG LQGLLPYLLP FLGPLLTLLL LLTIGPCIFN RLTAFINDKL
     NIIHAMVLTQ QYQVLRTDEE AQD
//