ENV_VILV
ID ENV_VILV Reviewed; 982 AA.
AC P03379;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 123.
DE RecName: Full=Envelope glycoprotein gp160;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE AltName: Full=Glycoprotein 135;
DE Short=gp135;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE AltName: Full=Glycoprotein 46;
DE Short=gp46;
DE Flags: Precursor;
GN Name=env;
OS Maedi visna virus (strain 1514) (MVV) (Visna lentivirus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11742;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2410140; DOI=10.1016/s0092-8674(85)80132-x;
RA Sonigo P., Alizon M., Staskus K., Klatzmann D., Cole S., Danos O.,
RA Retzel E., Tiollais P., Haase A., Wain-Hobson S.;
RT "Nucleotide sequence of the visna lentivirus: relationship to the AIDS
RT virus.";
RL Cell 42:369-382(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2824836; DOI=10.1128/jvi.61.12.4046-4054.1987;
RA Braun M.J., Clements J.E., Gonda M.A.;
RT "The visna virus genome: evidence for a hypervariable site in the env gene
RT and sequence homology among lentivirus envelope proteins.";
RL J. Virol. 61:4046-4054(1987).
RN [3]
RP CHARACTERIZATION OF THE TRANSMEMBRANE PROTEIN, AND FUNCTION IN FUSION.
RX PubMed=11447278; DOI=10.1073/pnas.151254798;
RA Malashkevich V.N., Singh M., Kim P.S.;
RT "The trimer-of-hairpins motif in membrane fusion: Visna virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8502-8506(2001).
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 noncovalent interactions or by a labile
CC interchain disulfide bond. {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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- PTM: The transmembrane protein is palmitoylated. {ECO:0000250}.
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DR EMBL; M10608; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; M51543; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; A15114; CAA01216.1; -; Unassigned_RNA.
DR BindingDB; P03379; -.
DR ChEMBL; CHEMBL5827; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW Glycoprotein; Host cell membrane; Host membrane; Host-virus interaction;
KW Lipoprotein; Membrane; Palmitate; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Virion; Virus entry into host cell.
FT SIGNAL 1..106
FT /evidence="ECO:0000255"
FT CHAIN 107..982
FT /note="Envelope glycoprotein gp160"
FT /id="PRO_0000239540"
FT CHAIN 107..656
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038735"
FT CHAIN 657..982
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038736"
FT TOPO_DOM 107..831
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 832..852
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 853..982
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 657..677
FT /note="Fusion peptide"
FT REGION 723..738
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 689..738
FT /evidence="ECO:0000255"
FT COILED 779..814
FT /evidence="ECO:0000255"
FT SITE 656..657
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT LIPID 855
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 787
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 12
FT /note="T -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="S -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="K -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 640..641
FT /note="ER -> AQ (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="R -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 982 AA; 113978 MW; 7D78BAE6E22BF53F CRC64;
MASKESKPSR TTWRDMEPPL RETWNQVLQE LVKRQQQEEE EQQGLVSGKK KSWVSIDLLG
TEGKDIKKVN IWEPCEKWFA QVVWGVLWVL QIVLWGCLMW EVRKGNQCQA EEVIALVSDP
GGFQRVQHVE TVPVTCVTKN FTQWGCQPEG AYPDPELEYR NISREILEEV YKQDWPWNTY
HWPLWQMENM RQWMKENEKE YKERTNKTKE DIDDLVAGRI RGRFCVPYPY ALLRCEEWCW
YPESINQETG HAEKIKINCT KAKAVSCTEK MPLAAVQRVY WEKEDEESMK FLNIKACNIS
LRCQDEGKSP GGCVQGYPIP KGAEIIPEAM KYLRGKKSRY GGIKDKNGEL KLPLSVRVWV
RMANLSGWVN GTPPYWSARI NGSTGINGTR WYGVGTLHHL GYNISSNPEG GICNFTGELW
IGGDRFPYYY KPSWNCSQNW TGHPVWHVFR YLDMTEHMTS RCIQRPKRHN ITVGNGTITG
NCSVTNWDGC NCTRSGNHLY NSTSGGLLVI ICRQNSTITG IMGTNTNWTT MWNIYQNCSR
CNNSSLDRTG SGTLGTVNNL KCSLPHRNES NKWTCKSQRD SYIAGRDFWG KVKAKYSCES
NLGGLDSMMH QQMLLQRYQV IRVRAYTYGV VEMPQSYMEE RGENRRSRRN LQRKKRGIGL
VIVLAIMAII AAAGAGLGVA NAVQQSYTRT AVQSLANATA AQQEVLEASY AMVQHIAKGI
RILEARVARV EALVDMMVYQ ELDCWHYQHY CVTSTRSEVA NYVNWTRFKD NCTWQQWEEE
IEQHEGNLSL LLREAALQVH IAQRDARRIP DAWKAIQEAF NWSSWFSWLK YIPWIIMGIV
GLMCFRILMC VISMCLQAYK QVKQIRYTQV TVVIEAPVEL EEKQKRNGDG TNGCASLEHE
RRTSHRSFIQ IWRATWWAWK TSPWRHNWRT MPYITLLPIL VIWQWMEENG WNGENQHKKK
KERVDCQDRE QMPTLENDYV EL
