ENV_VILV2
ID ENV_VILV2 Reviewed; 991 AA.
AC P23423;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 23-FEB-2022, entry version 112.
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 / clone LV1-1KS2) (MVV) (Visna lentivirus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11744;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1847257; DOI=10.1016/0042-6822(91)90488-w;
RA Staskus K.A., Retzel E.F., Lewis E.D., Wietgrefe S.W., Silsby J.L., Cyr S.,
RA Rank J.M., Haase A.T., Fast D., Geiser P.T., Harty J.T., Kong S.H.,
RA Cook R., Lahti C.J., Neufeld T.P., Porter T.E., Shoop E., Zachow K.R.;
RT "Isolation of replication-competent molecular clones of visna virus.";
RL Virology 181:228-240(1991).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17532.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M60610; AAA17532.1; ALT_INIT; Unassigned_DNA.
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 3: Inferred from homology;
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..991
FT /note="Envelope glycoprotein gp160"
FT /id="PRO_0000239542"
FT CHAIN 107..664
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038741"
FT CHAIN 665..991
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038742"
FT TOPO_DOM 107..840
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 841..861
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 862..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 665..685
FT /note="Fusion peptide"
FT REGION 731..747
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 697..747
FT /evidence="ECO:0000255"
FT COILED 788..823
FT /evidence="ECO:0000255"
FT SITE 664..665
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT LIPID 864
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 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 705
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 17
FT /note="E -> D (in Ref. 1; AAA17532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 991 AA; 115016 MW; D8920FF4AEBA55A7 CRC64;
MTSKESKPSR TTWRGMEPPL RETWNQVLQE LVKRQQQEEE EQQGLVSGKK KSWVSIDLLG
TEGKDIKKVN IWEPCEKWFA QVVWGVLWVL QIVLWGCLMW EMRKGNQCQA EEVIALVSDP
GGFQRVQHVE TVPVTCVTKN FTQWGCQPEG AYPDPELEYR NISREILEEV YKQDWPWNTY
HWPLWQMENM RQWMKENEKE YKERTNKTKE DIDDLVAGRI RGRFCVPYPY ALLRCEEWCW
YPESINQETG HAEKIKINCT KAKAVSCTEK MPLAAVQRVY WEKEDEESMK FLNIKACNIS
LRCQDEEKSP GGCVQGYPIP KGAEIIPEAM KYLRGKKSRY GGIKDKNGEL KLPLSVRVWV
RMANLSGWVN GTPPYWNARI NGSTGINGTR WYGVGTLHHL GYNISSNPER GICDFTGELW
IGGDKFPYYY KPSWNCSQNW TGHPVWQVFR YLDMTEHMTS RCIQRPERHN ITVGNGTITG
NCSVTNWDGC NCTRSGNHLY NSTSGGLLVI ICRQNSTITG IMGTNTNWTT MWNIYQNCSK
CNNSSLDRTG KGTLGTVNDL KCSLPHRNES NKWTCAARTG RKGSQRDSLY IAGRDFWGRV
KAKYSCESNL GGLDSMMHQQ MLLQRYQVIR VRAYTYGVVE MPQSYMEAQG KNRRSRRNLQ
RKKRGIGLVI VLAIMAIIAA AGAGLGVANA VQQSYTRTAV QSLANATAAQ QEVLEASYAM
VQHIAKGIRI LEARVARVEA LVDRMMVYHE LDCWHYQHYC VTSTRSEVAN YVNWTRFKDN
CTWQQWEEEI EQHEGNLSLL LREAALQVHI AQRDARRIPD AWKAIQEAFN WSSWFSWLKY
VPWIIMGIVG LICFRILMCV ISMCLQAYKQ VKQIRYTQVT VVIEAPVELE EKQKRNGDGT
NGCASLEHER RTSHRSFIQI WRATWWAWKT SPWRHNWRTM PYITLLPILV IWQWMEENGW
NGENQHKKKK ERVDCQDREQ MPTLENDYVE L
