ENV_VILVK
ID ENV_VILVK Reviewed; 983 AA.
AC P35954;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 02-JUN-2021, entry version 120.
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 KV1772) (MVV) (Visna lentivirus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=36374;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8382414; DOI=10.1006/viro.1993.1106;
RA Andresson O.S., Elser J.E., Tobin G.J., Greenwood J.D., Gonda M.A.,
RA Georgsson G., Andresdottir V., Benediktsdottir E., Carlsdottir H.M.,
RA Maentylae E.O., Rafnar B., Palsson P.A., Casey J.W., Petursson G.;
RT "Nucleotide sequence and biological properties of a pathogenic proviral
RT molecular clone of neurovirulent visna virus.";
RL Virology 193:89-105(1993).
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; S55323; AAB25463.1; -; Genomic_DNA.
DR EMBL; L06906; AAA48362.1; -; Genomic_RNA.
DR PDB; 1JEK; X-ray; 1.50 A; A=693-732, B=775-808.
DR PDBsum; 1JEK; -.
DR SMR; P35954; -.
DR EvolutionaryTrace; P35954; -.
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 3D-structure; Cleavage on pair of basic residues; Coiled coil;
KW Disulfide bond; Glycoprotein; Host cell membrane; Host membrane;
KW Host-virus interaction; Lipoprotein; Membrane; Palmitate; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virus entry into host cell.
FT SIGNAL 1..106
FT /evidence="ECO:0000255"
FT CHAIN 107..983
FT /note="Envelope glycoprotein gp160"
FT /id="PRO_0000239543"
FT CHAIN 107..656
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038744"
FT CHAIN 657..983
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038745"
FT TOPO_DOM 107..832
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..853
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 854..983
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..677
FT /note="Fusion peptide"
FT REGION 723..739
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 689..739
FT /evidence="ECO:0000255"
FT COILED 780..815
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 656..657
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT LIPID 856
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 765
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 900
FT /note="R -> H (in Ref. 1; AAA48362)"
FT /evidence="ECO:0000305"
FT HELIX 694..731
FT /evidence="ECO:0007829|PDB:1JEK"
FT HELIX 776..807
FT /evidence="ECO:0007829|PDB:1JEK"
SQ SEQUENCE 983 AA; 113939 MW; E03BCC254EA78268 CRC64;
MASKESKPSR TTRRGMEPPL 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 MSLAAVQRVY WEKEDEESMK FLNIKACNIS
LRCQDEGKSP GGCVQGYPIP KGAEIIPEAM KYLRGKKSRY GGIKDKNGEL KLPLSVRVWV
RMANLSGWVN GTPPYWSARI NGSTGINGTR WYGIGTLHHL GCNISSNPER GICNFTGELW
IGGDKFPYYY TPSWNCSQNW TGHPVWHVFR YLDMTEHMTS RCIQRPKRHN ITVGNGTITG
NCSVTNWDGC NCTRSGNHLY NSTSGGLLVI ICRQNSTITG IMGTNTNWTT MWNIYQNCSR
CNNSSLDRTG SGTLGTVNNL KCSLPHRNES NKWTCKSQRD SYIAGRDFWG KVKAKYSCES
NLGGLDSMMH QQMLLQRYQV IRVRAYTYGV VEMPQSYMEA QGENKRSRRN LQRKKRGIGL
VIVLAIMAII AAAGAGLGVA NAVQQSYTRT AVQSLANATA AQQEVLEASY AMVQHIAKGI
RILEARVARV EALVDRMMVY QELDCWHYQH YCVTSTRSEV ANYVNWTRFK DNCTWQQWEE
EIEQHEGNLS LLLREAALQV HIAQRDARRI PDAWKAIQEA FNWSSWFSWL KYIPWIIMGI
VGLMCFRILM CVISMCLQAY KQVKQIRYTQ VTVVIEAPVE LEEKQKRNGD GTNGCASLER
ERRTSHRSFI QIWRATWWAW KTSPWRHNWR TMPYITLLPI LVIWQWMEEN GWNGENQHKK
KKERVDCQDR EQMPTLENDY VEL
