ENV_VILV1
ID ENV_VILV1 Reviewed; 989 AA.
AC P23422;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 23-FEB-2022, entry version 109.
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 LV1-1KS1) (MVV) (Visna lentivirus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11743;
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}.
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DR EMBL; M60609; AAA17527.1; ALT_SEQ; Unassigned_RNA.
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..989
FT /note="Envelope glycoprotein gp160"
FT /id="PRO_0000239541"
FT CHAIN 107..662
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038738"
FT CHAIN 663..989
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038739"
FT TOPO_DOM 107..838
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 839..859
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 860..989
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 663..683
FT /note="Fusion peptide"
FT REGION 729..745
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT COILED 695..745
FT /evidence="ECO:0000255"
FT COILED 786..821
FT /evidence="ECO:0000255"
FT SITE 662..663
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT LIPID 862
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 551
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 703
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 778
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 989 AA; 114798 MW; 7808E92B8E3FF8A0 CRC64;
MTSKESKPSR TTWRGMEPPL RETWNQVLQE LVKRQQQEEE EQQGLVSGKK KSWVSIDLLG
TEGKDIKKVN IWEPCEKWFA QVIWGVLWVL QIVLWGCLMW EMRKGNQCQA 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 GTPPYWSARV NGSTGINGTR WYGVGTLHHL GYNISSNPER GICDFTGELW
IGGDKFPYYY KPSWNCSQNW TGHPVWQVFR YLDMTEHMTS RCIQRPERHN ITVGNGTITG
NCSVTNWDGC NCTRSGNHLY NSTSGGLLVI ICRQNSTITG IMGTNTNWTT MWNIYQNCSK
CNNSSLDRTG NGTLGTVNDL KCSLPHRNES NKWTCAARRK GSRRDSLYIA GRDFWGRVKA
KYSCESNLGG LDSMMHQQML LQRYQVIRVR AYTYGVVEMP QSYMEAQGEN RRSRRNLQRK
KRGIGLVIVL AIMAIIAAAG AGLGVANAVQ QSYTRTAVQS LANATAAQQE VLEASYAMVQ
HIAKGIRILE ARVARVEALV DRMMVYHELD CWHYQHYCVT STRSEVANYV NWTRFKDNCT
WQQWEEEIEQ HEGNLSLLLR EAALQVHIAQ RDARRIPDAW KAIQEAFNWS SWFSWLKYIP
WIIMGIVGLI CFRILMCVIS MCLQAYKQVK QIRYTQVTVV IEAPVELEEK QKRNGDGTNG
CASLERERRT SHRSFIQIWR ATWWAWKTSP WRHSWRTMPY ITLLPMLVIW QWMEENGWNG
ENQHKKKKER VDCQDREQMP TLENDYVEL
