ENV_OMVVS
ID ENV_OMVVS Reviewed; 990 AA.
AC P16899;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 23-FEB-2022, entry version 113.
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 Ovine maedi visna related virus (strain South Africa) (SA-OMVV) (Ovine
OS lentivirus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11664;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2158181; DOI=10.1016/0042-6822(90)90428-t;
RA Querat G., Audoly G., Sonigo P., Vigne R.;
RT "Nucleotide sequence analysis of SA-OMVV, a visna-related ovine lentivirus:
RT phylogenetic history of lentiviruses.";
RL Virology 175:434-447(1990).
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; M34193; AAA46783.1; -; Genomic_DNA.
DR EMBL; M31646; AAA66817.1; -; Genomic_RNA.
DR PRIDE; P16899; -.
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..107
FT /evidence="ECO:0000255"
FT CHAIN 108..990
FT /note="Envelope glycoprotein gp160"
FT /id="PRO_0000239539"
FT CHAIN 108..662
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038732"
FT CHAIN 663..990
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038733"
FT TOPO_DOM 108..838
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 839..859
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 860..990
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 663..683
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 729..745
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT REGION 890..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
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 CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
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 550
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
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"
SQ SEQUENCE 990 AA; 114498 MW; 279B816BE55614F3 CRC64;
MASSKNMPSR ITQKSMEPPL RETWQQVVQE MVMRKQRDEE EKQNLVTGKE KSWVSIDLLG
TKQEGKRQKV NIWGPWEKWG IKIVWVMLWV IQLMLWGCLI WEMGKKHSCN AEEVIALVDD
PGGFQKVKYV ESVPVTCMTK NFTQWGCQPE GAYPDPDLEY RNISQDILEQ VYKQEWPWNT
YHWPLWQMEN MRQWMKENEK EYTSRNNKTK EDIDALLAGK IRGRFCVPYP FALLKCEEWC
WYPANINQET GHAQQIKINC TKAKAVSCTE QMPLAAVQRV YWEKEDEEGM KFMNIQACNE
SQLRCKTSPG GCVQGYPIPV GAEIIPESMK YLRGKKSPYG GIKDKNGELK LPLSVRVWVR
MANLSGWVNG TPPYWSARIK GSTGINGTRW YGIGTLHHLG YNISSNPEKG LCNFTKELWI
GGDRFQYQYK PSWNCSQNWT GYPVWHVFRY LDMTEHMTSR CVQRPLRHNI TVGNGTITGN
CSVTDWEGCN CTRSGNYLYN STTGGLLVII CRQNSTITGI MGTNTNWTTM WGIYKNCSEC
KNSTLDRTDN GTLGTVNNIN CSLPHYNESN KWTCAARNSK KKRDSLYIAG RDFWGRVKAL
YSCESNLGGL DGMMHQQMVL QKYQVIKVRA YTYGVVDMPK AYREKNMRNK RSTEISRPRK
KRGIGLVIVL AIMAIIAAAG AGLGVANAVQ QSYTRTAVQS LANATAAQQN VLEATYAMVQ
HVAKGVRILE ARVARVEAIV DRMMLYHELD CWHYQHYCVT STRTEVAQYV NWTRYKDNCT
WQQWEEEIEQ HEANLSLLLK EAALQVQIAQ RDAQRIPDVW KALQEAFDWS GWFSWLKYIP
WIVVCIVGVI CFRLLMCVIT MCLQAYRQVR EIRYTRVTVV IEAPVDLEEK QREERDGSSG
SENLEHEKRT SPRSFIQIWR ATVQAWKTSP WGKGWKKILY MTLLPLLTLQ IWMEETGWNG
DKRCKKKKER VDCQDRESMP AIENEYVELS
