ENV_JEMBR
ID ENV_JEMBR Reviewed; 781 AA.
AC Q82857;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 82.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 62;
DE Short=gp62;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 40;
DE Short=gp40;
GN Name=env;
OS Jembrana disease virus (JDV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=36370;
OH NCBI_TaxID=9906; Bos javanicus (Wild banteng).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Tabanan/87;
RX PubMed=9049370; DOI=10.1099/0022-1317-76-7-1637;
RA Chadwick B.J., Coelen R.J., Wilcox G.E., Sammels L.M., Kertayadnya G.;
RT "Nucleotide sequence analysis of Jembrana disease virus: a bovine
RT lentivirus associated with an acute disease syndrome.";
RL J. Gen. Virol. 76:1637-1650(1995).
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 non-covalent 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U21603; AAA64390.1; -; Genomic_RNA.
DR Proteomes; UP000246436; Genome.
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:0005198; F:structural molecule activity; IEA:InterPro.
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.
DR CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR InterPro; IPR008411; BIV_Surface_Envelope.
DR InterPro; IPR000328; GP41-like.
DR Pfam; PF05858; BIV_Env; 2.
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 Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..781
FT /note="Envelope glycoprotein"
FT /id="PRO_0000272346"
FT CHAIN 1..422
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000272347"
FT CHAIN 423..781
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000272348"
FT TOPO_DOM 1..597
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 619..781
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 423..443
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 482..498
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT REGION 634..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 422..423
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 781 AA; 88837 MW; 9DCF711A8F09E6DF CRC64;
MMEEGRKEEP EERGEKSTMR DLLQRAVDKG HLTAREALDR WTLEDHGEIH PWIILFCFAG
AIGVIGGWGL RGELNVCMLI VLVVLVPIYW GIGEAARNID SLDWKWIRKV FIVIIFVLVG
LLGGCSAQRQ HVAMLLSPPG IRLPSTVDIP WFCISNAPIP DCVHWTVQKP DQKHQQIENV
MELQEVLDNA TFFEVPDLFD RVYLELARLD ANSTGVPVNI PPTGISQVKG DCSTGDIQGM
NETLSTRGTL GERTFLSIRP GGWFTNTTVW FCVHWPFGFI QRKENLSEGS AQVRNCLDPI
NVTEPRVANY SYCPLEYKGK NYINKGLKCV GGRVDLSSNP EQHTDLLACG TFCQNFRNCD
MVSRDILIGY HPSQQKQHIY INHTFWEQAN TQWILVQVPN YGFVPVPDTE RPWKGGKPRG
KRAVGMVIFL LVLAIMAMTA SVTAAATLVK QHATAQVVGR LSTNLTYITK IQNQYLHLFQ
NLNTRVNNLH HRVTYLEFLA EVHEVQTGLG CVPRGRYCHF DWRPEEVGLN MTLWNSTTWQ
QWMSYYDQIE ENIWNLKYNW SEALEKGKSN TDGLEPDVFR YLADLSSSFT WGSWVDKLVW
LAYILLAYFA FKVLQCIMSN LGAQTRYQLL NAQEDTDPAG DGDQPDDHRS GDTPRSGVPS
GGWSQKLSEG KKIGCLILRT EWQNWRNDLR TLRWLTLGGK ILQLPLSLLV LLVRILLHIL
SPTFQNQRGW TVGRKGTGGD DRELSPELEY LSWTGSSQEM VEMRDLKEED IPEEGIRPVE
M
