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Envelope glycoprotein (Env polyprotein) [Cleaved into: Surface protein (SU) (Glycoprotein 62) (gp62); Transmembrane protein (TM) (Glycoprotein 40) (gp40)]

 ENV_BIV29               Reviewed;         904 AA.
P19557; P19556; Q65597;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
20-JUN-2018, entry version 92.
RecName: Full=Envelope glycoprotein;
AltName: Full=Env polyprotein;
Contains:
RecName: Full=Surface protein;
Short=SU;
AltName: Full=Glycoprotein 62;
Short=gp62;
Contains:
RecName: Full=Transmembrane protein;
Short=TM;
AltName: Full=Glycoprotein 40;
Short=gp40;
Name=env;
Bovine immunodeficiency virus (strain R29) (BIV) (Bovine
immunodeficiency-like virus).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
NCBI_TaxID=417296;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate R29-106, and Isolate R29-127;
PubMed=2183467; DOI=10.1016/0042-6822(90)90424-P;
Garvey K.J., Oberste M.S., Elser J.E., Braun M.J., Gonda M.A.;
"Nucleotide sequence and genome organization of biologically active
proviruses of the bovine immunodeficiency-like virus.";
Virology 175:391-409(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Isolate R29-Nadin;
Nadin-Davis S.A., Chang S.C., Roth J.A., Carpenter S.;
"Isolation and characterization of cDNAs encoding rev and tat of
bovine immunodeficiency-like virus.";
Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-99.
PubMed=1645801;
Oberste M.S., Greenwood J.D., Gonda M.A.;
"Analysis of the transcription pattern and mapping of the putative rev
and env splice junctions of bovine immunodeficiency-like virus.";
J. Virol. 65:3932-3937(1991).
-!- FUNCTION: The surface protein (SU) attaches the virus to the host
cell by binding to its receptor. This interaction triggers the
refolding of the transmembrane protein (TM) and is thought to
activate its fusogenic potential by unmasking its fusion peptide.
Fusion occurs at the host cell plasma membrane (By similarity).
{ECO:0000250}.
-!- FUNCTION: The transmembrane protein (TM) acts as a class I viral
fusion protein. Under the current model, the protein has at least
3 conformational states: pre-fusion native state, pre-hairpin
intermediate state, and post-fusion hairpin state. During viral
and target cell membrane fusion, the coiled coil regions (heptad
repeats) assume a trimer-of-hairpins structure, positioning the
fusion peptide in close proximity to the C-terminal region of the
ectodomain. The formation of this structure appears to drive
apposition and subsequent fusion of viral and target cell
membranes. Membranes fusion leads to delivery of the nucleocapsid
into the cytoplasm (By similarity). {ECO:0000250}.
-!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of
SU-TM heterodimers attached by non-covalent interactions or by a
labile interchain disulfide bond. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Transmembrane protein: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host cell membrane {ECO:0000250}; Single-pass type I membrane
protein {ECO:0000250}. Note=It is probably concentrated at the
site of budding and incorporated into the virions possibly by
contacts between the cytoplasmic tail of Env and the N-terminus of
Gag. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Surface protein: Virion membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host
cell membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Note=The surface protein is not anchored to the
viral envelope, but associates with the extravirion surface
through its binding to TM. It is probably concentrated at the site
of budding and incorporated into the virions possibly by contacts
between the cytoplasmic tail of Env and the N-terminus of Gag (By
similarity). {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Envelope glycoproteins are synthesized as a inactive precursor
that is N-glycosylated and processed likely by host cell furin or
by a furin-like protease in the Golgi to yield the mature SU and
TM proteins. The cleavage site between SU and TM requires the
minimal sequence [KR]-X-[KR]-R (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The sequence shown is that of isolate R29-127.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M32690; AAA91274.1; -; Genomic_RNA.
EMBL; L04972; AAA42771.1; -; Genomic_DNA.
EMBL; M74711; AAA42762.1; -; mRNA.
PIR; E34742; VCLJBT.
RefSeq; NP_040566.1; NC_001413.1.
SMR; P19557; -.
GeneID; 1489969; -.
KEGG; vg:1489969; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd09909; HIV-1-like_HR1-HR2; 1.
InterPro; IPR008411; BIV_Surface_Envelope.
InterPro; IPR000328; GP41-like.
Pfam; PF05858; BIV_Env; 1.
Pfam; PF00517; GP41; 1.
2: Evidence at transcript level;
Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
Glycoprotein; Host cell membrane; Host membrane;
Host-virus interaction; Membrane; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein; Virion;
Virus entry into host cell.
CHAIN 1 904 Envelope glycoprotein.
/FTId=PRO_0000239521.
CHAIN 1 555 Surface protein. {ECO:0000250}.
/FTId=PRO_0000038685.
CHAIN 556 904 Transmembrane protein. {ECO:0000250}.
/FTId=PRO_0000038686.
TOPO_DOM 1 726 Extracellular. {ECO:0000255}.
TRANSMEM 727 747 Helical. {ECO:0000255}.
TOPO_DOM 748 904 Cytoplasmic. {ECO:0000255}.
REGION 556 576 Fusion peptide. {ECO:0000255}.
REGION 615 631 Immunosuppression. {ECO:0000250}.
COILED 588 638 {ECO:0000255}.
COILED 676 712 {ECO:0000255}.
SITE 555 556 Cleavage; by host. {ECO:0000250}.
CARBOHYD 131 131 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 376 376 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 385 385 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 432 432 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 509 509 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 541 541 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 597 597 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 663 663 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 694 694 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
VARIANT 7 7 G -> R (in strain: Isolate R29-106 and
Isolate R29-Nadin).
VARIANT 10 10 R -> H (in strain: Isolate R29-Nadin).
VARIANT 24 24 E -> K (in strain: Isolate R29-106).
VARIANT 92 92 E -> K (in strain: Isolate R29-106 and
Isolate R29-Nadin).
VARIANT 135 163 Missing (in strain: Isolate R29-106 and
Isolate R29-Nadin).
VARIANT 216 216 V -> I (in strain: Isolate R29-106).
VARIANT 217 217 M -> T (in strain: Isolate R29-Nadin).
VARIANT 236 236 S -> L (in strain: Isolate R29-106).
VARIANT 248 248 W -> R (in strain: Isolate R29-106).
VARIANT 255 255 N -> S (in strain: Isolate R29-106).
VARIANT 260 260 M -> V (in strain: Isolate R29-106 and
Isolate R29-Nadin).
VARIANT 316 316 S -> P (in strain: Isolate R29-Nadin).
VARIANT 338 338 E -> K (in strain: Isolate R29-Nadin).
VARIANT 494 494 F -> L (in strain: Isolate R29-106 and
Isolate R29-Nadin).
VARIANT 521 521 K -> R (in strain: Isolate R29-106).
VARIANT 624 624 H -> R (in strain: Isolate R29-106).
VARIANT 672 672 N -> S (in strain: Isolate R29-106).
VARIANT 762 762 A -> T (in strain: Isolate R29-106 and
Isolate R29-Nadin).
VARIANT 812 812 R -> K (in strain: Isolate R29-Nadin).
VARIANT 824 824 T -> I (in strain: Isolate R29-Nadin).
SEQUENCE 904 AA; 102270 MW; F56100BC2AECD66F CRC64;
MDQDLDGAER GERGGGSEEL LQEEINEGRL TAREALQTWI NNGEIHPWVL AGMLSMGVGM
LLGVYCQLPD TLIWILMFQL CLYWGLGETS RELDKDSWQW VRSVFIIAIL GTLTMAGTAL
ADDDQSTLIP NITKIPTKDT EPGCTYPWIL ILLILAFILG ILGIILVLRR SNSEDILAAR
DTIDWWLSAN QEIPPKFAFP IILISSPLAG IIGYYVMERH LEIFKKGCQI CGSLSSMWGM
LLEEIGRWLA RREWNVSRVM VILLISFSWG MYVNRVNASG SHVAMVTSPP GYRIVNDTSQ
APWYCFSSAP IPTCSSSQWG DKYFEEKINE TLVKQVYEQA AKHSRATWIE PDLLEEAVYE
LALLSANDSR QVVVENGTDV CSSQNSSTNK GHPMTLLKLR GQVSETWIGN SSLQFCVQWP
YVLVGLNNSD SNISFNSGDW IATNCMHPIT LNKSAQDLGK NFPRLTFLDG QLSQLKNTLC
GHNTNCLKFG NKSFSTNSLI LCQDNPIGND TFYSLSHSFS KQASARWILV KVPSYGFVVV
NDTDTPPSLR IRKPRAVGLA IFLLVLAIMA ITSSLVAATT LVNQHTTAKV VERVVQNVSY
IAQTQDQFTH LFRNINNRLN VLHHRVSYLE YVEEIRQKQV FFGCKPHGRY CHFDFGPEEV
GWNNSWNSKT WNDLQDEYDK IEEKILKIRV DWLNSSLSDT QDTFGLETSI FDHLVQLFDW
TSWKDWIKII IVIIVLWLLI KILLGMLRSC AKVSQNYQHL PAEEEDGDTE PESSPARGDP
ASGSLYENWL NKIGESKNDA YRVWTEEYNS LRILFATCRW DLLTPQLLQL PFFLLTLLLK
LLWDIFRHAP ILNLKGWTVG QGGTSGQQQP PDFPYVNWTG SREQNNPEGG LDSGAWYEGL
RGSQ


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