ENV_BIV29
ID ENV_BIV29 Reviewed; 904 AA.
AC P19557; P19556; Q65597;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 23-FEB-2022, entry version 100.
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 Bovine immunodeficiency virus (strain R29) (BIV) (Bovine
OS immunodeficiency-like virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=417296;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate R29-106, and Isolate R29-127;
RX PubMed=2183467; DOI=10.1016/0042-6822(90)90424-p;
RA Garvey K.J., Oberste M.S., Elser J.E., Braun M.J., Gonda M.A.;
RT "Nucleotide sequence and genome organization of biologically active
RT proviruses of the bovine immunodeficiency-like virus.";
RL Virology 175:391-409(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate R29-Nadin;
RA Nadin-Davis S.A., Chang S.C., Roth J.A., Carpenter S.;
RT "Isolation and characterization of cDNAs encoding rev and tat of bovine
RT immunodeficiency-like virus.";
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-99.
RX PubMed=1645801; DOI=10.1128/jvi.65.7.3932-3937.1991;
RA Oberste M.S., Greenwood J.D., Gonda M.A.;
RT "Analysis of the transcription pattern and mapping of the putative rev and
RT env splice junctions of bovine immunodeficiency-like virus.";
RL J. Virol. 65:3932-3937(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 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 -!- MISCELLANEOUS: The sequence shown is that of isolate R29-127.
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DR EMBL; M32690; AAA91274.1; -; Genomic_RNA.
DR EMBL; L04972; AAA42771.1; -; Genomic_DNA.
DR EMBL; M74711; AAA42762.1; -; mRNA.
DR PIR; E34742; VCLJBT.
DR RefSeq; NP_040566.1; NC_001413.1.
DR GeneID; 1489969; -.
DR KEGG; vg:1489969; -.
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; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW Glycoprotein; Host cell membrane; Host membrane; Host-virus interaction;
KW Membrane; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..904
FT /note="Envelope glycoprotein"
FT /id="PRO_0000239521"
FT CHAIN 1..555
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038685"
FT CHAIN 556..904
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038686"
FT TOPO_DOM 1..726
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 727..747
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 748..904
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 556..576
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT REGION 615..631
FT /note="Immunosuppression"
FT /evidence="ECO:0000250"
FT REGION 761..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 588..638
FT /evidence="ECO:0000255"
FT COILED 676..712
FT /evidence="ECO:0000255"
FT COMPBIAS 862..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 555..556
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
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 509
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VARIANT 7
FT /note="G -> R (in strain: Isolate R29-106 and Isolate R29-
FT Nadin)"
FT VARIANT 10
FT /note="R -> H (in strain: Isolate R29-Nadin)"
FT VARIANT 24
FT /note="E -> K (in strain: Isolate R29-106)"
FT VARIANT 92
FT /note="E -> K (in strain: Isolate R29-106 and Isolate R29-
FT Nadin)"
FT VARIANT 135..163
FT /note="Missing (in strain: Isolate R29-106 and Isolate R29-
FT Nadin)"
FT VARIANT 216
FT /note="V -> I (in strain: Isolate R29-106)"
FT VARIANT 217
FT /note="M -> T (in strain: Isolate R29-Nadin)"
FT VARIANT 236
FT /note="S -> L (in strain: Isolate R29-106)"
FT VARIANT 248
FT /note="W -> R (in strain: Isolate R29-106)"
FT VARIANT 255
FT /note="N -> S (in strain: Isolate R29-106)"
FT VARIANT 260
FT /note="M -> V (in strain: Isolate R29-106 and Isolate R29-
FT Nadin)"
FT VARIANT 316
FT /note="S -> P (in strain: Isolate R29-Nadin)"
FT VARIANT 338
FT /note="E -> K (in strain: Isolate R29-Nadin)"
FT VARIANT 494
FT /note="F -> L (in strain: Isolate R29-106 and Isolate R29-
FT Nadin)"
FT VARIANT 521
FT /note="K -> R (in strain: Isolate R29-106)"
FT VARIANT 624
FT /note="H -> R (in strain: Isolate R29-106)"
FT VARIANT 672
FT /note="N -> S (in strain: Isolate R29-106)"
FT VARIANT 762
FT /note="A -> T (in strain: Isolate R29-106 and Isolate R29-
FT Nadin)"
FT VARIANT 812
FT /note="R -> K (in strain: Isolate R29-Nadin)"
FT VARIANT 824
FT /note="T -> I (in strain: Isolate R29-Nadin)"
SQ 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
