ENV_FOAMV
ID ENV_FOAMV Reviewed; 989 AA.
AC P14351; P90288;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 23-FEB-2022, entry version 89.
DE RecName: Full=Envelope glycoprotein gp130;
DE AltName: Full=Env polyprotein;
DE Contains:
DE RecName: Full=Leader peptide;
DE Short=LP;
DE AltName: Full=Env leader protein;
DE Short=Elp;
DE AltName: Full=gp18LP;
DE Contains:
DE RecName: Full=Surface protein;
DE Short=SU;
DE AltName: Full=Glycoprotein 80;
DE Short=gp80;
DE Contains:
DE RecName: Full=Transmembrane protein;
DE Short=TM;
DE AltName: Full=Glycoprotein 48;
DE Short=gp48;
GN Name=env;
OS Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Spumavirus.
OX NCBI_TaxID=11963;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2820721; DOI=10.1002/j.1460-2075.1987.tb02473.x;
RA Fluegel R.M., Rethwilm A., Maurer B., Darai G.;
RT "Nucleotide sequence analysis of the env gene and its flanking regions of
RT the human spumaretrovirus reveals two novel genes.";
RL EMBO J. 6:2077-2084(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND SEQUENCE REVISION.
RA Fluegel R.M.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP ENDOPLASMIC RETICULUM RETENTION MOTIF, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-985 AND 985-LYS--LYS-987.
RX PubMed=10438808; DOI=10.1128/jvi.73.9.7210-7217.1999;
RA Goepfert P.A., Shaw K., Wang G., Bansal A., Edwards B.H., Mulligan M.J.;
RT "An endoplasmic reticulum retrieval signal partitions human foamy virus
RT maturation to intracytoplasmic membranes.";
RL J. Virol. 73:7210-7217(1999).
RN [4]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF ARG-572.
RX PubMed=10684317; DOI=10.1128/jvi.74.6.2949-2954.2000;
RA Bansal A., Shaw K.L., Edwards B.H., Goepfert P.A., Mulligan M.J.;
RT "Characterization of the R572T point mutant of a putative cleavage site in
RT human foamy virus Env.";
RL J. Virol. 74:2949-2954(2000).
RN [5]
RP ELECTRON MICROSCOPY (34 ANGSTROMS) OF VIRAL PARTICLES, AND SUBUNIT.
RX PubMed=10684305; DOI=10.1128/jvi.74.6.2885-2887.2000;
RA Wilk T., de Haas F., Wagner A., Rutten T., Fuller S.D., Fluegel R.M.,
RA Loechelt M.;
RT "The intact retroviral Env glycoprotein of human foamy virus is a trimer.";
RL J. Virol. 74:2885-2887(2000).
RN [6]
RP CHARACTERIZATION OF THE FUSOGENIC REGION.
RX PubMed=11409874; DOI=10.1006/bbrc.2001.5060;
RA Epand R.M., Epand R.F.;
RT "Factors contributing to the fusogenic potency of foamy virus.";
RL Biochem. Biophys. Res. Commun. 284:870-874(2001).
RN [7]
RP FUNCTION OF N-TERMINUS, AND MUTAGENESIS OF TRP-10 AND TRP-13.
RX PubMed=11390578; DOI=10.1128/jvi.75.13.5762-5771.2001;
RA Lindemann D., Pietschmann T., Picard-Maureau M., Berg A., Heinkelein M.,
RA Thurow J., Knaus P., Zentgraf H., Rethwilm A.;
RT "A particle-associated glycoprotein signal peptide essential for virus
RT maturation and infectivity.";
RL J. Virol. 75:5762-5771(2001).
RN [8]
RP PROTEIN SEQUENCE OF 127-131, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=15564494; DOI=10.1128/jvi.78.24.13865-13870.2004;
RA Duda A., Stange A., Lueftenegger D., Stanke N., Westphal D.,
RA Pietschmann T., Eastman S.W., Linial M.L., Rethwilm A., Lindemann D.;
RT "Prototype foamy virus envelope glycoprotein leader peptide processing is
RT mediated by a furin-like cellular protease, but cleavage is not essential
RT for viral infectivity.";
RL J. Virol. 78:13865-13870(2004).
RN [9]
RP GLYCOSYLATION AT ASN-109; ASN-141; ASN-183; ASN-286; ASN-311; ASN-346;
RP ASN-391; ASN-405; ASN-423; ASN-528; ASN-557; ASN-783; ASN-809 AND ASN-834.
RX PubMed=15919919; DOI=10.1128/jvi.79.12.7664-7672.2005;
RA Lueftenegger D., Picard-Maureau M., Stanke N., Rethwilm A., Lindemann D.;
RT "Analysis and function of prototype foamy virus envelope N glycosylation.";
RL J. Virol. 79:7664-7672(2005).
RN [10]
RP UBIQUITINATION OF LEADER PEPTIDE, AND MUTAGENESIS OF LYS-14; LYS-15;
RP LYS-18; LYS-34 AND LYS-53.
RX PubMed=16306578; DOI=10.1128/jvi.79.24.15074-15083.2005;
RA Stanke N., Stange A., Lueftenegger D., Zentgraf H., Lindemann D.;
RT "Ubiquitination of the prototype foamy virus envelope glycoprotein leader
RT peptide regulates subviral particle release.";
RL J. Virol. 79:15074-15083(2005).
RN [11]
RP REVIEW.
RX PubMed=12908770; DOI=10.1007/978-3-642-55701-9_5;
RA Lindemann D., Goepfert P.A.;
RT "The foamy virus envelope glycoproteins.";
RL Curr. Top. Microbiol. Immunol. 277:111-129(2003).
RN [12]
RP REVIEW.
RX PubMed=15358259; DOI=10.1016/j.mib.2004.06.009;
RA Delelis O., Lehmann-Che J., Saib A.;
RT "Foamy viruses-a world apart.";
RL Curr. Opin. Microbiol. 7:400-406(2004).
CC -!- FUNCTION: The surface protein (SU) attaches the virus to the host cell
CC by binding to the cell receptor. This interaction triggers the
CC refolding of transmembrane protein (TM) and is thought to activate its
CC fusogenic potential by unmasking its fusion peptide (By similarity).
CC {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 -!- FUNCTION: The leader peptide is a component of released, infectious
CC virions and is required for particle budding. {ECO:0000250}.
CC -!- SUBUNIT: The mature envelope protein consists of a trimer of SU-TM
CC heterodimers. The N-terminus of leader peptide specifically interacts
CC with Gag protein. This specific interaction between Gag protein and Env
CC glycoprotein may allow particle egress (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein gp130]: Host endoplasmic
CC reticulum membrane. Note=The polyprotein has a highly unusual
CC biosynthesis for a retroviral glycoprotein. It is translated as a full-
CC length precursor protein into the rough endoplasmic reticulum and
CC initially has a type III protein configuration with both its N and C-
CC termini located intracytoplasmically (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Leader peptide]: Virion membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}. Host endoplasmic
CC reticulum membrane {ECO:0000250}; Single-pass type II membrane protein
CC {ECO:0000250}. Note=Its N-terminus is located inside the viral
CC particle. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Host endoplasmic reticulum
CC membrane; Peripheral membrane protein. Note=The surface protein is not
CC anchored to the viral envelope, but associates with the extravirion
CC surface through its binding to TM. {ECO:0000305}.
CC -!- DOMAIN: The ER retention signal plays an important role in establishing
CC the intracellular site of budding. {ECO:0000250}.
CC -!- PTM: Envelope glycoproteins are synthesized as an inactive precursor
CC that is processed by host furin or a furin-like protease to yield a
CC functional hetero-oligomeric complex. {ECO:0000250}.
CC -!- PTM: The transmembrane protein and the surface protein are N-
CC glycosylated. {ECO:0000250}.
CC -!- PTM: Mono- and polyubiquitinated leader peptide are found in viral
CC particles. Ubiquitination may be involved in regulating the balance
CC between viral and subviral particles release (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Foamy viruses are distinct from other retroviruses in
CC many respects. Their protease is active as an uncleaved Pro-Pol
CC protein. Mature particles do not include the usual processed retroviral
CC structural protein (MA, CA and NC), but instead contain two large Gag
CC proteins. Their functional nucleic acid appears to be either RNA or
CC dsDNA (up to 20% of extracellular particles), because they probably
CC proceed either to an early (before integration) or late reverse
CC transcription (after assembly). Foamy viruses have the ability to
CC retrotranspose intracellularly with high efficiency. They bud
CC predominantly into the endoplasmic reticulum (ER) and occasionally at
CC the plasma membrane. Budding requires the presence of Env proteins.
CC Most viral particles probably remain within the infected cell.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA46123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA29086.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X05591; CAA29086.1; ALT_INIT; Genomic_RNA.
DR EMBL; M54978; AAA46123.1; ALT_INIT; Genomic_RNA.
DR EMBL; U21247; AAB48113.1; -; Genomic_RNA.
DR iPTMnet; P14351; -.
DR Proteomes; UP000138352; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum 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 InterPro; IPR005070; Foamy_env.
DR Pfam; PF03408; Foamy_virus_ENV; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Host endoplasmic reticulum; Host membrane; Isopeptide bond;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Viral envelope protein; Virion.
FT CHAIN 1..989
FT /note="Envelope glycoprotein gp130"
FT /id="PRO_0000125468"
FT CHAIN 1..126
FT /note="Leader peptide"
FT /id="PRO_0000245428"
FT CHAIN 127..572
FT /note="Surface protein"
FT /id="PRO_0000245429"
FT CHAIN 573..989
FT /note="Transmembrane protein"
FT /id="PRO_0000245430"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..88
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..961
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 962..982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 983..989
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..15
FT /note="Involved in virion budding"
FT /evidence="ECO:0000255"
FT REGION 577..599
FT /note="Fusion peptide"
FT /evidence="ECO:0000305"
FT MOTIF 985..987
FT /note="Endoplasmic reticulum retention signal"
FT SITE 25
FT /note="Not glycosylated"
FT SITE 126..127
FT /note="Cleavage; by host"
FT SITE 572..573
FT /note="Cleavage; by host"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:15919919"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16306578"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16306578"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16306578"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16306578"
FT CROSSLNK 53
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16306578"
FT MUTAGEN 10
FT /note="W->A: Complete loss of particle release; when
FT associated with A-13."
FT /evidence="ECO:0000269|PubMed:11390578"
FT MUTAGEN 13
FT /note="W->A: Complete loss of particle release; when
FT associated with A-10."
FT /evidence="ECO:0000269|PubMed:11390578"
FT MUTAGEN 14
FT /note="K->R: Strong increase of subviral particles release;
FT when associated with R-15; R-18; R-34 and R-53."
FT /evidence="ECO:0000269|PubMed:16306578"
FT MUTAGEN 15
FT /note="K->R: Strong increase of subviral particles release;
FT when associated with R-14; R-18; R-34 and R-53."
FT /evidence="ECO:0000269|PubMed:16306578"
FT MUTAGEN 18
FT /note="K->R: Strong increase of subviral particles release;
FT when associated with R-14; R-15; R-34 and R-53."
FT /evidence="ECO:0000269|PubMed:16306578"
FT MUTAGEN 34
FT /note="K->R: Strong increase of subviral particles release;
FT when associated with R-14; R-15; R-18 and R-53."
FT /evidence="ECO:0000269|PubMed:16306578"
FT MUTAGEN 53
FT /note="K->R: Strong increase of subviral particles release;
FT when associated with R-14; R-15; R-18 and R-34."
FT /evidence="ECO:0000269|PubMed:16306578"
FT MUTAGEN 572
FT /note="R->T: Complete loss of processing between SU and
FT TM."
FT /evidence="ECO:0000269|PubMed:10684317"
FT MUTAGEN 985..987
FT /note="KKK->RRR: Increased budding from plasma membrane and
FT decreased budding from ER."
FT /evidence="ECO:0000269|PubMed:10438808"
FT MUTAGEN 985..987
FT /note="KKK->SSS: Increased budding from plasma membrane and
FT decreased budding from ER."
FT /evidence="ECO:0000269|PubMed:10438808"
FT MUTAGEN 985
FT /note="K->S: Increased budding from plasma membrane and
FT decreased budding from ER."
FT /evidence="ECO:0000269|PubMed:10438808"
SQ SEQUENCE 989 AA; 113891 MW; E0E8338ECE44E0A5 CRC64;
MAPPMTLQQW IIWKKMNKAH EALQNTTTVT EQQKEQIILD IQNEEVQPTR RDKFRYLLYT
CCATSSRVLA WMFLVCILLI IVLVSCFVTI SRIQWNKDIQ VLGPVIDWNV TQRAVYQPLQ
TRRIARSLRM QHPVPKYVEV NMTSIPQGVY YEPHPEPIVV KERVLGLSQI LMINSENIAN
NANLTQEVKK LLTEMVNEEM QSLSDVMIDF EIPLGDPRDQ EQYIHRKCYQ EFANCYLVKY
KEPKPWPKEG LIADQCPLPG YHAGLTYNRQ SIWDYYIKVE SIRPANWTTK SKYGQARLGS
FYIPSSLRQI NVSHVLFCSD QLYSKWYNIE NTIEQNERFL LNKLNNLTSG TSVLKKRALP
KDWSSQGKNA LFREINVLDI CSKPESVILL NTSYYSFSLW EGDCNFTKDM ISQLVPECDG
FYNNSKWMHM HPYACRFWRS KKNEKEETKC RDGETKRCLY YPLWDSPEST YDFGYLAYQK
NFPSPICIEQ QKIRDQDYEV YSLYQERKIA SKAYGIDTVL FSLKNFLNYT GTPVNEMPNA
RAFVGLIDPK FPPSYPNVTR EHYTSCNNRK RRSVDNNYAK LRSMGYALTG AVQTLSQISD
INDENLQQGI YLLRDHVITL MEATLHDISV MEGMFAVQHL HTHLNHLKTM LLERRIDWTY
MSSTWLQQQL QKSDDEMKVI KRIARSLVYY VKQTHSSPTA TAWEIGLYYE LVIPKHIYLN
NWNVVNIGHL VKSAGQLTHV TIAHPYEIIN KECVETIYLH LEDCTRQDYV ICDVVKIVQP
CGNSSDTSDC PVWAEAVKEP FVQVNPLKNG SYLVLASSTD CQIPPYVPSI VTVNETTSCF
GLDFKRPLVA EERLSFEPRL PNLQLRLPHL VGIIAKIKGI KIEVTSSGES IKEQIERAKA
ELLRLDIHEG DTPAWIQQLA AATKDVWPAA ASALQGIGNF LSGTAQGIFG TAFSLLGYLK
PILIGVGVIL LVILIFKIVS WIPTKKKNQ
