ENV_SFV1
ID ENV_SFV1 Reviewed; 989 AA.
AC P23073;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 3.
DT 03-AUG-2022, entry version 86.
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 Simian foamy virus type 1 (SFVmac) (SFV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Spumavirus.
OX NCBI_TaxID=338478;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9539; Macaca (macaques).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1647358; DOI=10.1016/0378-1119(91)90410-d;
RA Kupiec J.-J., Kay A., Hayat M., Ravier R., Peries J., Galibert F.;
RT "Sequence analysis of the simian foamy virus type 1 genome.";
RL Gene 101:185-194(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2152825; DOI=10.1128/jvi.64.1.406-410.1990;
RA Mergia A., Shaw K.E.S., Lackner J.E., Luciw P.A.;
RT "Relationship of the env genes and the endonuclease domain of the pol genes
RT of simian foamy virus type 1 and human foamy virus.";
RL J. Virol. 64:406-410(1990).
RN [3]
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 {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=The surface protein is not anchored to the viral envelope, but
CC associates with the extravirion surface through its binding to TM.
CC {ECO:0000250}.
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=AAA47794.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X54482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M33561; AAA47794.1; ALT_INIT; Genomic_RNA.
DR PIR; B33562; VCLJSF.
DR PIR; S18739; S18739.
DR RefSeq; YP_001961123.1; NC_010819.1.
DR PRIDE; P23073; -.
DR Proteomes; UP000007216; 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 3: Inferred from homology;
KW Cleavage on pair of basic residues; Glycoprotein;
KW Host endoplasmic reticulum; Host membrane; Isopeptide bond; Membrane;
KW Signal-anchor; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Viral envelope protein; Virion.
FT CHAIN 1..989
FT /note="Envelope glycoprotein gp130"
FT /id="PRO_0000125469"
FT CHAIN 1..126
FT /note="Leader peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000245431"
FT CHAIN 127..572
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000245432"
FT CHAIN 573..989
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000245433"
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:0000250"
FT MOTIF 985..987
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000250"
FT SITE 126..127
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 572..573
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
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 351
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
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 509
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 53
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CONFLICT 164
FT /note="I -> V (in Ref. 2; AAA47794)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="M -> I (in Ref. 2; AAA47794)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="R -> Q (in Ref. 2; AAA47794)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="K -> E (in Ref. 2; AAA47794)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="M -> I (in Ref. 2; AAA47794)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="T -> A (in Ref. 2; AAA47794)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="F -> S (in Ref. 2; AAA47794)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="P -> L (in Ref. 2; AAA47794)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 989 AA; 113705 MW; 035DD093FB63D6E4 CRC64;
MAPPMTLEQW LLWKKMSQAH QALENVTTLT EEQKQQVIID IQHEDVVPTR MDKLKYLAYS
CCATSTRVLC WIVLVCVLLL VVFISCFVTM SRIQWNKDIA VFGPVIDWNV SQQAVIQQIR
AKRLARSIRV EHATETYVEV NMTSIPQGVL YVPHPEPIIL KERILGLSQV MMINSENIAN
TANLTQETKV LLADMINEEM NDLANQMIDF EIPLGDPRDQ KQYQHQKCFQ EFAHCYLVKY
KTTKGWPSST VIADQCPLPG NHPTVQYAHQ NIWDYYVPFE QIRPEGWNSK SYYEDARIGG
FYIPKWLRNN SYTHVLFCSD QIYGKWYNID LTAQERENLL VRKLINLAKG NSSQLKDRAM
PAEWDKQGKA DLFRQINTLD VCNRPEMVFL LNSSYYEFSL WEGDCGFTRQ NVTQANSLCK
DFYNNSKWQK LHPYSCRFWR YKQEKEETKC SNGEKKKCLY YPQWDTPEAL YDFGFLAYLN
SFPSPICIKN QTIREPEYKI SSLYLECMNA SDRHGIDSAL LALKTFLNFT GQSVNEMPLA
RAFVGLTDPK FPPTYPNITR ESSGCNNNKR KRRSVNNYER LRSMGYALTG AVQTLSQISD
INDERLQHGV YLLRDHVVTL MEAALHDVSI MEGMLAIQHV HTHLNHLKTM LLMRKIDWTF
IRSDWIQQQL QKTDDEMKLI RRTARSLVYY VTQTSSSPTA TSWEIGIYYE IVIPKHIYLN
NWQVINVGHL LESAGHLTHV KVKHPYEIIN KECSDTQYLH LEECIREDYV ICDIVQIVQP
CGNATELSDC PVTALKVKTP YIQVSPLKNG SYLVLSSTKD CSIPAYVPSV VTVNETVKCF
GVEFHKPLYA ETKTSYEPQV PHLKLRLPHL TGIIASLQSL EIEVTSTQEN IKDQIERAKA
QLLRLDIHEG DFPDWLKQVA SATRDVWPAA ASFIQGVGNF LSNTAQGIFG SAVSLLFYAK
PILIGIGVIL LIALLFKIIS WLPGKPKKN
