ENV_SFVCP
ID ENV_SFVCP Reviewed; 988 AA.
AC Q87041;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 07-OCT-2020, entry version 58.
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 (isolate chimpanzee) (SFVcpz).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Spumaretrovirinae; Spumavirus.
OX NCBI_TaxID=298339;
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8184531; DOI=10.1006/viro.1994.1285;
RA Herchenroder O., Renne R., Loncar D., Cobb E.K., Murthy K.K., Schneider J.,
RA Mergia A., Luciw P.A.;
RT "Isolation, cloning, and sequencing of simian foamy viruses from
RT chimpanzees (SFVcpz): high homology to human foamy virus (HFV).";
RL Virology 201:187-199(1994).
RN [2]
RP CLEAVAGE BY SPPL2A; SPPL2B AND SPPL3, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF ARG-123 AND ARG-126.
RX PubMed=23132852; DOI=10.1074/jbc.m112.371369;
RA Voss M., Fukumori A., Kuhn P.H., Kunzel U., Klier B., Grammer G.,
RA Haug-Kroper M., Kremmer E., Lichtenthaler S.F., Steiner H., Schroder B.,
RA Haass C., Fluhrer R.;
RT "Foamy virus envelope protein is a substrate for signal peptide peptidase-
RT like 3 (SPPL3).";
RL J. Biol. Chem. 287:43401-43409(2012).
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 (By similarity). This specific interaction between Gag
CC protein and Env glycoprotein may allow particle egress. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein gp130]: Host endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:23132852}. Note=The polyprotein
CC has a highly unusual biosynthesis for a retroviral glycoprotein. It is
CC translated as a full-length precursor protein into the rough
CC endoplasmic reticulum and initially has a type III protein
CC configuration with both its N and C-termini located
CC 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; Single-pass type I membrane protein.
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.
CC -!- PTM: Envelope glycoproteins are synthesized as an inactive precursor
CC that is processed by host furin or a furin-like proprotein convertase
CC (PC)-mediated cleavage proteolysis to yield a functional
CC heterooligomeric complex (By similarity). Further proteolytically
CC processed through regulated intramembrane proteolysis either by SPPL2A
CC and SPPL2B or by SPPL3 in a PC-mediated cleavage-dependent or
CC -independent manner, respectively (PubMed:23132852). {ECO:0000250,
CC ECO:0000269|PubMed:23132852}.
CC -!- PTM: The transmembrane protein and the surface protein are N-
CC glycosylated.
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.
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.
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DR EMBL; U04327; AAA19979.1; -; Genomic_DNA.
DR RefSeq; NP_056804.1; NC_001364.1.
DR GeneID; 1489966; -.
DR KEGG; vg:1489966; -.
DR Proteomes; UP000001063; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IDA:UniProtKB.
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:0002020; F:protease binding; IPI:UniProtKB.
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; Glycoprotein;
KW Host endoplasmic reticulum; Host membrane; Isopeptide bond; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Viral envelope protein; Virion.
FT CHAIN 1..988
FT /note="Envelope glycoprotein gp130"
FT /id="PRO_0000378587"
FT CHAIN 1..126
FT /note="Leader peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000378588"
FT CHAIN 127..571
FT /note="Surface protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000378589"
FT CHAIN 572..988
FT /note="Transmembrane protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000378590"
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..960
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 961..981
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 982..988
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..15
FT /note="Involved in virion budding"
FT /evidence="ECO:0000255"
FT REGION 576..598
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT MOTIF 984..986
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 126..127
FT /note="Cleavage; by human protease SPPL3"
FT /evidence="ECO:0000269|PubMed:23132852"
FT SITE 571..572
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 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 833
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 18
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 MUTAGEN 123
FT /note="R->A: Loss of host furin or a furin-like protease
FT activity; when associated with A-126. Does not affect
FT subcellular localization; when associated with A-126."
FT /evidence="ECO:0000269|PubMed:23132852"
FT MUTAGEN 126
FT /note="R->A: Loss of host furin or a furin-like protease
FT activity; when associated with A-123. Does not affect
FT subcellular localization; when associated with A-126."
FT /evidence="ECO:0000269|PubMed:23132852"
SQ SEQUENCE 988 AA; 113353 MW; 9A88951475BE9C62 CRC64;
MAPPMTLQQW IIWNKMNKAH EALQNSTTVT DQQKEQIILE IQNEEVRPTR KDKIRYLLYT
CCATSSRVLA WMLLVCVLLI VVLVSCFLTI SRIQWNRDIQ VLGPVIDWNV TQRAVYQPLQ
TRRIARSLRM QHPVPKYIEV NMTSIPQGVY YEPHPEPIVV TERVLGLSQV LMINSENIAN
NANLTQEVKK LLAEVVNEEM QSLSDVMIDF EIPLGDPRDQ EQYIHRKCYQ EFAHCYLVKY
KTPKSWPTEG LIADQCPLPG YHAGLSYKPQ SIWDYYIKVE ITRPANWSSQ AVYGQARLGS
FYVPKGIRQN NYSHVLFCSD QLYSKWYNIE NSIEQNEKFL LNKLDNLTTG SSLLKKRALP
KEWSSQGKNA LFKEINVLDV CSKPELVILL NTSYYSFSLW EGDCNFTKNM ISQLVPECEG
FYNNSKWMHM HPYACRFWRS KNEKEETKCR PGEKEKCLYY PYQDSLESTY DFGFLAYQKN
FPAPICIEQQ EIRDKDYEVY SLYQECKLAS KVHGIDTVLF SLKNFLNHTG RPVNEMPNAR
AFVGLVDPKF PPSYPNVTRE HYTSCNNRKR RSTDNNYAKL KSMGYALTGA VQTLSQISDI
NDENLQQGIY LLRDHVITLM EATLHDISVM EGMFAVQHLH THLNHLKTML LERRIDWTYM
SSAWLQQQLQ KSDDEMKVIK RIAKSLVYYV KQTYNSPTAT AWEIGLYYEL TIPKHVYLNN
WNVVNIGHLV QSAGQLTHVT IAHPYEIINK ECTETKYLHL KDCRRQDYVI CDVVEIVQPC
GNSTDTSDCP VWAEAVKEPF VQVNPLKNGS YLVLASSTDC QIPPYVPSIV TVNETTSCYG
LNFKKPLVAE ERLGFEPRLP NLQLRLPHLV GIIAKIKGLK IEVTSSGESI KDQIERAKAE
LLRLDIHEGD TPAWIQQLAA ATKDVWPAAA SALQGIGNFL SGAAHGIFGT AFSLLGYLKP
ILIGVGVILL IILIFKIVSW IPTKKKSQ
