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P03391

- ENV_FSVGA

UniProt

P03391 - ENV_FSVGA

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Protein

Envelope glycoprotein

Gene

env

Organism
Feline sarcoma virus (strain Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein feline leukemia oncovirus B)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi

Functioni

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).By similarity
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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei465 – 4662Cleavage; by hostBy similarity
Sitei645 – 6462Cleavage; by viral proteaseBy similarity

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Fusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein
Alternative name(s):
Env polyprotein
Cleaved into the following 3 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 70
Short name:
gp70
Transmembrane protein
Short name:
TM
Alternative name(s):
Envelope protein p15E
Alternative name(s):
p2E
Gene namesi
Name:env
OrganismiFeline sarcoma virus (strain Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein feline leukemia oncovirus B)
Taxonomic identifieri11774 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostiFelidae (cat family) [TaxID: 9681]

Subcellular locationi

Chain Surface protein : Virion membrane; Peripheral membrane protein. Host cell membrane By similarity; Peripheral membrane protein By similarity
Note: The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be 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).By similarity
R-peptide : Host cell membrane By similarity; Peripheral membrane protein By similarity
Note: The R-peptide is membrane-associated through its palmitate.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 606572ExtracellularSequence AnalysisAdd
BLAST
Transmembranei607 – 62721HelicalSequence AnalysisAdd
BLAST
Topological domaini628 – 66235CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral capsid Source: InterPro
  4. viral envelope Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Sequence AnalysisAdd
BLAST
Chaini35 – 662628Envelope glycoproteinPRO_0000239570Add
BLAST
Chaini35 – 465431Surface proteinBy similarityPRO_0000040724Add
BLAST
Chaini466 – 645180Transmembrane proteinBy similarityPRO_0000040725Add
BLAST
Peptidei646 – 66217R-peptideBy similarityPRO_0000239571Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi58 – 581N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi115 ↔ 132By similarity
Disulfide bondi124 ↔ 137By similarity
Glycosylationi286 – 2861N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi322 – 3221N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi327 – 3271N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi332 ↔ 559Interchain (between SU and TM chains, or C-335 with C-559); in linked formBy similarity
Disulfide bondi332 ↔ 335By similarity
Glycosylationi351 – 3511N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi354 – 3541N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi394 – 3941N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi410 – 4101N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi430 – 4301N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi551 ↔ 558By similarity
Lipidationi626 – 6261S-palmitoyl cysteine; by hostBy similarity

Post-translational modificationi

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. The R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic (By similarity).By similarity
The CXXC motif is highly conserved across a broad range of retroviral envelope proteins. It is thought to participate in the formation of a labile disulfide bond possibly with the CX6CC motif present in the transmembrane protein. Isomerization of the intersubunit disulfide bond to an SU intrachain disulfide bond is thought to occur upon receptor recognition in order to allow membrane fusion (By similarity).By similarity
The transmembrane protein is palmitoylated.By similarity
The R-peptide is palmitoylated.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by a labile interchain disulfide bond.By similarity

Structurei

3D structure databases

ProteinModelPortaliP03391.
SMRiP03391. Positions 38-242, 511-563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni468 – 48821Fusion peptideSequence AnalysisAdd
BLAST
Regioni534 – 55017ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili496 – 54550Sequence AnalysisAdd
BLAST
Coiled coili555 – 59137Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi332 – 3354CXXC
Motifi551 – 5599CX6CC

Domaini

The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo (By similarity).By similarity

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.90.310.10. 1 hit.
InterProiIPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMiSSF49830. SSF49830. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03391-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MESPTHPKPS KDKTLSWNLV FLVGILFTID IGMANPSPHQ VYNVTWTITN
60 70 80 90 100
LVTGTKANAT SMLGTLTDAF PTMYFDLCDI IGNTWNPSDQ EPFPGYGCDQ
110 120 130 140 150
PMRRWQQRNT PFYVCPGHAN RKQCGGPQDG FCAVWGCETT GETYWRPTSS
160 170 180 190 200
WDYITVKKGV TQGIYQCSGG GWCGPCYDKA VHSSTTGASE GGRCNPLILQ
210 220 230 240 250
FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI TPPQAMGPNL
260 270 280 290 300
VLPDQKPPSR QSQIESRVTP HHSQGNGGTP GITLVNASIA PLSTPVTPAS
310 320 330 340 350
PKRIGTGDRL INLVQGTYLA LNATDPNRTK DCWLCLVSRP PYYEGIAILG
360 370 380 390 400
NYSNQTNPPP SCLSIPQHKL TISEVSGQGL CIGTVPKTHQ ALCNETQQGH
410 420 430 440 450
TGAHYLAAPN GTYWACNTGL TPCISMAVLN WTSDFCVLIE LWPRVTYHQP
460 470 480 490 500
EYVYTHFAKA ARFRREPISL TVALMLGGLT VGGIAAGVGT GTKALIETAQ
510 520 530 540 550
FRQLQMAMHT DIQALEESIS ALEKSLTSLS EVVLQNRRGL DILFLQEGGL
560 570 580 590 600
CAALKEECCF YADHTGLVRD NMAKLRERLK QRQQLFDSQQ GWFEGWFNKS
610 620 630 640 650
PWFTTLISSI MGPLLILLLI LLFGPCILNR LVQFVKDRIS VVQALILTQQ
660
YQQIKQYDPD RP
Length:662
Mass (Da):73,150
Last modified:July 21, 1986 - v1
Checksum:i1482088D547CFF47
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151Missing(PubMed:2823466)Curated
Sequence conflicti41 – 411V → I(PubMed:2823466)Curated
Sequence conflicti47 – 471T → V(PubMed:2823466)Curated
Sequence conflicti51 – 566LVTGTK → VQTNTQ(PubMed:2823466)Curated
Sequence conflicti70 – 756FPTMYF → YPTLHV(PubMed:2823466)Curated
Sequence conflicti80 – 9516IIGNT…EPFPG → LVGDSWEPIVLDPNNVKHGA RYSSSK(PubMed:2823466)CuratedAdd
BLAST
Sequence conflicti99 – 11012DQPMR…QQRNT → KTTDRKKQQQTY(PubMed:2823466)CuratedAdd
BLAST
Sequence conflicti120 – 1234NRKQ → PSLGPKGTH(PubMed:2823466)Curated
Sequence conflicti127 – 1271P → A(PubMed:2823466)Curated
Sequence conflicti134 – 1341V → A(PubMed:2823466)Curated
Sequence conflicti143 – 1486TYWRPT → AWWKPS(PubMed:2823466)Curated
Sequence conflicti158 – 19336KGVTQ…SEGGR → RGSSQDTNSCEGK(PubMed:2823466)CuratedAdd
BLAST
Sequence conflicti208 – 2081T → A(PubMed:2823466)Curated
Sequence conflicti215 – 2151S → M(PubMed:2823466)Curated
Sequence conflicti223 – 2231S → T(PubMed:2823466)Curated
Sequence conflicti232 – 2321S → T(PubMed:2823466)Curated
Sequence conflicti238 – 2381M → S(PubMed:2823466)Curated
Sequence conflicti264 – 30037IESRV…VTPAS → TGSKVATQRPQTNESAPRSV APTTMG(PubMed:2823466)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01209 Genomic RNA. Translation: AAA43052.1.
V01172 Genomic DNA. Translation: CAA24497.1.
X00188 Genomic DNA. Translation: CAA25008.1.
M23026 Genomic DNA. No translation available.
PIRiA03991. VCVWGF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01209 Genomic RNA. Translation: AAA43052.1 .
V01172 Genomic DNA. Translation: CAA24497.1 .
X00188 Genomic DNA. Translation: CAA25008.1 .
M23026 Genomic DNA. No translation available.
PIRi A03991. VCVWGF.

3D structure databases

ProteinModelPortali P03391.
SMRi P03391. Positions 38-242, 511-563.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.90.310.10. 1 hit.
InterProi IPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view ]
PANTHERi PTHR10424. PTHR10424. 1 hit.
Pfami PF00429. TLV_coat. 1 hit.
[Graphical view ]
SUPFAMi SSF49830. SSF49830. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequences of the envelope genes of two isolates of feline leukemia virus subgroup B."
    Nunberg J.H., Williams M.E., Innis M.A.
    J. Virol. 49:629-632(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Nucleotide sequence of the envelope gene of Gardner-Arnstein feline leukemia virus B reveals unique sequence homologies with a murine mink cell focus-forming virus."
    Elder J.H., Mullins J.I.
    J. Virol. 46:871-880(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence analysis of Gardner-Arnstein feline leukaemia virus envelope gene reveals common structural properties of mammalian retroviral envelope genes."
    Wunsch M., Schulz A.S., Koch W., Friedrich R., Hunsmann G.
    EMBO J. 2:2239-2246(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Nucleotide sequence analysis of the LTRs and env genes of SM-FeSV and GA-FeSV."
    Guilhot S., Hampe A., D'Auriol L., Galibert F.
    Virology 161:252-258(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiENV_FSVGA
AccessioniPrimary (citable) accession number: P03391
Secondary accession number(s): P21446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program