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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: 4 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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei465 – 4662Cleavage; by host By similarity
Sitei645 – 6462Cleavage; by viral protease By similarity

GO - Molecular functioni

  1. structural molecule activity Source: InterPro
Complete GO annotation...

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; 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.
R-peptide : Host cell membrane; 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 – 606572Extracellular Reviewed prediction
Add
BLAST
Transmembranei607 – 62721Helical; Reviewed prediction
Add
BLAST
Topological domaini628 – 66235Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. viral capsid Source: InterPro
  4. viral envelope Source: UniProtKB-KW
  5. virion membrane Source: UniProtKB-SubCell
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 – 3434 Reviewed prediction
Add
BLAST
Chaini35 – 662628Envelope glycoprotein
PRO_0000239570Add
BLAST
Chaini35 – 465431Surface protein By similarity
PRO_0000040724Add
BLAST
Chaini466 – 645180Transmembrane protein By similarity
PRO_0000040725Add
BLAST
Peptidei646 – 66217R-peptide By similarity
PRO_0000239571Add
BLAST

Amino acid modifications

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni468 – 48821Fusion peptide Reviewed prediction
Add
BLAST
Regioni534 – 55017Immunosuppression By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili496 – 54550 Reviewed prediction
Add
BLAST
Coiled coili555 – 59137 Reviewed prediction
Add
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.

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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MESPTHPKPS KDKTLSWNLV FLVGILFTID IGMANPSPHQ VYNVTWTITN    50
LVTGTKANAT SMLGTLTDAF PTMYFDLCDI IGNTWNPSDQ EPFPGYGCDQ 100
PMRRWQQRNT PFYVCPGHAN RKQCGGPQDG FCAVWGCETT GETYWRPTSS 150
WDYITVKKGV TQGIYQCSGG GWCGPCYDKA VHSSTTGASE GGRCNPLILQ 200
FTQKGRQTSW DGPKSWGLRL YRSGYDPIAL FSVSRQVMTI TPPQAMGPNL 250
VLPDQKPPSR QSQIESRVTP HHSQGNGGTP GITLVNASIA PLSTPVTPAS 300
PKRIGTGDRL INLVQGTYLA LNATDPNRTK DCWLCLVSRP PYYEGIAILG 350
NYSNQTNPPP SCLSIPQHKL TISEVSGQGL CIGTVPKTHQ ALCNETQQGH 400
TGAHYLAAPN GTYWACNTGL TPCISMAVLN WTSDFCVLIE LWPRVTYHQP 450
EYVYTHFAKA ARFRREPISL TVALMLGGLT VGGIAAGVGT GTKALIETAQ 500
FRQLQMAMHT DIQALEESIS ALEKSLTSLS EVVLQNRRGL DILFLQEGGL 550
CAALKEECCF YADHTGLVRD NMAKLRERLK QRQQLFDSQQ GWFEGWFNKS 600
PWFTTLISSI MGPLLILLLI LLFGPCILNR LVQFVKDRIS VVQALILTQQ 650
YQQIKQYDPD RP 662
Length:662
Mass (Da):73,150
Last modified:July 21, 1986 - v1
Checksum:i1482088D547CFF47
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151Missing1 Publication
Sequence conflicti41 – 411V → I1 Publication
Sequence conflicti47 – 471T → V1 Publication
Sequence conflicti51 – 566LVTGTK → VQTNTQ1 Publication
Sequence conflicti70 – 756FPTMYF → YPTLHV1 Publication
Sequence conflicti80 – 9516IIGNT…EPFPG → LVGDSWEPIVLDPNNVKHGA RYSSSK1 Publication
Add
BLAST
Sequence conflicti99 – 11012DQPMR…QQRNT → KTTDRKKQQQTY1 Publication
Add
BLAST
Sequence conflicti120 – 1234NRKQ → PSLGPKGTH1 Publication
Sequence conflicti127 – 1271P → A1 Publication
Sequence conflicti134 – 1341V → A1 Publication
Sequence conflicti143 – 1486TYWRPT → AWWKPS1 Publication
Sequence conflicti158 – 19336KGVTQ…SEGGR → RGSSQDTNSCEGK1 Publication
Add
BLAST
Sequence conflicti208 – 2081T → A1 Publication
Sequence conflicti215 – 2151S → M1 Publication
Sequence conflicti223 – 2231S → T1 Publication
Sequence conflicti232 – 2321S → T1 Publication
Sequence conflicti238 – 2381M → S1 Publication
Sequence conflicti264 – 30037IESRV…VTPAS → TGSKVATQRPQTNESAPRSV APTTMG1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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...

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: September 3, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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