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P06752

- ENV_FLVSA

UniProt

P06752 - ENV_FLVSA

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Protein

Envelope glycoprotein

Gene

env

Organism
Feline leukemia virus (strain C/Sarma)
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.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
Sitei442 – 4432Cleavage; by hostBy similarity
Sitei622 – 6232Cleavage; 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 leukemia virus (strain C/Sarma)
Taxonomic identifieri103919 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostiFelis catus (Cat) (Felis silvestris catus) [TaxID: 9685]

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

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 – 639605Envelope glycoproteinPRO_0000239568Add
BLAST
Chaini35 – 442408Surface proteinBy similarityPRO_0000040716Add
BLAST
Chaini443 – 622180Transmembrane proteinBy similarityPRO_0000040717Add
BLAST
Peptidei623 – 63917R-peptideBy similarityPRO_0000239569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi35 – 351N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi43 – 431N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi58 – 581N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi122 ↔ 144By similarity
Disulfide bondi136 ↔ 149By similarity
Glycosylationi299 – 2991N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi304 – 3041N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi309 ↔ 536Interchain (between SU and TM chains, or C-312 with C-536); in linked formBy similarity
Disulfide bondi309 ↔ 312By similarity
Glycosylationi328 – 3281N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi331 – 3311N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi387 – 3871N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi407 – 4071N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi528 ↔ 535By similarity
Lipidationi603 – 6031S-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

ProteinModelPortaliP06752.
SMRiP06752. Positions 38-230, 488-540.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 583549ExtracellularSequence AnalysisAdd
BLAST
Topological domaini605 – 63935CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei584 – 60421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni445 – 46521Fusion peptideSequence AnalysisAdd
BLAST
Regioni511 – 52717ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili473 – 52250Sequence AnalysisAdd
BLAST
Coiled coili532 – 56837Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi309 – 3124CXXC
Motifi528 – 5369CX6CC

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.

P06752-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MESPTHPKPS KDKTFPWNLV FLVGILFQID MGMANPSPHQ VYNVTWVITN
60 70 80 90 100
VQTNSRANAT SMLGTLTDAY PTLYVDLCDL VGDTWEPIAP DPRSWARYSS
110 120 130 140 150
STHGCKTTDR KKQQQTYPFY VCPGHAPSMG PKGTYCGGAQ DGFCAAWGCE
160 170 180 190 200
TTGEAWWKPT SSWDYITVKR GSNQDNSCKG KCNPLVLQFT QKGRQASWDR
210 220 230 240 250
PKMWGLRLYR SGYDPIALFS VSRQVMTITP PQAMGPNLVL PDQKPPSRQS
260 270 280 290 300
QTKSKVTTQR PQITSSTPRS VASATMGPKR IGTGDRLINL VQGTYLALNA
310 320 330 340 350
TDPNKTKDCW LCLVSRPPYY EGIAVLGNYS NQTNPPPSCL STPQHKLTIS
360 370 380 390 400
EVSGQGLCIG TVPKTHQALC KKTQKGHKGT HYLAAPNGTY WACNTGLTPC
410 420 430 440 450
ISMAVLNWTS DFCVLIELWP RVTYHQPEYI YTHFDKAVRF RREPISLTVA
460 470 480 490 500
LMLGGLTVGG IAAGVGTGTK ALLETAQFRQ LQIAMHTDIQ ALEESISALE
510 520 530 540 550
KSLTSLSEVV LQNRRGLDIL FLQEGGLCAA LKEECCFYAD HTGLVRDNMA
560 570 580 590 600
KLRERLKQRQ QLFDSQQGWF EGWFNKSPWF TTLISSIMGP LLILLLILLL
610 620 630
GPCILNRLVQ FVKDRISVVQ ALILTQQYQQ IQQYDSDRP
Length:639
Mass (Da):71,162
Last modified:January 1, 1988 - v1
Checksum:iA309B64AC8EC74E4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14331 Genomic DNA. Translation: AAA43049.1.
PIRiA29013. VCMVSA.
A46165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14331 Genomic DNA. Translation: AAA43049.1 .
PIRi A29013. VCMVSA.
A46165.

3D structure databases

ProteinModelPortali P06752.
SMRi P06752. Positions 38-230, 488-540.
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. "Molecular analysis and pathogenesis of the feline aplastic anemia retrovirus, feline leukemia virus C-Sarma."
    Riedel N., Hoover E.A., Gasper P.W., Nicolson M.O., Mullins J.I.
    J. Virol. 60:242-250(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiENV_FLVSA
AccessioniPrimary (citable) accession number: P06752
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program