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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.
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
Sitei442 – 4432Cleavage; by host By similarity
Sitei622 – 6232Cleavage; 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 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; 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 – 583549Extracellular Reviewed prediction
Add
BLAST
Transmembranei584 – 60421Helical; Reviewed prediction
Add
BLAST
Topological domaini605 – 63935Cytoplasmic 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 – 639605Envelope glycoprotein
PRO_0000239568Add
BLAST
Chaini35 – 442408Surface protein By similarity
PRO_0000040716Add
BLAST
Chaini443 – 622180Transmembrane protein By similarity
PRO_0000040717Add
BLAST
Peptidei623 – 63917R-peptide By similarity
PRO_0000239569Add
BLAST

Amino acid modifications

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

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni445 – 46521Fusion peptide Reviewed prediction
Add
BLAST
Regioni511 – 52717Immunosuppression By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili473 – 52250 Reviewed prediction
Add
BLAST
Coiled coili532 – 56837 Reviewed prediction
Add
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.

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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MESPTHPKPS KDKTFPWNLV FLVGILFQID MGMANPSPHQ VYNVTWVITN    50
VQTNSRANAT SMLGTLTDAY PTLYVDLCDL VGDTWEPIAP DPRSWARYSS 100
STHGCKTTDR KKQQQTYPFY VCPGHAPSMG PKGTYCGGAQ DGFCAAWGCE 150
TTGEAWWKPT SSWDYITVKR GSNQDNSCKG KCNPLVLQFT QKGRQASWDR 200
PKMWGLRLYR SGYDPIALFS VSRQVMTITP PQAMGPNLVL PDQKPPSRQS 250
QTKSKVTTQR PQITSSTPRS VASATMGPKR IGTGDRLINL VQGTYLALNA 300
TDPNKTKDCW LCLVSRPPYY EGIAVLGNYS NQTNPPPSCL STPQHKLTIS 350
EVSGQGLCIG TVPKTHQALC KKTQKGHKGT HYLAAPNGTY WACNTGLTPC 400
ISMAVLNWTS DFCVLIELWP RVTYHQPEYI YTHFDKAVRF RREPISLTVA 450
LMLGGLTVGG IAAGVGTGTK ALLETAQFRQ LQIAMHTDIQ ALEESISALE 500
KSLTSLSEVV LQNRRGLDIL FLQEGGLCAA LKEECCFYAD HTGLVRDNMA 550
KLRERLKQRQ QLFDSQQGWF EGWFNKSPWF TTLISSIMGP LLILLLILLL 600
GPCILNRLVQ FVKDRISVVQ ALILTQQYQQ IQQYDSDRP 639
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...

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: September 3, 2014
This is version 87 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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