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P31791

- ENV_FENV1

UniProt

P31791 - ENV_FENV1

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Protein

Envelope glycoprotein

Gene
env
Organism
Feline endogenous virus ECE1
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
Sitei470 – 4712Cleavage; by host By similarity
Sitei650 – 6512Cleavage; by viral protease By 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 endogenous virus ECE1
Taxonomic identifieri11766 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
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 domaini23 – 611589Extracellular Reviewed predictionAdd
BLAST
Transmembranei612 – 63221Helical; Reviewed predictionAdd
BLAST
Topological domaini633 – 67139Cytoplasmic Reviewed predictionAdd
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 – 2222 Reviewed predictionAdd
BLAST
Chaini23 – 671649Envelope glycoproteinPRO_0000239558Add
BLAST
Chaini23 – 470448Surface protein By similarityPRO_0000040703Add
BLAST
Chaini471 – 650180Transmembrane protein By similarityPRO_0000040704Add
BLAST
Peptidei651 – 67121R-peptide By similarityPRO_0000239559Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi121 ↔ 142 By similarity
Disulfide bondi134 ↔ 147 By similarity
Glycosylationi169 – 1691N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi281 – 2811N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi326 – 3261N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi331 – 3311N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi355 – 3551N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi358 – 3581N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi415 – 4151N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi435 – 4351N-linked (GlcNAc...); by host Reviewed prediction
Lipidationi631 – 6311S-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 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 noncovalent interactions or by a labile interchain disulfide bond By similarity.

Structurei

3D structure databases

ProteinModelPortaliP31791.
SMRiP31791. Positions 516-568.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni473 – 49321Fusion peptide Reviewed predictionAdd
BLAST
Regioni539 – 55517Immunosuppression By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili501 – 55050 Reviewed predictionAdd
BLAST
Coiled coili560 – 59637 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi336 – 3394CXXC
Motifi556 – 5649CX6CC
Motifi656 – 6594YXXL motif; contains endocytosis signal By similarity

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.

P31791-1 [UniParc]FASTAAdd to Basket

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MKPPAGMVFL WVLTSLGAGI GAKIVKEGNP HQVYTLTWQI YSQSGEVVWE    50
VQGNHALNTW WPALTPDFCQ LAAGLDTWDI PDRSPKNLET SMEGTSQQLT 100
PQGCSKPWKR CALTERDFYV CPRDNRDRAT AHRCGGYEEY FCSAWGCETT 150
GDAYWQPTST WDLITITRNY TKPDSCDDRV ERERKTSRHW RDPLSLPLKI 200
TFTDSGKRAL GWQTGYTWGL RWYLPGKDRG IILKIKLKID TITQTVGPNL 250
VLADQKTPVQ LAIPVQPPRA PTQTPRVNPV NSTLSPSLGY PAPAPGPRPP 300
YPTSPSRPGT GDRLLNLVQG VYLTLNLTAP NQTQDCWLCL TAKPPYYQGV 350
AIIGNFTNHT NAPLRCSTTP RHGLTLTEVT GYGLCIGKIP PSHQNLCSQT 400
VPSVGQGPYY LTAPNGTYWV CNTGLTPCIS LQILNDTADY CILIELWPKI 450
FYHDSEYIYG HYEPGGRFRR DPVSLTVALL LGGLTMGSLA AGIGTGTAAL 500
IETNQFKQLQ IAMHSDIQAL EESISALERS LISLSEVVLQ NRRGLDLLFL 550
QEGGLCAALK EECCFYADHT GIVRDSMAKL RERFKQRQKL FESQQGWFEG 600
WYNKSPWFTT LVSSLMVPLI LLLLILMFGP CILNHLLQFI RERLSVIQAL 650
VLTQQYHQLR QFDAERPDAI E 671
Length:671
Mass (Da):75,152
Last modified:July 1, 1993 - v1
Checksum:iEA9847024EF794A0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X51929 Genomic DNA. Translation: CAB38567.1.
PIRiS12815. VCMVCE.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X51929 Genomic DNA. Translation: CAB38567.1 .
PIRi S12815. VCMVCE.

3D structure databases

ProteinModelPortali P31791.
SMRi P31791. Positions 516-568.
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. "The exogenous RD-114 and the related endogenous proviral element ECE1 of domestic cat differ in their env genes."
    Moehring R., Drescher B., Riedel H., Bauer D., Rohde K., Beyer W., Rosenthal S.
    Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiENV_FENV1
AccessioniPrimary (citable) accession number: P31791
Secondary accession number(s): Q28416
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 81 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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