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P21445

- ENV_FSVSM

UniProt

P21445 - ENV_FSVSM

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Protein

Envelope glycoprotein

Gene
env
Organism
Feline sarcoma virus (strain SM) (Sm-FeSV)
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
Sitei448 – 4492Cleavage; by host By similarity
Sitei628 – 6292Cleavage; 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 sarcoma virus (strain SM) (Sm-FeSV)
Taxonomic identifieri11779 [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 domaini37 – 589553Extracellular Reviewed predictionAdd
BLAST
Transmembranei590 – 61021Helical; Reviewed predictionAdd
BLAST
Topological domaini611 – 64535Cytoplasmic 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 – 3636 Reviewed predictionAdd
BLAST
Chaini37 – 645609Envelope glycoproteinPRO_0000239572Add
BLAST
Chaini37 – 448412Surface protein By similarityPRO_0000040727Add
BLAST
Chaini449 – 628180Transmembrane protein By similarityPRO_0000040728Add
BLAST
Peptidei629 – 64517R-peptide By similarityPRO_0000239573Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi61 – 611N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi128 ↔ 150 By similarity
Disulfide bondi142 ↔ 155 By similarity
Glycosylationi270 – 2701N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi305 – 3051N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi310 – 3101N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi315 ↔ 542Interchain (between SU and TM chains, or C-318 with C-542); in linked form By similarity
Disulfide bondi315 ↔ 318 By similarity
Glycosylationi334 – 3341N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi337 – 3371N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi377 – 3771N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi393 – 3931N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi413 – 4131N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi534 ↔ 541 By similarity
Lipidationi609 – 6091S-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

ProteinModelPortaliP21445.
SMRiP21445. Positions 41-236, 494-546.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni451 – 47121Fusion peptide Reviewed predictionAdd
BLAST
Regioni517 – 53317Immunosuppression By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili479 – 52850 Reviewed predictionAdd
BLAST
Coiled coili538 – 57437 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi315 – 3184CXXC
Motifi534 – 5429CX6CC

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.

P21445-1 [UniParc]FASTAAdd to Basket

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MEGPTHPKPF KDKTFSWDLI ILVGVVRVLL RLDVGMANPS PHQVYNVTWV    50
ITNVQTNSQA NATSMLGTLT DAYPTLHVDL CDLVGDTWEP IVLDPSNVKH 100
GARYSSSKYG CKTTDRKKQQ QTYPFYVCPG HAPSMGPKGT HCGGAHDGFC 150
AAWGCETTGE AWWKPTSSWD YITVKRGSSQ DTSCDKNCNP LVLQFTQKGR 200
QASWDGPKLW GLRLYRTGYD PIALFSVSRQ VSTIMPPQAM GPNLVLPEQK 250
PPSRQSQTKS KVATQKPQTN GTTPRSVAPA TMSPKRIGTR DRLINLVQGT 300
YLALNATDPN KTKDCWLCLV SRPPYYEGIA ILGNYSNQTN PPPSCLSTPQ 350
HKLTISEVSG QGLCIGTVPR THQALCNKTQ QGHTGAHYLA APNGTYWACN 400
TGLTPCISMA VLNWTSDFCV LIELWPRVTY HQPEYIYTHF DKAVRFRREP 450
ISLTVALMLG GLTVGGIAAG VGTGTKALLE TAQFRQLQIA MHTDIQALEE 500
SISALEKSLT SLSEVVLQNR RGLDILFLQG GGLCAALKEE CCFYADHTGL 550
VRDNMAKLRE RLKQRQQLFD SQQGWFEGWF NKSPWFTTLI SSIMGPLLIL 600
LLILLFGPCI LNRLVQFVKD RISVVQALIL TQQYQQIQQY DPDRP 645
Length:645
Mass (Da):71,594
Last modified:February 1, 1996 - v2
Checksum:i4E6DB90A00A43B21
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23025 Genomic DNA. Translation: AAA74004.1.
PIRiA33741. VCMVSS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23025 Genomic DNA. Translation: AAA74004.1 .
PIRi A33741. VCMVSS.

3D structure databases

ProteinModelPortali P21445.
SMRi P21445. Positions 41-236, 494-546.
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 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_FSVSM
AccessioniPrimary (citable) accession number: P21445
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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