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P15073

- ENV_MCFF

UniProt

P15073 - ENV_MCFF

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Protein
Envelope glycoprotein
Gene
env
Organism
Mink cell focus-forming murine leukemia virus
Status
Reviewed - Annotation score: 5 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
Sitei440 – 4412Cleavage; by host By similarity
Sitei620 – 6212Cleavage; by viral protease p14 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
OrganismiMink cell focus-forming murine leukemia virus
Taxonomic identifieri11935 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]

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 virion 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 domaini33 – 581549Extracellular Reviewed prediction
Add
BLAST
Transmembranei582 – 60221Helical; Reviewed prediction
Add
BLAST
Topological domaini603 – 63634Cytoplasmic 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 – 3232 Reviewed prediction
Add
BLAST
Chaini33 – 636604Envelope glycoprotein
PRO_0000239577Add
BLAST
Chaini33 – 440408Surface protein By similarity
PRO_0000040739Add
BLAST
Chaini441 – 620180Transmembrane protein By similarity
PRO_0000040740Add
BLAST
Peptidei621 – 63616R-peptide By similarity
PRO_0000040741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...); by host By similarity
Glycosylationi58 – 581N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi109 ↔ 126 By similarity
Disulfide bondi118 ↔ 131 By similarity
Glycosylationi297 – 2971N-linked (GlcNAc...); by host By similarity
Disulfide bondi307 ↔ 534Interchain (between SU and TM chains, or C-310 with C-534); in linked form By similarity
Disulfide bondi307 ↔ 310 By similarity
Glycosylationi329 – 3291N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi336 – 3361N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi337 ↔ 391 By similarity
Disulfide bondi356 ↔ 368 By similarity
Glycosylationi369 – 3691N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi398 ↔ 411 By similarity
Glycosylationi405 – 4051N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi526 ↔ 533 By similarity
Lipidationi601 – 6011S-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

ProteinModelPortaliP15073.
SMRiP15073. Positions 38-230, 486-538.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 233202Receptor-binding domain (RBD) Reviewed prediction
Add
BLAST
Regioni443 – 46321Fusion peptide By similarity
Add
BLAST
Regioni509 – 52517Immunosuppression By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili472 – 50837 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi307 – 3104CXXC
Motifi526 – 5349CX6CC
Motifi626 – 6294YXXL motif; contains endocytosis signal By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi230 – 27950Pro-rich
Add
BLAST

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.
The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis.

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. 2 hits.
[Graphical view]
SUPFAMiSSF49830. SSF49830. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15073-1 [UniParc]FASTAAdd to Basket

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MEGPAFSKPL KDKINPWGPL IILGILIRAG VSVQHDSPHQ VFNVTWRVTN    50
LMTGQTANAT SLLGTMTDAF PKLYFDLCDL IGDDWDETGL GCRTPGGRKR 100
ARTFDFYVCP GHTVPTGCGG PREGYCGKWG CETTGQAYWK PSSSWDLISL 150
KRGNTPRNQG PCYDSSVVSS GIQGATPGGR CNPLVLEFTD AGKKASWDGP 200
KVWGLRLYRS TGIDPVTRFS LTRQVLNIGP RLPIGPNPVI TGQLPPSRPV 250
QIRLPRPPQP PPPGAASIVP ETAPPSQQPG TGDRLLNLVD GAYQALNLTS 300
PDKTQECWLC LVAGPPYYEG VAVLGTYSNH TSAPANCSVA SQHKLTLSEV 350
TGQGLCVGAV PKTHQALCNT TQKTSDGSYY LAAPAGTIWA CNTGLTPCLS 400
TTVLNLTTDY CVLVELWPKV TYHSPDYVYT QFEPGARFRR EPVSLTLALL 450
LGGLTMGGIA AGVGTGTTAL VATQQFQQLQ AAVHNDLKEV EKSITNLEKS 500
LTSLSEVALQ NRRGLDLLFL KEGGLCAALK EECCFYADHT GLVRDSMAKL 550
RERLNQRQKL FESGQGWFEG LFNRSPWFTT LISTIMGPLI VLLLILLFGP 600
CILNRLVQFV KDRISVVQAL VLTQQYHQLK PIEYEP 636
Length:636
Mass (Da):69,113
Last modified:April 1, 1990 - v1
Checksum:iDF6208F7EA968E2A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23029 Genomic RNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23029 Genomic RNA. No translation available.

3D structure databases

ProteinModelPortali P15073.
SMRi P15073. Positions 38-230, 486-538.
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. 2 hits.
[Graphical view ]
SUPFAMi SSF49830. SSF49830. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Biologic and molecular genetic characteristics of a unique MCF virus that is highly leukemogenic in ecotropic virus-negative mice."
    Chattopadhyay S.K., Baroudy B.M., Holmes K.L., Fredrickson T.N., Lander M.R., Morse H.C. III, Hartley J.W.
    Virology 168:90-100(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiENV_MCFF
AccessioniPrimary (citable) accession number: P15073
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 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

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