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P03386

- ENV_MLVAV

UniProt

P03386 - ENV_MLVAV

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Protein
Envelope glycoprotein
Gene
env
Organism
AKV murine leukemia virus (AKR (endogenous) murine leukemia virus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Metal bindingi117 – 1171Zinc By similarity
Sitei470 – 4712Cleavage; by host By similarity
Sitei650 – 6512Cleavage; by viral protease p14 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. 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

Keywords - Ligandi

Metal-binding, Zinc

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
OrganismiAKV murine leukemia virus (AKR (endogenous) murine leukemia virus)
Taxonomic identifieri11791 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
ProteomesiUP000008875: Genome

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 domaini32 – 611580Extracellular Reviewed prediction
Add
BLAST
Transmembranei612 – 63221Helical; Reviewed prediction
Add
BLAST
Topological domaini633 – 66937Cytoplasmic 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 – 3131 Reviewed prediction
Add
BLAST
Chaini32 – 669638Envelope glycoprotein
PRO_0000239579Add
BLAST
Chaini32 – 470439Surface protein By similarity
PRO_0000040745Add
BLAST
Chaini471 – 650180Transmembrane protein By similarity
PRO_0000040746Add
BLAST
Peptidei651 – 66919R-peptide By similarity
PRO_0000040747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...); by host By similarity
Disulfide bondi77 ↔ 129 By similarity
Disulfide bondi103 ↔ 118 By similarity
Disulfide bondi104 ↔ 114 By similarity
Disulfide bondi152 ↔ 172 By similarity
Disulfide bondi164 ↔ 177 By similarity
Glycosylationi199 – 1991N-linked (GlcNAc...); by host By similarity
Disulfide bondi209 ↔ 215 By similarity
Glycosylationi293 – 2931N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi327 – 3271N-linked (GlcNAc...); by host By similarity
Disulfide bondi337 ↔ 564Interchain (between SU and TM chains, or C-340 with C-564); in linked form
Disulfide bondi337 ↔ 340
Glycosylationi359 – 3591N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi366 – 3661N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi367 ↔ 421 By similarity
Disulfide bondi386 ↔ 398 By similarity
Glycosylationi399 – 3991N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi428 ↔ 441 By similarity
Disulfide bondi556 ↔ 563 By similarity
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 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

ProteinModelPortaliP03386.
SMRiP03386. Positions 40-266, 516-568.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 267236Receptor-binding domain (RBD) Reviewed prediction
Add
BLAST
Regioni473 – 49321Fusion peptide By similarity
Add
BLAST
Regioni539 – 55517Immunosuppression By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili502 – 53837 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi337 – 3404CXXC
Motifi556 – 5649CX6CC
Motifi656 – 6594YXXL motif; contains endocytosis signal By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi264 – 30845Pro-rich
Add
BLAST

Domaini

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

P03386-1 [UniParc]FASTAAdd to Basket

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MESTTLSKPF KNQVNPWGPL IVLLILGGVN PVTLGNSPHQ VFNLTWEVTN    50
GDRETVWAIT GNHPLWTWWP DLTPDLCMLA LHGPSYWGLE YRAPFSPPPG 100
PPCCSGSSDS TPGCSRDCEE PLTSYTPRCN TAWNRLKLSK VTHAHNGGFY 150
VCPGPHRPRW ARSCGGPESF YCASWGCETT GRASWKPSSS WDYITVSNNL 200
TSDQATPVCK GNEWCNSLTI RFTSFGKQAT SWVTGHWWGL RLYVSGHDPG 250
LIFGIRLKIT DSGPRVPIGP NPVLSDRRPP SRPRPTRSPP PSNSTPTETP 300
LTLPEPPPAG VENRLLNLVK GAYQALNLTS PDKTQECWLC LVSGPPYYEG 350
VAVLGTYSNH TSAPANCSVA SQHKLTLSEV TGQGLCIGAV PKTHQVLCNT 400
TQKTSDGSYY LAAPTGTTWA CSTGLTPCIS TTILDLTTDY CVLVELWPRV 450
TYHSPSYVYH QFERRAKYKR EPVSLTLALL LGGLTMGGIA AGVGTGTTAL 500
VATQQFQQLQ AAMHDDLKEV EKSITNLEKS LTSLSEVVLQ NRRGLDLLFL 550
KEGGLCAALK EECCFYADHT GLVRDSMAKL RERLSQRQKL FESQQGWFEG 600
LFNKSPWFTT LISTIMGPLI ILLLILLFGP CILNRLVQFI KDRISVVQAL 650
VLTQQYHQLK TIEDCKSRE 669
Length:669
Mass (Da):73,756
Last modified:July 21, 1986 - v1
Checksum:i3A6C3845208A13F2
GO

Sequence cautioni

The sequence CAA24493.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351G → R1 Publication
Sequence conflicti463 – 4631E → K1 Publication
Sequence conflicti592 – 5921E → K1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01998 Genomic RNA. Translation: AAB03092.1.
V01164 Genomic DNA. Translation: CAA24493.1. Different initiation.
PIRiA92995. VCVWEK.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01998 Genomic RNA. Translation: AAB03092.1 .
V01164 Genomic DNA. Translation: CAA24493.1 . Different initiation.
PIRi A92995. VCVWEK.

3D structure databases

ProteinModelPortali P03386.
SMRi P03386. Positions 40-266, 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. "Nucleotide sequence of AKV murine leukemia virus."
    Herr W.
    J. Virol. 49:471-478(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Nucleotide sequence of the Akv env gene."
    Lenz J., Crowther R., Straceski A., Haseltine W.
    J. Virol. 42:519-529(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiENV_MLVAV
AccessioniPrimary (citable) accession number: P03386
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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