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Protein

Envelope glycoprotein

Gene

env

Organism
AKV murine leukemia virus (AKR (endogenous) murine leukemia virus)
Status
Reviewed-Annotation score: 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).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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi117ZincBy similarity1

GO - Molecular functioni

GO - Biological processi

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]
Proteomesi
  • UP000008875 Componenti: Genome

Subcellular locationi

Surface protein :
  • Virion membrane; Peripheral membrane protein
  • Host cell membrane By similarity; 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).By similarity
Peptide R-peptide :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini32 – 611ExtracellularSequence analysisAdd BLAST580
Transmembranei612 – 632HelicalSequence analysisAdd BLAST21
Topological domaini633 – 669CytoplasmicSequence analysisAdd BLAST37

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_000023957932 – 669Envelope glycoproteinAdd BLAST638
ChainiPRO_000004074532 – 470Surface proteinBy similarityAdd BLAST439
ChainiPRO_0000040746471 – 650Transmembrane proteinBy similarityAdd BLAST180
PeptideiPRO_0000040747651 – 669R-peptideBy similarityAdd BLAST19

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi43N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi77 ↔ 129By similarity
Disulfide bondi103 ↔ 118By similarity
Disulfide bondi104 ↔ 114By similarity
Disulfide bondi152 ↔ 172By similarity
Disulfide bondi164 ↔ 177By similarity
Glycosylationi199N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi209 ↔ 215By similarity
Glycosylationi293N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi327N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi337 ↔ 564Interchain (between SU and TM chains, or C-340 with C-564); in linked form
Disulfide bondi337 ↔ 340
Glycosylationi359N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi366N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi367 ↔ 421By similarity
Disulfide bondi386 ↔ 398By similarity
Glycosylationi399N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi428 ↔ 441By similarity
Disulfide bondi556 ↔ 563By similarity
Lipidationi631S-palmitoyl cysteine; by hostBy similarity1

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).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).By similarity
The transmembrane protein is palmitoylated.By similarity
The R-peptide is palmitoylated.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei470 – 471Cleavage; by hostBy similarity2
Sitei650 – 651Cleavage; by viral protease p14By similarity2

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 267Receptor-binding domain (RBD)Sequence analysisAdd BLAST236
Regioni473 – 493Fusion peptideBy similarityAdd BLAST21
Regioni539 – 555ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili502 – 538Sequence analysisAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi337 – 340CXXC4
Motifi556 – 564CX6CC9
Motifi656 – 659YXXL motif; contains endocytosis signalBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi264 – 308Pro-richAdd BLAST45

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).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. 2 hits.
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

« Hide

        10         20         30         40         50
MESTTLSKPF KNQVNPWGPL IVLLILGGVN PVTLGNSPHQ VFNLTWEVTN
60 70 80 90 100
GDRETVWAIT GNHPLWTWWP DLTPDLCMLA LHGPSYWGLE YRAPFSPPPG
110 120 130 140 150
PPCCSGSSDS TPGCSRDCEE PLTSYTPRCN TAWNRLKLSK VTHAHNGGFY
160 170 180 190 200
VCPGPHRPRW ARSCGGPESF YCASWGCETT GRASWKPSSS WDYITVSNNL
210 220 230 240 250
TSDQATPVCK GNEWCNSLTI RFTSFGKQAT SWVTGHWWGL RLYVSGHDPG
260 270 280 290 300
LIFGIRLKIT DSGPRVPIGP NPVLSDRRPP SRPRPTRSPP PSNSTPTETP
310 320 330 340 350
LTLPEPPPAG VENRLLNLVK GAYQALNLTS PDKTQECWLC LVSGPPYYEG
360 370 380 390 400
VAVLGTYSNH TSAPANCSVA SQHKLTLSEV TGQGLCIGAV PKTHQVLCNT
410 420 430 440 450
TQKTSDGSYY LAAPTGTTWA CSTGLTPCIS TTILDLTTDY CVLVELWPRV
460 470 480 490 500
TYHSPSYVYH QFERRAKYKR EPVSLTLALL LGGLTMGGIA AGVGTGTTAL
510 520 530 540 550
VATQQFQQLQ AAMHDDLKEV EKSITNLEKS LTSLSEVVLQ NRRGLDLLFL
560 570 580 590 600
KEGGLCAALK EECCFYADHT GLVRDSMAKL RERLSQRQKL FESQQGWFEG
610 620 630 640 650
LFNKSPWFTT LISTIMGPLI ILLLILLFGP CILNRLVQFI KDRISVVQAL
660
VLTQQYHQLK TIEDCKSRE
Length:669
Mass (Da):73,756
Last modified:July 21, 1986 - v1
Checksum:i3A6C3845208A13F2
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti35G → R (PubMed:6294621).Curated1
Sequence conflicti463E → K (PubMed:6294621).Curated1
Sequence conflicti592E → K (PubMed:6294621).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
J01998 Genomic RNA. Translation: AAB03092.1.
V01164 Genomic DNA. Translation: CAA24493.1. Different initiation.
PIRiA92995. VCVWEK.

3D structure databases

ProteinModelPortaliP03386.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.90.310.10. 1 hit.
InterProiIPR008981. FMuLV_rcpt-bd.
IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 2 hits.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]
SUPFAMiSSF49830. SSF49830. 1 hit.
ProtoNetiSearch...

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: October 5, 2016
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.