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Protein

Envelope glycoprotein

Gene

env

Organism
Hortulanus murine leukemia virus (HoMuLV) (Mus hortulanus 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 bindingi115ZincBy 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 76
Short name:
gp76
Transmembrane protein
Short name:
TM
Alternative name(s):
Envelope protein p15E
Alternative name(s):
p2E
Gene namesi
Name:env
OrganismiHortulanus murine leukemia virus (HoMuLV) (Mus hortulanus virus)
Taxonomic identifieri11799 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusMurine leukemia virus
Virus hostiMus musculus (Mouse) [TaxID: 10090]

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 domaini34 – 607ExtracellularSequence analysisAdd BLAST574
Transmembranei608 – 628HelicalSequence analysisAdd BLAST21
Topological domaini629 – 666CytoplasmicSequence analysisAdd BLAST38

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 – 33Sequence analysisAdd BLAST33
ChainiPRO_000023958534 – 666Envelope glycoproteinAdd BLAST633
ChainiPRO_000004076034 – 466Surface proteinBy similarityAdd BLAST433
ChainiPRO_0000040761467 – 646Transmembrane proteinBy similarityAdd BLAST180
PeptideiPRO_0000239586647 – 666R-peptideBy similarityAdd BLAST20

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi42N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi76 ↔ 127By similarity
Disulfide bondi102 ↔ 116By similarity
Disulfide bondi103 ↔ 112By similarity
Disulfide bondi150 ↔ 170By similarity
Disulfide bondi162 ↔ 175By similarity
Glycosylationi197N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi207 ↔ 213By similarity
Glycosylationi290N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi324N-linked (GlcNAc...); by hostBy similarity1
Disulfide bondi334 ↔ 560Interchain (between SU and TM chains, or C-337 with C-560); in linked form
Disulfide bondi334 ↔ 337
Glycosylationi356N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi363N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi364 ↔ 417By similarity
Disulfide bondi424 ↔ 437By similarity
Glycosylationi431N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi552 ↔ 560By similarity
Lipidationi627S-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
Sitei466 – 467Cleavage; by hostBy similarity2
Sitei646 – 647Cleavage; 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

ProteinModelPortaliP21436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni31 – 264Receptor-binding domain (RBD)Sequence analysisAdd BLAST234
Regioni469 – 489Fusion peptideBy similarityAdd BLAST21
Regioni535 – 551ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili500 – 534Sequence analysisAdd BLAST35

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi334 – 337CXXC4
Motifi552 – 560CX6CC9
Motifi652 – 655YXXL motif; contains endocytosis signalBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi261 – 304Pro-richAdd BLAST44

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.

P21436-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRPALPKSI KDKTNPWGPI ILGILIMLGG ALGKGSPHKV FNLTWEVYNQ
60 70 80 90 100
EYETVWATSG SHPLWTWWPT LTPDLCMLAQ LAKPSWGLSD YPPYSKPPGP
110 120 130 140 150
PCCTTDNNPP GCSRDCNGPL TYLTPRCSTA WNRLKLVLTT HHLNQGFYVC
160 170 180 190 200
PGPHRPRHAR NCGGPDDFYC AHWGCETTGQ AYWKPSSSWD YIRVSNNASS
210 220 230 240 250
SDATTACKNN NWCSPLAISF TDPGKRATSW TSGFTWGLRL YISGHPGLIF
260 270 280 290 300
GVRLKISDLG PRVPIGPNPV LSEQRPPSQP EPARLPPSSN LTQGGTPSAP
310 320 330 340 350
TGPPQEGTGD RLLDLVQGAY QALNATSPDK TQECWLCLVS SPPYYEGVAV
360 370 380 390 400
VGPYSNHTTA PANCSADSQH KLTLSEVTGK PLPRKGSQDP PGPVQYHSGA
410 420 430 440 450
RQKYSLSGGS RGTMWACNTG LTPCLSTAVL NLTTDYCVLV ELWPRVTYHS
460 470 480 490 500
LDFVYRQVEG RTRYQREPVS LTLALLLGGL TMGGIAAGVG TGTSALVKTQ
510 520 530 540 550
QFEQLHAAIQ ADLKEVESSI TNLEKSLTSL SEVVLQNRRG LDLLFLEKGG
560 570 580 590 600
LCAALKEECC FYADHTGLVR DSMAKLRERL NQRQKLFEAG QGWFEGLFNR
610 620 630 640 650
SPWLTTLIST IMGPLIILLL ILMFGPCILN RLVQFVKDRI SVVQALVLTQ
660
QYHQLKPLEH GRAIVK
Length:666
Mass (Da):73,035
Last modified:May 1, 1991 - v1
Checksum:iFDC77956E4B213D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26527 Genomic RNA. No translation available.
PIRiB32594. VCMVHL.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26527 Genomic RNA. No translation available.
PIRiB32594. VCMVHL.

3D structure databases

ProteinModelPortaliP21436.
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_MLVHO
AccessioniPrimary (citable) accession number: P21436
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 5, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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.