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P21436

- ENV_MLVHO

UniProt

P21436 - ENV_MLVHO

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Protein

Envelope glycoprotein

Gene

env

Organism
Hortulanus murine leukemia virus (HoMuLV) (Mus hortulanus 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).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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi115 – 1151ZincBy similarity
Sitei466 – 4672Cleavage; by hostBy similarity
Sitei646 – 6472Cleavage; by viral protease p14By 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 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

Chain 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
R-peptide : Host cell membrane By similarity; Peripheral membrane protein By similarity
Note: The R-peptide is membrane-associated through its palmitate.By similarity

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral capsid Source: InterPro
  4. viral envelope Source: UniProtKB-KW
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 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 666633Envelope glycoproteinPRO_0000239585Add
BLAST
Chaini34 – 466433Surface proteinBy similarityPRO_0000040760Add
BLAST
Chaini467 – 646180Transmembrane proteinBy similarityPRO_0000040761Add
BLAST
Peptidei647 – 66620R-peptideBy similarityPRO_0000239586Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...); by hostBy similarity
Disulfide bondi76 ↔ 127By similarity
Disulfide bondi102 ↔ 116By similarity
Disulfide bondi103 ↔ 112By similarity
Disulfide bondi150 ↔ 170By similarity
Disulfide bondi162 ↔ 175By similarity
Glycosylationi197 – 1971N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi207 ↔ 213By similarity
Glycosylationi290 – 2901N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...); by hostBy similarity
Disulfide bondi334 ↔ 560Interchain (between SU and TM chains, or C-337 with C-560); in linked form
Disulfide bondi334 ↔ 337
Glycosylationi356 – 3561N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi363 – 3631N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi364 ↔ 417By similarity
Disulfide bondi424 ↔ 437By similarity
Glycosylationi431 – 4311N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi552 ↔ 560By similarity
Lipidationi627 – 6271S-palmitoyl cysteine; by hostBy 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).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

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.
SMRiP21436. Positions 39-263, 512-564.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 607574ExtracellularSequence AnalysisAdd
BLAST
Topological domaini629 – 66638CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei608 – 62821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni31 – 264234Receptor-binding domain (RBD)Sequence AnalysisAdd
BLAST
Regioni469 – 48921Fusion peptideBy similarityAdd
BLAST
Regioni535 – 55117ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili500 – 53435Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi334 – 3374CXXC
Motifi552 – 5609CX6CC
Motifi652 – 6554YXXL motif; contains endocytosis signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi261 – 30444Pro-richAdd
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).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.

P21436-1 [UniParc]FASTAAdd to Basket

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        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:
EMBL
GenBank
DDBJ
Links Updated
M26527 Genomic RNA. No translation available.
PIRiB32594. VCMVHL.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26527 Genomic RNA. No translation available.
PIRi B32594. VCMVHL.

3D structure databases

ProteinModelPortali P21436.
SMRi P21436. Positions 39-263, 512-564.
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 and mode of transmission of the wild mouse ecotropic virus, HoMuLV."
    Voytek P., Kozak C.A.
    Virology 173:58-67(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

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 29, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program