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P31796

- ENV_AVISN

UniProt

P31796 - ENV_AVISN

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Protein

Envelope glycoprotein

Gene

env

Organism
Avian spleen necrosis virus
Status
Reviewed - Annotation score: 4 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).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
Sitei398 – 3992Cleavage; by hostBy similarity

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 2 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 73
Short name:
gp73
Transmembrane protein
Short name:
TM
Alternative name(s):
Glycoprotein 22
Short name:
gp22
Gene namesi
Name:env
OrganismiAvian spleen necrosis virus
Taxonomic identifieri11899 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirus
Virus hostiGalliformes [TaxID: 8976]

Subcellular locationi

Chain Transmembrane protein : Virion membrane By similarity; Single-pass type I membrane protein By similarity. Host cell membrane By similarity; Single-pass type I membrane protein By similarity
Note: It is probably 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
Chain Surface protein : Virion membrane By similarity; Peripheral membrane protein By similarity. 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 extravirion surface through its binding to TM. It is probably 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

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. 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 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 567532Envelope glycoproteinPRO_0000239547Add
BLAST
Chaini36 – 398363Surface proteinBy similarityPRO_0000040685Add
BLAST
Chaini399 – 567169Transmembrane proteinBy similarityPRO_0000040686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi245 – 2451N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi255 ↔ 487Interchain (between SU and TM chains, or C-258 with C-487); in linked formBy similarity
Disulfide bondi255 ↔ 258By similarity
Glycosylationi274 – 2741N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi280 – 2801N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi306 – 3061N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi319 – 3191N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi328 – 3281N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi335 – 3351N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi479 ↔ 486By similarity
Glycosylationi491 – 4911N-linked (GlcNAc...); by hostSequence Analysis
Lipidationi549 – 5491S-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 (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

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

ProteinModelPortaliP31796.
SMRiP31796. Positions 439-491.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 525490ExtracellularSequence AnalysisAdd
BLAST
Topological domaini547 – 56721CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei526 – 54621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni402 – 42221Fusion peptideSequence AnalysisAdd
BLAST
Regioni462 – 47817ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili423 – 47351Sequence AnalysisAdd
BLAST
Coiled coili483 – 51937Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi255 – 2584CXXC
Motifi479 – 4879CX6CC

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).By similarity

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P31796-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDCLTNLRSA EGKVDQASKI LILLVAWWGF GTTAEGYPLQ QLWELPCDCS
60 70 80 90 100
GGYVSSIPTY YTYSLDCGGS TAYLTYGSGT GSWSWGGGFK QQWECVFKPK
110 120 130 140 150
IIPSVQGQPG PCPSECLQIA TQMHSTCYEK TQECTLLGKT YFTAILQKTK
160 170 180 190 200
LGSYEDGPNK LIQASCTGTV GKPVCWDPVA PVYVSDGGGP TDMIREESVR
210 220 230 240 250
ERLEEIIRHS YPSVQYHPLA LPRSRGVDLD PQTSDILEAT HQVLNATNPK
260 270 280 290 300
LAENCWLCMT LGTPIPAAIP TNGNVTLDGN CSLSLPFGCN PPGSIDVSCY
310 320 330 340 350
AGEADNRTGI PVGYVHFTNC TSIQEVTNET SQMGNLTRLC PPPGHVFVCG
360 370 380 390 400
NNMAYTALPN KWIGLCILAS IVPDISIISG EEPIPLPSIE YTARRHKRAV
410 420 430 440 450
QFIPLLVGLG ISGATLAGGT GLGVSVHTYH KLSNQLIEDV QALSGTINDL
460 470 480 490 500
QDQIDSLAEV VLQNRRGLDL LTAEQGGICL ALQEKCCFYA NKSGIVRDKI
510 520 530 540 550
RKLQEDLIER KRALYDNPLW SGLNGFLPYL LPLLGPLFGL ILFLTLGPCI
560
MKTLTRIIHD KIQAVKS
Length:567
Mass (Da):61,597
Last modified:July 1, 1993 - v1
Checksum:i204EA57C32159175
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87666 Genomic DNA. No translation available.
PIRiA38212. VCFVAS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M87666 Genomic DNA. No translation available.
PIRi A38212. VCFVAS.

3D structure databases

ProteinModelPortali P31796.
SMRi P31796. Positions 439-491.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR018154. TLV/ENV_coat_polyprotein.
[Graphical view ]
PANTHERi PTHR10424. PTHR10424. 1 hit.
Pfami PF00429. TLV_coat. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Spleen necrosis virus, an avian immunosuppressive retrovirus, shares a receptor with the type D simian retroviruses."
    Kewalramani V.N., Panganiban A.T., Emerman M.
    J. Virol. 66:3026-3031(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Clone PPB101.

Entry informationi

Entry nameiENV_AVISN
AccessioniPrimary (citable) accession number: P31796
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program