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Q9TTC0

- ENV_KORV

UniProt

Q9TTC0 - ENV_KORV

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Protein

Envelope glycoprotein

Gene

env

Organism
Koala retrovirus (KoRV)
Status
Reviewed - Annotation score: 5 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
Sitei463 – 4642Cleavage; by hostBy similarity
Sitei643 – 6442Cleavage; by viral proteaseBy similarity

GO - Molecular functioni

  1. 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

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
OrganismiKoala retrovirus (KoRV)
Taxonomic identifieri394239 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeGammaretrovirusunclassified Gammaretrovirus
Virus hostiPhascolarctos cinereus (Koala) [TaxID: 38626]
ProteomesiUP000007765: Genome

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 extravirion 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 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 659624Envelope glycoproteinPRO_0000249423Add
BLAST
Chaini36 – 463428Surface proteinBy similarityPRO_0000249424Add
BLAST
Chaini464 – 659196Transmembrane proteinBy similarityPRO_0000249425Add
BLAST
Peptidei645 – 65915R-peptideBy similarityPRO_0000249426Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi141 ↔ 162By similarity
Disulfide bondi154 ↔ 167By similarity
Glycosylationi318 – 3181N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi328 ↔ 558Interchain (between SU and TM chains, or C-357 with C-584); in linked formBy similarity
Disulfide bondi328 ↔ 331By similarity
Glycosylationi389 – 3891N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi395 – 3951N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi407 – 4071N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi427 – 4271N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi550 ↔ 557By similarity
Lipidationi625 – 6251S-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

ProteinModelPortaliQ9TTC0.
SMRiQ9TTC0. Positions 510-562.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 606571ExtracellularSequence AnalysisAdd
BLAST
Topological domaini628 – 65932CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei607 – 62721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni466 – 48621Fusion peptideBy similarityAdd
BLAST
Regioni533 – 54917ImmunosuppressionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili506 – 53227Sequence AnalysisAdd
BLAST
Coiled coili567 – 58721Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi328 – 3314CXXCBy similarity
Motifi550 – 5589CX6CCBy similarity
Motifi650 – 6534YXXL motif; contains endocytosis signalBy similarity

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

Q9TTC0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLISNPRHL GHPMSPGNWK RLIILLSCVF GGAEMNQQHN NPHQPMTLTW
60 70 80 90 100
QVLSQTGSVV WEKKAVEPPW TWWPSLEPDV CALVAGLESW DIPELTASAS
110 120 130 140 150
QQARPPDSNY EHAYNQITWG TLGCSYPRAR TRIARSQFYV CPRDGRSLSE
160 170 180 190 200
ARRCGGLESL YCKEWGCETA GTAYWQPRSS WDLITVGQGH PTGTCERTGW
210 220 230 240 250
CNPLKIEFTE PGKRFRNWLQ GRTWGLRFYV TGHPGVQLTI RLVITSPPPV
260 270 280 290 300
VVGPDPVLAE QGPPRKIPFL PRVPVPTLSP PASPIPTVQA SPPAPSTPSP
310 320 330 340 350
TTGDRLFGLV QGAFLALNAT NPEATESCWL CLALGPPYYE GIATPGQVTY
360 370 380 390 400
ASTDSQCRWG GKGKLTLTEV SGLGLCIGKV PPTHQHLCNL TIPLNASHTH
410 420 430 440 450
KYLLPSNRSW WACNSGLTPC LSTSVFNQSN DFCIQIQLVP RIYYHPDGTL
460 470 480 490 500
LQAYESPHSR NKREPVSLTL AVLLGLGVAA GIGTGSTALI KGPIDLQQGL
510 520 530 540 550
TSLQIAMDTD LRALQDSISK LEDSLTSLSE VVLQNRRGLD LLFLKEGGLC
560 570 580 590 600
AALKEECCFY VDHSGAVRDS MRRLKERLDK RQLEHQKNLS WYEGWFNRSP
610 620 630 640 650
WLTTLLSALA GPLLLLLLLL TLGPCVINKL VQFINDRVSA VRILVLRHKY

QTLDNEDNL
Length:659
Mass (Da):72,860
Last modified:May 1, 2000 - v1
Checksum:i68B2220DAA6A2ABA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF151794 Genomic DNA. Translation: AAF15099.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF151794 Genomic DNA. Translation: AAF15099.1 .

3D structure databases

ProteinModelPortali Q9TTC0.
SMRi Q9TTC0. Positions 510-562.
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. "The nucleotide sequence of koala (Phascolarctos cinereus) retrovirus: a novel type C endogenous virus related to Gibbon ape leukemia virus."
    Hanger J.J., Bromham L.D., McKee J.J., O'Brien T.M., Robinson W.F.
    J. Virol. 74:4264-4272(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiENV_KORV
AccessioniPrimary (citable) accession number: Q9TTC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Koala retrovirus is both a circulating virus and an endogenous retrovirus of koala, except in some isolated populations in south Australia.

Keywords - Technical termi

Complete proteome

External Data

Dasty 3