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Protein

Envelope glycoprotein gp63

Gene

env

Organism
Human T-cell leukemia virus 2 (HTLV-2)
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

GO - Biological processi

Complete GO annotation...

Keywordsi

Biological processFusion 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 gp63
Alternative name(s):
Env polyprotein
Cleaved into the following 2 chains:
Surface protein
Short name:
SU
Alternative name(s):
Glycoprotein 46
Short name:
gp46
Transmembrane protein
Short name:
TM
Alternative name(s):
Glycoprotein 21
Short name:
gp21
Gene namesi
Name:env
OrganismiHuman T-cell leukemia virus 2 (HTLV-2)
Taxonomic identifieri11909 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeDeltaretrovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009254 Componenti: Genome

Subcellular locationi

Transmembrane protein :
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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 438ExtracellularSequence analysisAdd BLAST420
Transmembranei439 – 459HelicalSequence analysisAdd BLAST21
Topological domaini460 – 486CytoplasmicSequence analysisAdd BLAST27

GO - Cellular componenti

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000023954419 – 486Envelope glycoprotein gp63Add BLAST468
ChainiPRO_000003876119 – 308Surface proteinBy similarityAdd BLAST290
ChainiPRO_0000038762309 – 486Transmembrane proteinBy similarityAdd BLAST178

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi136N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi218N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi221 ↔ 397Interchain (between SU and TM chains, or C-224 with C-397); in linked formBy similarity
Disulfide bondi221 ↔ 224By similarity
Glycosylationi240N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi286N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi389 ↔ 396By similarity
Glycosylationi400N-linked (GlcNAc...); by hostSequence analysis1
Lipidationi458S-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 (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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei308 – 309Cleavage; by host furin2

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

Binary interactionsi

WithEntry#Exp.IntActNotes
MED7O435133EBI-9676086,EBI-394632From Homo sapiens.

Protein-protein interaction databases

IntActiP03383. 1 interactor.

Structurei

3D structure databases

ProteinModelPortaliP03383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni309 – 329Fusion peptideSequence analysisAdd BLAST21
Regioni372 – 388ImmunosuppressionBy similarityAdd BLAST17

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili337 – 383Sequence analysisAdd BLAST47
Coiled coili393 – 425Sequence analysisAdd BLAST33

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi221 – 224CXXC4
Motifi389 – 397CX6CC9

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

Phylogenomic databases

KOiK19259.

Family and domain databases

InterProiIPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P03383-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNVFFLLLF SLTHFPLAQQ SRCTLTIGIS SYHSSPCSPT QPVCTWNLDL
60 70 80 90 100
NSLTTDQRLH PPCPNLITYS GFHKTYSLYL FPHWIKKPNR QGLGYYSPSY
110 120 130 140 150
NDPCSLQCPY LGCQAWTSAY TGPVSSPSWK FHSDVNFTQE VSQVSLRLHF
160 170 180 190 200
SKCGSSMTLL VDAPGYDPLW FITSEPTQPP PTSPPLVHDS DLEHVLTPST
210 220 230 240 250
SWTTKILKFI QLTLQSTNYS CMVCVDRSSL SSWHVLYTPN ISIPQQTSSR
260 270 280 290 300
TILFPSLALP APPSQPFPWT HCYQPRLQAI TTDNCNNSII LPPFSLAPVP
310 320 330 340 350
PPATRRRRAV PIAVWLVSAL AAGTGIAGGV TGSLSLASSK SLLLEVDKDI
360 370 380 390 400
SHLTQAIVKN HQNILRVAQY AAQNRRGLDL LFWEQGGLCK AIQEQCCFLN
410 420 430 440 450
ISNTHVSVLQ ERPPLEKRVI TGWGLNWDLG LSQWAREALQ TGITILALLL
460 470 480
LVILFGPCIL RQIQALPQRL QNRHNQYSLI NPETML
Length:486
Mass (Da):54,158
Last modified:July 21, 1986 - v1
Checksum:i60D70B9CE8986CE5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27I → V in AAA45410 (PubMed:6204380).Curated1
Sequence conflicti56D → H in AAA45410 (PubMed:6204380).Curated1
Sequence conflicti115A → S in AAA45410 (PubMed:6204380).Curated1
Sequence conflicti118 – 119SA → CP in AAA45410 (PubMed:6204380).Curated2
Sequence conflicti267F → P (PubMed:6204380).Curated1
Sequence conflicti302P → L in AAA45410 (PubMed:6204380).Curated1
Sequence conflicti318S → P in AAA45410 (PubMed:6204380).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10060 Genomic DNA. Translation: AAB59887.1.
K02024 Genomic RNA. Translation: AAA45410.1.
PIRiA03980. VCLJT2.
A03981. VCLJH2.
RefSeqiNP_041006.1. NC_001488.1.

Genome annotation databases

GeneIDi1491942.
KEGGivg:1491942.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10060 Genomic DNA. Translation: AAB59887.1.
K02024 Genomic RNA. Translation: AAA45410.1.
PIRiA03980. VCLJT2.
A03981. VCLJH2.
RefSeqiNP_041006.1. NC_001488.1.

3D structure databases

ProteinModelPortaliP03383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP03383. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1491942.
KEGGivg:1491942.

Phylogenomic databases

KOiK19259.

Family and domain databases

InterProiIPR018154. TLV/ENV_coat_polyprotein.
[Graphical view]
PANTHERiPTHR10424. PTHR10424. 1 hit.
PfamiPF00429. TLV_coat. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENV_HTLV2
AccessioniPrimary (citable) accession number: P03383
Secondary accession number(s): P03382
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 5, 2016
This is version 103 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.