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Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

 ENV_HV1B1               Reviewed;         856 AA.
P03375; P03376;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 144.
RecName: Full=Envelope glycoprotein gp160 {ECO:0000255|HAMAP-Rule:MF_04083};
AltName: Full=Env polyprotein {ECO:0000255|HAMAP-Rule:MF_04083};
Contains:
RecName: Full=Surface protein gp120 {ECO:0000255|HAMAP-Rule:MF_04083};
Short=SU {ECO:0000255|HAMAP-Rule:MF_04083};
AltName: Full=Glycoprotein 120 {ECO:0000255|HAMAP-Rule:MF_04083};
Short=gp120 {ECO:0000255|HAMAP-Rule:MF_04083};
Contains:
RecName: Full=Transmembrane protein gp41 {ECO:0000255|HAMAP-Rule:MF_04083};
Short=TM {ECO:0000255|HAMAP-Rule:MF_04083};
AltName: Full=Glycoprotein 41 {ECO:0000255|HAMAP-Rule:MF_04083};
Short=gp41 {ECO:0000255|HAMAP-Rule:MF_04083};
Flags: Precursor;
Name=env {ECO:0000255|HAMAP-Rule:MF_04083};
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
(HIV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11678;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2578615; DOI=10.1038/313277a0;
Ratner L., Haseltine W.A., Patarca R., Livak K.J., Starcich B.R.,
Josephs S.F., Doran E.R., Rafalski J.A., Whitehorn E.A.,
Baumeister K., Ivanoff L., Petteway S.R. Jr., Pearson M.L.,
Lautenberger J.A., Papas T.S., Ghrayeb J., Chang N.T., Gallo R.C.,
Wong-Staal F.;
"Complete nucleotide sequence of the AIDS virus, HTLV-III.";
Nature 313:277-284(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Isolate PV22;
PubMed=2982104; DOI=10.1038/313450a0;
Muesing M.A., Smith D.H., Cabradilla C.D., Benton C.V., Lasky L.A.,
Capon D.J.;
"Nucleic acid structure and expression of the human
AIDS/lymphadenopathy retrovirus.";
Nature 313:450-458(1985).
[3]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=2450679; DOI=10.1016/0092-8674(88)90487-4;
McCune J.M., Rabin L.B., Feinberg M.B., Lieberman M., Kosek J.C.,
Reyes G.R., Weissman I.L.;
"Endoproteolytic cleavage of gp160 is required for the activation of
human immunodeficiency virus.";
Cell 53:55-67(1988).
[4]
PROTEIN SEQUENCE OF C-TERMINUS, DISULFIDE BONDS, GLYCOSYLATION AT
ASN-88; ASN-136; ASN-141; ASN-156; ASN-160; ASN-186; ASN-197; ASN-230;
ASN-234; ASN-241; ASN-262; ASN-276; ASN-289; ASN-295; ASN-301;
ASN-332; ASN-339; ASN-356; ASN-386; ASN-392; ASN-397; ASN-406; ASN-448
AND ASN-463, AND STRUCTURE OF CARBOHYDRATES.
PubMed=2355006;
Leonard C.K., Spellman M.W., Riddle L., Harris R.J., Thomas J.N.,
Gregory T.J.;
"Assignment of intrachain disulfide bonds and characterization of
potential glycosylation sites of the type 1 recombinant human
immunodeficiency virus envelope glycoprotein (gp120) expressed in
Chinese hamster ovary cells.";
J. Biol. Chem. 265:10373-10382(1990).
[5]
INTERACTION OF GLYCOPROTEIN 120 WITH HOST CD4.
PubMed=2214026;
Crise B., Buonocore L., Rose J.K.;
"CD4 is retained in the endoplasmic reticulum by the human
immunodeficiency virus type 1 glycoprotein precursor.";
J. Virol. 64:5585-5593(1990).
[6]
INTERACTION OF TRANSMEMBRANE PROTEIN GP41 WITH GALACTOSYL CERAMIDE.
PubMed=11342649; DOI=10.4049/jimmunol.166.10.6257;
Alfsen A., Iniguez P., Bouguyon E., Bomsel M.;
"Secretory IgA specific for a conserved epitope on gp41 envelope
glycoprotein inhibits epithelial transcytosis of HIV-1.";
J. Immunol. 166:6257-6265(2001).
[7]
REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
PubMed=11181151; DOI=10.1086/318823;
Fenouillet E., Barbouche R., Courageot J., Miquelis R.;
"The catalytic activity of protein disulfide isomerase is involved in
human immunodeficiency virus envelope-mediated membrane fusion after
CD4 cell binding.";
J. Infect. Dis. 183:744-752(2001).
[8]
REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
PubMed=12218052; DOI=10.1074/jbc.M205467200;
Barbouche R., Miquelis R., Jones I.M., Fenouillet E.;
"Protein-disulfide isomerase-mediated reduction of two disulfide bonds
of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is
required for fusion.";
J. Biol. Chem. 278:3131-3136(2003).
[9]
REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
PubMed=14592831; DOI=10.1182/blood-2003-05-1390;
Markovic I., Stantchev T.S., Fields K.H., Tiffany L.J., Tomic M.,
Weiss C.D., Broder C.C., Strebel K., Clouse K.A.;
"Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1
envelope-mediated T-cell fusion during viral entry.";
Blood 103:1586-1594(2004).
[10]
REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
PubMed=15644496; DOI=10.1124/mol.104.008276;
Barbouche R., Lortat-Jacob H., Jones I.M., Fenouillet E.;
"Glycosaminoglycans and protein disulfide isomerase-mediated reduction
of HIV Env.";
Mol. Pharmacol. 67:1111-1118(2005).
[11]
REVIEW.
PubMed=12974773; DOI=10.1034/j.1600-0463.2003.11107803.x;
Geijtenbeek T.B., van Kooyk Y.;
"Pathogens target DC-SIGN to influence their fate DC-SIGN functions as
a pathogen receptor with broad specificity.";
APMIS 111:698-714(2003).
[12]
REVIEW.
PubMed=12873764; DOI=10.1016/S0005-2736(03)00161-5;
Gallo S.A., Finnegan C.M., Viard M., Raviv Y., Dimitrov A.,
Rawat S.S., Puri A., Durell S., Blumenthal R.;
"The HIV Env-mediated fusion reaction.";
Biochim. Biophys. Acta 1614:36-50(2003).
[13]
REVIEW.
PubMed=15719026; DOI=10.1038/sj.cdd.4401584;
Perfettini J.-L., Castedo M., Roumier T., Andreau K., Nardacci R.,
Piacentini M., Kroemer G.;
"Mechanisms of apoptosis induction by the HIV-1 envelope.";
Cell Death Differ. 12:916-923(2005).
[14]
REVIEW.
PubMed=15725757; DOI=10.1089/aid.2005.21.171;
Hartley O., Klasse P.J., Sattentau Q.J., Moore J.P.;
"V3: HIV's switch-hitter.";
AIDS Res. Hum. Retroviruses 21:171-189(2005).
[15]
REVIEW.
PubMed=16114975; DOI=10.2165/00003495-200565130-00002;
Reeves J.D., Piefer A.J.;
"Emerging drug targets for antiretroviral therapy.";
Drugs 65:1747-1766(2005).
[16]
REVIEW.
PubMed=16437164; DOI=10.1038/sj.emboj.7600947;
Lusso P.;
"HIV and the chemokine system: 10 years later.";
EMBO J. 25:447-456(2006).
-!- FUNCTION: Envelope glycoprotein gp160: Oligomerizes in the host
endoplasmic reticulum into predominantly trimers. In a second
time, gp160 transits in the host Golgi, where glycosylation is
completed. The precursor is then proteolytically cleaved in the
trans-Golgi and thereby activated by cellular furin or furin-like
proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-
Rule:MF_04083}.
-!- FUNCTION: Surface protein gp120: Attaches the virus to the host
lymphoid cell by binding to the primary receptor CD4. This
interaction induces a structural rearrangement creating a high
affinity binding site for a chemokine coreceptor like CXCR4 and/or
CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR,
which are respectively found on dendritic cells (DCs), and on
endothelial cells of liver sinusoids and lymph node sinuses. These
interactions allow capture of viral particles at mucosal surfaces
by these cells and subsequent transmission to permissive cells.
HIV subverts the migration properties of dendritic cells to gain
access to CD4+ T-cells in lymph nodes. Virus transmission to
permissive T-cells occurs either in trans (without DCs infection,
through viral capture and transmission), or in cis (following DCs
productive infection, through the usual CD4-gp120 interaction),
thereby inducing a robust infection. In trans infection, bound
virions remain infectious over days and it is proposed that they
are not degraded, but protected in non-lysosomal acidic organelles
within the DCs close to the cell membrane thus contributing to the
viral infectious potential during DCs' migration from the
periphery to the lymphoid tissues. On arrival at lymphoid tissues,
intact virions recycle back to DCs' cell surface allowing virus
transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- FUNCTION: Transmembrane protein gp41: 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 fusion
of viral and target intracellular membranes, 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. Complete fusion occurs in host cell
endosomes and is dynamin-dependent, however some lipid transfer
might occur at the plasma membrane. The virus undergoes clathrin-
dependent internalization long before endosomal fusion, thus
minimizing the surface exposure of conserved viral epitopes during
fusion and reducing the efficacy of inhibitors targeting these
epitopes. Membranes fusion leads to delivery of the nucleocapsid
into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- SUBUNIT: The mature envelope protein (Env) consists of a
homotrimer of non-covalently associated gp120-gp41 heterodimers.
The resulting complex protrudes from the virus surface as a spike.
There seems to be as few as 10 spikes on the average virion.
Surface protein gp120 interacts with host CD4, CCR5 and CXCR4.
Gp120 also interacts with the C-type lectins CD209/DC-SIGN and
CLEC4M/DC-SIGNR (collectively referred to as DC-SIGN(R)). Gp120
and gp41 interact with GalCer. Gp120 interacts with host
ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction results in
rapid activation of integrin ITGAL/LFA-1, which facilitates
efficient cell-to-cell spreading of HIV-1. Gp120 interacts with
cell-associated heparan sulfate; this interaction increases virus
infectivity on permissive cells and may be involved in infection
of CD4- cells. {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2214026}.
-!- SUBCELLULAR LOCATION: Surface protein gp120: Virion membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04083}. 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. {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- SUBCELLULAR LOCATION: Transmembrane protein gp41: Virion membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04083}. 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. {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- DOMAIN: Some of the most genetically diverse regions of the viral
genome are present in Env. They are called variable regions 1
through 5 (V1 through V5). Coreceptor usage of gp120 is determined
mainly by the primary structure of the third variable region (V3)
in the outer domain of gp120. The sequence of V3 determines which
coreceptor, CCR5 and/or CXCR4 (corresponding to R5/macrophage,
X4/T cell and R5X4/T cell and macrophage tropism), is used to
trigger the fusion potential of the Env complex, and hence which
cells the virus can infect. Binding to CCR5 involves a region
adjacent in addition to V3. {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- DOMAIN: The membrane proximal external region (MPER) present in
gp41 is a tryptophan-rich region recognized by the antibodies 2F5,
Z13, and 4E10. MPER seems to play a role in fusion.
{ECO:0000255|HAMAP-Rule:MF_04083}.
-!- DOMAIN: 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. {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- DOMAIN: The YXXL motif is involved in determining the exact site
of viral release at the surface of infected mononuclear cells and
promotes endocytosis. YXXL and di-leucine endocytosis motifs
interact directly or indirectly with the clathrin adapter
complexes, opperate independently, and their activities are not
additive. {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- DOMAIN: The CD4-binding region is targeted by the antibody b12.
{ECO:0000255|HAMAP-Rule:MF_04083}.
-!- PTM: Highly glycosylated by host. The high number of glycan on the
protein is reffered to as 'glycan shield' because it contributes
to hide protein sequence from adaptive immune system.
{ECO:0000255|HAMAP-Rule:MF_04083}.
-!- PTM: Palmitoylation of the transmembrane protein and of Env
polyprotein (prior to its proteolytic cleavage) is essential for
their association with host cell membrane lipid rafts.
Palmitoylation is therefore required for envelope trafficking to
classical lipid rafts, but not for viral replication.
{ECO:0000255|HAMAP-Rule:MF_04083}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Envelope glycoproteins are synthesized as a inactive precursor
that is heavily N-glycosylated and processed likely by host cell
furin 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. About 2 of the 9 disulfide bonds of gp41 are
reduced by P4HB/PDI, following binding to CD4 receptor.
{ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:12218052,
ECO:0000269|PubMed:14592831, ECO:0000269|PubMed:15644496}.
-!- MISCELLANEOUS: Inhibitors targeting HIV-1 viral envelope proteins
are used as antiretroviral drugs. Attachment of virions to the
cell surface via non-specific interactions and CD4 binding can be
blocked by inhibitors that include cyanovirin-N,
cyclotriazadisulfonamide analogs, PRO 2000, TNX 355 and PRO 542.
In addition, BMS 806 can block CD4-induced conformational changes.
Env interactions with the coreceptor molecules can be targeted by
CCR5 antagonists including SCH-D, maraviroc (UK 427857) and
aplaviroc (GW 873140), and the CXCR4 antagonist AMD 070. Fusion of
viral and cellular membranes can be inhibited by peptides such as
enfuvirtide and tifuvirtide (T 1249). Resistance to inhibitors
associated with mutations in Env are observed. Most of the time,
single mutations confer only a modest reduction in drug
susceptibility. Combination of several mutations is usually
required to develop a high-level drug resistance.
{ECO:0000255|HAMAP-Rule:MF_04083}.
-!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M
(for Major), O (for Outlier), and N (for New, or Non-M, Non-O).
The vast majority of strains found worldwide belong to the group
M. Group O seems to be endemic to and largely confined to Cameroon
and neighboring countries in West Central Africa, where these
viruses represent a small minority of HIV-1 strains. The group N
is represented by a limited number of isolates from Cameroonian
persons. The group M is further subdivided in 9 clades or subtypes
(A to D, F to H, J and K). {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- SIMILARITY: Belongs to the HIV-1 env protein family.
{ECO:0000255|HAMAP-Rule:MF_04083}.
-!- WEB RESOURCE: Name=hivdb; Note=HIV drug resistance database;
URL="http://hivdb.stanford.edu";
-!- WEB RESOURCE: Name=BioAfrica: HIV bioinformatics in Africa;
URL="http://www.bioafrica.net/index.html";
-!- WEB RESOURCE: Name=HIV drug resistance mutations;
URL="https://www.iasusa.org/content/hiv-drug-resistance-mutations";
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EMBL; M15654; AAA44205.1; -; Genomic_RNA.
EMBL; K02083; AAB59873.1; -; Genomic_DNA.
EMBL; X01762; CAA25903.1; ALT_SEQ; Genomic_RNA.
PIR; A03973; VCLJH3.
PIR; A03974; VCLJVL.
PDB; 2ARI; NMR; -; A=512-541.
PDB; 3VGY; X-ray; 2.03 A; C=546-588.
PDB; 3VH7; X-ray; 2.02 A; A/C/E=546-588.
PDB; 3VU5; X-ray; 2.09 A; A=553-590.
PDB; 3VU6; X-ray; 2.32 A; A=553-590.
PDB; 3W19; X-ray; 1.28 A; C=553-590.
PDBsum; 2ARI; -.
PDBsum; 3VGY; -.
PDBsum; 3VH7; -.
PDBsum; 3VU5; -.
PDBsum; 3VU6; -.
PDBsum; 3W19; -.
ProteinModelPortal; P03375; -.
SMR; P03375; -.
MINT; MINT-1523031; -.
ChEMBL; CHEMBL5057; -.
iPTMnet; P03375; -.
OrthoDB; VOG09000036; -.
Reactome; R-HSA-5621480; Dectin-2 family.
EvolutionaryTrace; P03375; -.
PMAP-CutDB; P03376; -.
Proteomes; UP000007690; Genome.
Proteomes; UP000107234; Genome.
Proteomes; UP000126245; Genome.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0044538; C:host cell periphery; IDA:UniProtKB.
GO; GO:0020002; C:host cell plasma membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; TAS:Reactome.
GO; GO:0019012; C:virion; ISS:UniProtKB.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0042609; F:CD4 receptor binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; ISS:UniProtKB.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; ISS:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0019082; P:viral protein processing; ISS:UniProtKB.
GO; GO:0019062; P:virion attachment to host cell; ISS:UniProtKB.
CDD; cd09909; HIV-1-like_HR1-HR2; 1.
Gene3D; 2.170.40.20; -; 2.
HAMAP; MF_04083; HIV_ENV; 1.
InterPro; IPR036377; Gp120_core_sf.
InterPro; IPR000328; GP41-like.
InterPro; IPR000777; HIV1_Gp120.
Pfam; PF00516; GP120; 1.
Pfam; PF00517; GP41; 1.
SUPFAM; SSF56502; SSF56502; 3.
1: Evidence at protein level;
3D-structure; AIDS; Apoptosis;
Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Coiled coil; Complete proteome;
Direct protein sequencing; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host endosome; Host membrane;
Host-virus interaction; Lipoprotein; Membrane; Palmitate;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
SIGNAL 1 32 {ECO:0000255|HAMAP-Rule:MF_04083}.
CHAIN 33 856 Envelope glycoprotein gp160.
{ECO:0000255|HAMAP-Rule:MF_04083}.
/FTId=PRO_0000239239.
CHAIN 33 511 Surface protein gp120.
{ECO:0000255|HAMAP-Rule:MF_04083}.
/FTId=PRO_0000038371.
CHAIN 512 856 Transmembrane protein gp41.
{ECO:0000255|HAMAP-Rule:MF_04083}.
/FTId=PRO_0000038372.
TOPO_DOM 33 684 Extracellular. {ECO:0000255|HAMAP-
Rule:MF_04083}.
TRANSMEM 685 705 Helical. {ECO:0000255|HAMAP-
Rule:MF_04083}.
TOPO_DOM 706 856 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 131 156 V1. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 157 196 V2. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 296 330 V3. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 364 374 CD4-binding loop. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 385 418 V4. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 461 471 V5.
REGION 463 471 V5. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 512 532 Fusion peptide. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 574 592 Immunosuppression. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 662 683 MPER; binding to GalCer.
{ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 662 667 Involved in GalCer binding.
COILED 633 667 {ECO:0000255|HAMAP-Rule:MF_04083}.
MOTIF 712 715 YXXL motif; contains endocytosis signal.
{ECO:0000255|HAMAP-Rule:MF_04083}.
MOTIF 855 856 Di-leucine internalization motif.
{ECO:0000255|HAMAP-Rule:MF_04083}.
SITE 511 512 Cleavage; by host furin.
{ECO:0000255|HAMAP-Rule:MF_04083}.
LIPID 764 764 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 339 339 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
CARBOHYD 611 611 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 616 616 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 625 625 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 637 637 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 674 674 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 54 74 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
DISULFID 119 205 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
DISULFID 126 196 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
DISULFID 131 157 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
DISULFID 218 247 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
DISULFID 228 239 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
DISULFID 296 331 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
DISULFID 378 445 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
DISULFID 385 418 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:2355006}.
DISULFID 598 604 {ECO:0000255|HAMAP-Rule:MF_04083}.
VARIANT 403 403 K -> E (in strain: Isolate PV22).
VARIANT 423 423 I -> F (in strain: Isolate PV22).
VARIANT 461 461 S -> N (in strain: Isolate PV22).
VARIANT 668 668 S -> N (in strain: Isolate PV22).
VARIANT 673 673 F -> L (in strain: Isolate PV22).
VARIANT 704 704 V -> I (in strain: Isolate PV22).
VARIANT 723 723 I -> T (in strain: Isolate PV22).
VARIANT 737 737 G -> D (in strain: Isolate PV22).
HELIX 516 530 {ECO:0000244|PDB:2ARI}.
TURN 531 533 {ECO:0000244|PDB:2ARI}.
STRAND 536 538 {ECO:0000244|PDB:2ARI}.
HELIX 554 589 {ECO:0000244|PDB:3W19}.
SEQUENCE 856 AA; 97225 MW; 0BFFB1A18931BB27 CRC64;
MRVKEKYQHL WRWGWRWGTM LLGMLMICSA TEKLWVTVYY GVPVWKEATT TLFCASDAKA
YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM VEQMHEDIIS LWDQSLKPCV
KLTPLCVSLK CTDLKNDTNT NSSSGRMIME KGEIKNCSFN ISTSIRGKVQ KEYAFFYKLD
IIPIDNDTTS YTLTSCNTSV ITQACPKVSF EPIPIHYCAP AGFAILKCNN KTFNGTGPCT
NVSTVQCTHG IRPVVSTQLL LNGSLAEEEV VIRSANFTDN AKTIIVQLNQ SVEINCTRPN
NNTRKSIRIQ RGPGRAFVTI GKIGNMRQAH CNISRAKWNN TLKQIDSKLR EQFGNNKTII
FKQSSGGDPE IVTHSFNCGG EFFYCNSTQL FNSTWFNSTW STKGSNNTEG SDTITLPCRI
KQIINMWQEV GKAMYAPPIS GQIRCSSNIT GLLLTRDGGN SNNESEIFRP GGGDMRDNWR
SELYKYKVVK IEPLGVAPTK AKRRVVQREK RAVGIGALFL GFLGAAGSTM GAASMTLTVQ
ARQLLSGIVQ QQNNLLRAIE AQQHLLQLTV WGIKQLQARI LAVERYLKDQ QLLGIWGCSG
KLICTTAVPW NASWSNKSLE QIWNNMTWME WDREINNYTS LIHSLIEESQ NQQEKNEQEL
LELDKWASLW NWFNITNWLW YIKLFIMIVG GLVGLRIVFA VLSVVNRVRQ GYSPLSFQTH
LPIPRGPDRP EGIEEEGGER DRDRSIRLVN GSLALIWDDL RSLCLFSYHR LRDLLLIVTR
IVELLGRRGW EALKYWWNLL QYWSQELKNS AVSLLNATAI AVAEGTDRVI EVVQGAYRAI
RHIPRRIRQG LERILL


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