ENV_HV1Y2
ID ENV_HV1Y2 Reviewed; 843 AA.
AC P35961;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Envelope glycoprotein gp160 {ECO:0000255|HAMAP-Rule:MF_04083};
DE AltName: Full=Env polyprotein {ECO:0000255|HAMAP-Rule:MF_04083};
DE Contains:
DE RecName: Full=Surface protein gp120 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Short=SU {ECO:0000255|HAMAP-Rule:MF_04083};
DE AltName: Full=Glycoprotein 120 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Short=gp120 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Contains:
DE RecName: Full=Transmembrane protein gp41 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Short=TM {ECO:0000255|HAMAP-Rule:MF_04083};
DE AltName: Full=Glycoprotein 41 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Short=gp41 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Flags: Precursor;
GN Name=env {ECO:0000255|HAMAP-Rule:MF_04083};
OS Human immunodeficiency virus type 1 group M subtype B (isolate YU-2)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=362651;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1404605; DOI=10.1128/jvi.66.11.6587-6600.1992;
RA Li Y., Hui H., Burgess C.J., Price R.W., Sharp P.M., Hahn B.H., Shaw G.M.;
RT "Complete nucleotide sequence, genome organization, and biological
RT properties of human immunodeficiency virus type 1 in vivo: evidence for
RT limited defectiveness and complementation.";
RL J. Virol. 66:6587-6600(1992).
RN [2]
RP INTERACTION OF SURFACE PROTEIN GP120 WITH HUMAN CCR5.
RX PubMed=9632396; DOI=10.1126/science.280.5371.1949;
RA Rizzuto C.D., Wyatt R., Hernandez-Ramos N., Sun Y., Kwong P.D.,
RA Hendrickson W.A., Sodroski J.;
RT "A conserved HIV gp120 glycoprotein structure involved in chemokine
RT receptor binding.";
RL Science 280:1949-1953(1998).
RN [3]
RP REVIEW.
RX PubMed=12974773; DOI=10.1034/j.1600-0463.2003.11107803.x;
RA Geijtenbeek T.B., van Kooyk Y.;
RT "Pathogens target DC-SIGN to influence their fate DC-SIGN functions as a
RT pathogen receptor with broad specificity.";
RL APMIS 111:698-714(2003).
RN [4]
RP REVIEW.
RX PubMed=12873764; DOI=10.1016/s0005-2736(03)00161-5;
RA Gallo S.A., Finnegan C.M., Viard M., Raviv Y., Dimitrov A., Rawat S.S.,
RA Puri A., Durell S., Blumenthal R.;
RT "The HIV Env-mediated fusion reaction.";
RL Biochim. Biophys. Acta 1614:36-50(2003).
RN [5]
RP REVIEW.
RX PubMed=15719026; DOI=10.1038/sj.cdd.4401584;
RA Perfettini J.-L., Castedo M., Roumier T., Andreau K., Nardacci R.,
RA Piacentini M., Kroemer G.;
RT "Mechanisms of apoptosis induction by the HIV-1 envelope.";
RL Cell Death Differ. 12:916-923(2005).
RN [6]
RP REVIEW.
RX PubMed=15725757; DOI=10.1089/aid.2005.21.171;
RA Hartley O., Klasse P.J., Sattentau Q.J., Moore J.P.;
RT "V3: HIV's switch-hitter.";
RL AIDS Res. Hum. Retroviruses 21:171-189(2005).
RN [7]
RP REVIEW.
RX PubMed=16114975; DOI=10.2165/00003495-200565130-00002;
RA Reeves J.D., Piefer A.J.;
RT "Emerging drug targets for antiretroviral therapy.";
RL Drugs 65:1747-1766(2005).
RN [8]
RP REVIEW.
RX PubMed=16437164; DOI=10.1038/sj.emboj.7600947;
RA Lusso P.;
RT "HIV and the chemokine system: 10 years later.";
RL EMBO J. 25:447-456(2006).
CC -!- FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host
CC endoplasmic reticulum into predominantly trimers. In a second time,
CC gp160 transits in the host Golgi, where glycosylation is completed. The
CC precursor is then proteolytically cleaved in the trans-Golgi and
CC thereby activated by cellular furin or furin-like proteases to produce
CC gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- FUNCTION: [Surface protein gp120]: Attaches the virus to the host
CC lymphoid cell by binding to the primary receptor CD4. This interaction
CC induces a structural rearrangement creating a high affinity binding
CC site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a
CC ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively
CC found on dendritic cells (DCs), and on endothelial cells of liver
CC sinusoids and lymph node sinuses. These interactions allow capture of
CC viral particles at mucosal surfaces by these cells and subsequent
CC transmission to permissive cells. HIV subverts the migration properties
CC of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus
CC transmission to permissive T-cells occurs either in trans (without DCs
CC infection, through viral capture and transmission), or in cis
CC (following DCs productive infection, through the usual CD4-gp120
CC interaction), thereby inducing a robust infection. In trans infection,
CC bound virions remain infectious over days and it is proposed that they
CC are not degraded, but protected in non-lysosomal acidic organelles
CC within the DCs close to the cell membrane thus contributing to the
CC viral infectious potential during DCs' migration from the periphery to
CC the lymphoid tissues. On arrival at lymphoid tissues, intact virions
CC recycle back to DCs' cell surface allowing virus transmission to CD4+
CC T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion
CC protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During fusion of
CC viral and target intracellular membranes, the coiled coil regions
CC (heptad repeats) assume a trimer-of-hairpins structure, positioning the
CC fusion peptide in close proximity to the C-terminal region of the
CC ectodomain. The formation of this structure appears to drive apposition
CC and subsequent fusion of viral and target cell membranes. Complete
CC fusion occurs in host cell endosomes and is dynamin-dependent, however
CC some lipid transfer might occur at the plasma membrane. The virus
CC undergoes clathrin-dependent internalization long before endosomal
CC fusion, thus minimizing the surface exposure of conserved viral
CC epitopes during fusion and reducing the efficacy of inhibitors
CC targeting these epitopes. Membranes fusion leads to delivery of the
CC nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- SUBUNIT: [Surface protein gp120]: The mature envelope protein (Env)
CC consists of a homotrimer of non-covalently associated gp120-gp41
CC heterodimers. The resulting complex protrudes from the virus surface as
CC a spike. There seems to be as few as 10 spikes on the average virion.
CC Interacts with host CD4, CCR5 and CXCR4. Gp120 also interacts with the
CC C-type lectins CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred
CC to as DC-SIGN(R)). Gp120 and gp41 interact with GalCer. Gp120 interacts
CC with host ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction
CC results in rapid activation of integrin ITGAL/LFA-1, which facilitates
CC efficient cell-to-cell spreading of HIV-1. Gp120 interacts with cell-
CC associated heparan sulfate; this interaction increases virus
CC infectivity on permissive cells and may be involved in infection of
CC CD4- cells. {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- SUBUNIT: [Transmembrane protein gp41]: The mature envelope protein
CC (Env) consists of a homotrimer of non-covalently associated gp120-gp41
CC heterodimers. The resulting complex protrudes from the virus surface as
CC a spike. There seems to be as few as 10 spikes on the average virion.
CC {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not
CC anchored to the viral envelope, but associates with the extravirion
CC surface through its binding to TM. It is probably concentrated at the
CC site of budding and incorporated into the virions possibly by contacts
CC between the cytoplasmic tail of Env and the N-terminus of Gag.
CC {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at
CC the site of budding and incorporated into the virions possibly by
CC contacts between the cytoplasmic tail of Env and the N-terminus of Gag.
CC {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- DOMAIN: Some of the most genetically diverse regions of the viral
CC genome are present in Env. They are called variable regions 1 through 5
CC (V1 through V5). Coreceptor usage of gp120 is determined mainly by the
CC primary structure of the third variable region (V3) in the outer domain
CC of gp120. The sequence of V3 determines which coreceptor, CCR5 and/or
CC CXCR4 (corresponding to R5/macrophage, X4/T cell and R5X4/T cell and
CC macrophage tropism), is used to trigger the fusion potential of the Env
CC complex, and hence which cells the virus can infect. Binding to CCR5
CC involves a region adjacent in addition to V3. {ECO:0000255|HAMAP-
CC Rule:MF_04083}.
CC -!- DOMAIN: The membrane proximal external region (MPER) present in gp41 is
CC a tryptophan-rich region recognized by the antibodies 2F5, Z13, and
CC 4E10. MPER seems to play a role in fusion. {ECO:0000255|HAMAP-
CC Rule:MF_04083}.
CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC many retroviral envelope proteins. Synthetic peptides derived from this
CC relatively conserved sequence inhibit immune function in vitro and in
CC vivo. {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- DOMAIN: The YXXL motif is involved in determining the exact site of
CC viral release at the surface of infected mononuclear cells and promotes
CC endocytosis. YXXL and di-leucine endocytosis motifs interact directly
CC or indirectly with the clathrin adapter complexes, opperate
CC independently, and their activities are not additive.
CC {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- DOMAIN: The CD4-binding region is targeted by the antibody b12.
CC {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- PTM: Highly glycosylated by host. The high number of glycan on the
CC protein is reffered to as 'glycan shield' because it contributes to
CC hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-
CC Rule:MF_04083}.
CC -!- PTM: Palmitoylation of the transmembrane protein and of Env polyprotein
CC (prior to its proteolytic cleavage) is essential for their association
CC with host cell membrane lipid rafts. Palmitoylation is therefore
CC required for envelope trafficking to classical lipid rafts, but not for
CC viral replication. {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as an inactive precursor that is
CC heavily N-glycosylated and processed likely by host cell furin in the
CC Golgi to yield the mature SU and TM proteins. The cleavage site between
CC SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9
CC disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to
CC CD4 receptor. {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- MISCELLANEOUS: Inhibitors targeting HIV-1 viral envelope proteins are
CC used as antiretroviral drugs. Attachment of virions to the cell surface
CC via non-specific interactions and CD4 binding can be blocked by
CC inhibitors that include cyanovirin-N, cyclotriazadisulfonamide analogs,
CC PRO 2000, TNX 355 and PRO 542. In addition, BMS 806 can block CD4-
CC induced conformational changes. Env interactions with the coreceptor
CC molecules can be targeted by CCR5 antagonists including SCH-D,
CC maraviroc (UK 427857) and aplaviroc (GW 873140), and the CXCR4
CC antagonist AMD 070. Fusion of viral and cellular membranes can be
CC inhibited by peptides such as enfuvirtide and tifuvirtide (T 1249).
CC Resistance to inhibitors associated with mutations in Env are observed.
CC Most of the time, single mutations confer only a modest reduction in
CC drug susceptibility. Combination of several mutations is usually
CC required to develop a high-level drug resistance. {ECO:0000255|HAMAP-
CC Rule:MF_04083}.
CC -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for
CC Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
CC majority of strains found worldwide belong to the group M. Group O
CC seems to be endemic to and largely confined to Cameroon and neighboring
CC countries in West Central Africa, where these viruses represent a small
CC minority of HIV-1 strains. The group N is represented by a limited
CC number of isolates from Cameroonian persons. The group M is further
CC subdivided in 9 clades or subtypes (A to D, F to H, J and K).
CC {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- SIMILARITY: Belongs to the HIV-1 env protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- WEB RESOURCE: Name=hivdb; Note=HIV drug resistance database;
CC URL="https://hivdb.stanford.edu";
CC -!- WEB RESOURCE: Name=HIV drug resistance mutations;
CC URL="https://www.iasusa.org/content/hiv-drug-resistance-mutations";
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DR EMBL; M93258; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PIR; H44001; H44001.
DR PDB; 1G9N; X-ray; 2.90 A; G=82-126, G=191-293, G=325-479.
DR PDB; 1RZK; X-ray; 2.90 A; G=82-479.
DR PDB; 1YYL; X-ray; 2.75 A; G/P=82-126, G/P=191-293, G/P=325-483.
DR PDB; 1YYM; X-ray; 2.20 A; G/P=82-126, G/P=191-296, G/P=325-483.
DR PDB; 2I5Y; X-ray; 2.20 A; G/P=82-126, G/P=191-293, G/P=325-479.
DR PDB; 2I60; X-ray; 2.40 A; G/P=82-126, G/P=191-293, G/P=325-479.
DR PDB; 2NY7; X-ray; 2.30 A; G=158-479.
DR PDB; 2QAD; X-ray; 3.30 A; A/E=88-120, A/E=195-479.
DR PDB; 3HI1; X-ray; 2.90 A; G/J=89-122, G/J=195-479.
DR PDB; 3TGQ; X-ray; 3.40 A; A/B/C/D=43-479.
DR PDB; 4DVR; X-ray; 2.50 A; G=82-122, G=199-301, G=324-484.
DR PDB; 4JO3; X-ray; 2.60 A; P/Q=313-327.
DR PDB; 4JZW; X-ray; 1.78 A; A/G=43-479.
DR PDB; 4JZZ; X-ray; 1.49 A; A=43-479.
DR PDB; 4K0A; X-ray; 2.13 A; A=43-479.
DR PDB; 4KA2; X-ray; 1.79 A; A=43-479.
DR PDB; 4LAJ; X-ray; 2.14 A; A/B/F/J=43-479.
DR PDB; 4R4F; X-ray; 3.51 A; A=43-479.
DR PDB; 4RQS; X-ray; 4.49 A; G=82-126, G=191-293, G=325-479.
DR PDB; 4RWY; X-ray; 2.13 A; A=43-479.
DR PDB; 5A7X; EM; 17.00 A; A/E/I=82-479.
DR PDB; 5A8H; EM; 23.00 A; A/G/M=82-479.
DR PDBsum; 1G9N; -.
DR PDBsum; 1RZK; -.
DR PDBsum; 1YYL; -.
DR PDBsum; 1YYM; -.
DR PDBsum; 2I5Y; -.
DR PDBsum; 2I60; -.
DR PDBsum; 2NY7; -.
DR PDBsum; 2QAD; -.
DR PDBsum; 3HI1; -.
DR PDBsum; 3TGQ; -.
DR PDBsum; 4DVR; -.
DR PDBsum; 4JO3; -.
DR PDBsum; 4JZW; -.
DR PDBsum; 4JZZ; -.
DR PDBsum; 4K0A; -.
DR PDBsum; 4KA2; -.
DR PDBsum; 4LAJ; -.
DR PDBsum; 4R4F; -.
DR PDBsum; 4RQS; -.
DR PDBsum; 4RWY; -.
DR PDBsum; 5A7X; -.
DR PDBsum; 5A8H; -.
DR SMR; P35961; -.
DR DIP; DIP-48439N; -.
DR IntAct; P35961; 4.
DR BindingDB; P35961; -.
DR ChEMBL; CHEMBL6180; -.
DR DrugBank; DB11854; Astodrimer.
DR DrugBank; DB04639; Biphenylalanine.
DR ABCD; P35961; 6 sequenced antibodies.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR EvolutionaryTrace; P35961; -.
DR Proteomes; UP000007419; Genome.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR GO; GO:0090527; P:actin filament reorganization; IEA:UniProtKB-UniRule.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; ISS:UniProtKB.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; ISS:UniProtKB.
DR GO; GO:1903905; P:positive regulation of establishment of T cell polarity; IEA:UniProtKB-UniRule.
DR GO; GO:1903908; P:positive regulation of plasma membrane raft polarization; IEA:UniProtKB-UniRule.
DR GO; GO:1903911; P:positive regulation of receptor clustering; IEA:UniProtKB-UniRule.
DR GO; GO:0019082; P:viral protein processing; ISS:UniProtKB.
DR GO; GO:0019062; P:virion attachment to host cell; ISS:UniProtKB.
DR CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR Gene3D; 2.170.40.20; -; 2.
DR HAMAP; MF_04083; HIV_ENV; 1.
DR InterPro; IPR036377; Gp120_core_sf.
DR InterPro; IPR037527; Gp160.
DR InterPro; IPR000328; GP41-like.
DR InterPro; IPR000777; HIV1_Gp120.
DR Pfam; PF00516; GP120; 1.
DR Pfam; PF00517; GP41; 1.
DR SUPFAM; SSF56502; SSF56502; 2.
PE 1: Evidence at protein level;
KW 3D-structure; AIDS; Apoptosis;
KW Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host endosome; Host membrane; Host-virus interaction;
KW Lipoprotein; Membrane; Palmitate; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT SIGNAL 1..31
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CHAIN 32..843
FT /note="Envelope glycoprotein gp160"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT /id="PRO_0000239469"
FT CHAIN 32..498
FT /note="Surface protein gp120"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT /id="PRO_0000038377"
FT CHAIN 499..843
FT /note="Transmembrane protein gp41"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT /id="PRO_0000038378"
FT TOPO_DOM 32..671
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT TOPO_DOM 693..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 130..154
FT /note="V1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 155..192
FT /note="V2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 292..325
FT /note="V3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 359..369
FT /note="CD4-binding loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 380..405
FT /note="V4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 448..458
FT /note="V5"
FT REGION 450..458
FT /note="V5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 499..519
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 561..579
FT /note="Immunosuppression"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 649..670
FT /note="MPER; binding to GalCer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 706..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 620..654
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT MOTIF 699..702
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT MOTIF 842..843
FT /note="Di-leucine internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT COMPBIAS 714..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 498..499
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT LIPID 751
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 53..73
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 118..201
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 125..192
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 130..155
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 214..243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 224..235
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 292..326
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 373..432
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 380..405
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 585..591
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3TGQ"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:4JZZ"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4RWY"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1G9N"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:3HI1"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 231..243
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:4DVR"
FT STRAND 280..294
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:2QAD"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:1G9N"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:4JZZ"
FT HELIX 330..348
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:2QAD"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:4JZZ"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:4JZZ"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:1RZK"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:4LAJ"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:2QAD"
FT STRAND 400..412
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 414..421
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:1YYM"
FT STRAND 430..443
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:2I5Y"
FT STRAND 452..457
FT /evidence="ECO:0007829|PDB:4JZZ"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:4JZZ"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:4JZZ"
SQ SEQUENCE 843 AA; 95648 MW; C69DFD971C918B71 CRC64;
MRATEIRKNY QHLWKGGTLL LGMLMICSAA EQLWVTVYYG VPVWKEATTT LFCASDAKAY
DTEVHNVWAT HACVPTDPNP QEVKLENVTE NFNMWKNNMV EQMHEDIISL WDQSLKPCVK
LTPLCVTLNC TDLRNATNTT SSSWETMEKG EIKNCSFNIT TSIRDKVQKE YALFYNLDVV
PIDNASYRLI SCNTSVITQA CPKVSFEPIP IHYCAPAGFA ILKCNDKKFN GTGPCTNVST
VQCTHGIRPV VSTQLLLNGS LAEEEIVIRS ENFTNNAKTI IVQLNESVVI NCTRPNNNTR
KSINIGPGRA LYTTGEIIGD IRQAHCNLSK TQWENTLEQI AIKLKEQFGN NKTIIFNPSS
GGDPEIVTHS FNCGGEFFYC NSTQLFTWND TRKLNNTGRN ITLPCRIKQI INMWQEVGKA
MYAPPIRGQI RCSSNITGLL LTRDGGKDTN GTEIFRPGGG DMRDNWRSEL YKYKVVKIEP
LGVAPTKAKR RVVQREKRAV GLGALFLGFL GAAGSTMGAA SITLTVQARQ LLSGIVQQQN
NLLRAIEAQQ HLLQLTVWGI KQLQARVLAV ERYLRDQQLL GIWGCSGKLI CTTTVPWNTS
WSNKSLNEIW DNMTWMKWER EIDNYTHIIY SLIEQSQNQQ EKNEQELLAL DKWASLWNWF
DITKWLWYIK IFIMIVGGLI GLRIVFVVLS IVNRVRQGYS PLSFQTHLPA QRGPDRPDGI
EEEGGERDRD RSGPLVDGFL AIIWVDLRSL CLFSYHRLRD LLLIVTRIVE LLGRRGWGVL
KYWWNLLQYW IQELKNSAVS LLNATAIAVA EGTDRVIEIL QRAFRAVLHI PVRIRQGLER
ALL
