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ENV_HV1V9
ID   ENV_HV1V9               Reviewed;         859 AA.
AC   Q9Q714;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
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 H (isolate VI991)
OS   (HIV-1).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=388888;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10983640; DOI=10.1097/00002030-200007280-00009;
RA   Janssens W., Laukkanen T., Salminen M.O., Carr J.K., Van der Auwera G.,
RA   Heyndrickx L., van der Groen G., McCutchan F.E.;
RT   "HIV-1 subtype H near-full length genome reference strains and analysis of
RT   subtype-H-containing inter-subtype recombinants.";
RL   AIDS 14:1533-1543(2000).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
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   [7]
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; AF190127; AAF18394.1; -; Genomic_DNA.
DR   PDB; 3UJJ; X-ray; 2.00 A; P=305-327.
DR   PDBsum; 3UJJ; -.
DR   SMR; Q9Q714; -.
DR   PRIDE; Q9Q714; -.
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..28
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CHAIN           29..859
FT                   /note="Envelope glycoprotein gp160"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT                   /id="PRO_0000244693"
FT   CHAIN           29..514
FT                   /note="Surface protein gp120"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT                   /id="PRO_0000244694"
FT   CHAIN           515..859
FT                   /note="Transmembrane protein gp41"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT                   /id="PRO_0000244695"
FT   TOPO_DOM        29..687
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   TRANSMEM        688..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   TOPO_DOM        709..859
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   REGION          127..154
FT                   /note="V1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   REGION          155..199
FT                   /note="V2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   REGION          300..333
FT                   /note="V3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   REGION          366..376
FT                   /note="CD4-binding loop"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   REGION          387..423
FT                   /note="V4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   REGION          466..474
FT                   /note="V5"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   REGION          515..535
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   REGION          577..595
FT                   /note="Immunosuppression"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   REGION          665..686
FT                   /note="MPER; binding to GalCer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   REGION          724..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          636..670
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   MOTIF           715..718
FT                   /note="YXXL motif; contains endocytosis signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   MOTIF           858..859
FT                   /note="Di-leucine internalization motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   SITE            514..515
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   LIPID           767
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        140
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        188
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        200
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        244
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        399
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        468
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        614
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        619
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        628
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   CARBOHYD        640
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   DISULFID        50..70
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   DISULFID        115..208
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   DISULFID        122..199
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   DISULFID        127..155
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   DISULFID        221..250
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   DISULFID        231..242
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   DISULFID        300..334
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   DISULFID        380..450
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   DISULFID        387..423
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   DISULFID        601..607
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT   STRAND          312..314
FT                   /evidence="ECO:0007829|PDB:3UJJ"
SQ   SEQUENCE   859 AA;  97577 MW;  ECD8CE2BF28A452D CRC64;
     METQRNYPSL WRWGTLILGM LLICSVVGNL WVTVYYGVPV WKEAKTTLFC ASDAKAYDTE
     RHNVWATHAC VPTDPNPQEM VLENVTETFN MWVNDMVEQM HTDIISLWDQ SLKPCVKLTP
     LCVTLDCSSV NATNVTKSNN STDINIGEIQ EQRNCSFNVT TAIRDKNQKV HALFYRADIV
     QIDEGERNKS DNHYRLINCN TSVIKQACPK VSFEPIPIHY CAPAGFAILK CNGKKFNGTG
     PCTNVSTVQC THGIRPVVST QLLLNGSLAE VEEVIIRSKN ITDNTKNIIV QLNEPVQINC
     TRTGNNTRKS IRIGPGQAFY ATGDIIGDIR RAYCNISGKQ WNETLHKVIT KLGSYFDNKT
     IILQPPAGGD IEIITHSFNC GGEFFYCNTT KLFNSTWTNS SYTNDTYNSN STEDITGNIT
     LQCKIKQIVN MWQRVGQAMY APPIRGNITC ISNITGLILT FDRNNTNNVT FRPGGGDMRD
     NWRSELYKYK VVKIEPLGVA PTEARRRVVE REKRAVGMGA FFLGFLGAAG STMGAASITL
     TVQARQLLSG IVQQQSNLLR AIQAQQHMLQ LTVWGIKQLQ ARVLAVERYL KDQQLLGIWG
     CSGKLICTTN VPWNSSWSNK SLDEIWDNMT WMEWDKQINN YTDEIYRLLE VSQNQQEKNE
     QDLLALDKWA NLWNWFSITN WLWYIRIFIM IVGGIIGLRI VFAVLSIVNR VRQGYSPLSL
     QTLIPNQRGP DRPREIEEEG GEQDRDRSIR LVNGFLPLVW EDLRNLCLFS YRRLRDLLSI
     VARTVELLGR RGWEALKLLG NLLLYWGQEL KNSAISLLNT TAIAVAEGTD RIIELVQRAW
     RAILHIPRRI RQGFERALL
 
 
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