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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
 
 
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