ID A0A7D6INZ5_9HIV1 Unreviewed; 843 AA. AC A0A7D6INZ5; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 07-APR-2021, entry version 3. DE RecName: Full=Envelope glycoprotein gp160 {ECO:0000256|HAMAP-Rule:MF_04083}; DE AltName: Full=Env polyprotein {ECO:0000256|HAMAP-Rule:MF_04083}; DE Contains: DE RecName: Full=Surface protein gp120 {ECO:0000256|HAMAP-Rule:MF_04083}; DE Short=SU {ECO:0000256|HAMAP-Rule:MF_04083}; DE AltName: Full=Glycoprotein 120 {ECO:0000256|HAMAP-Rule:MF_04083}; DE Short=gp120 {ECO:0000256|HAMAP-Rule:MF_04083}; DE Contains: DE RecName: Full=Transmembrane protein gp41 {ECO:0000256|HAMAP-Rule:MF_04083}; DE Short=TM {ECO:0000256|HAMAP-Rule:MF_04083}; DE AltName: Full=Glycoprotein 41 {ECO:0000256|HAMAP-Rule:MF_04083}; DE Short=gp41 {ECO:0000256|HAMAP-Rule:MF_04083}; GN Name=env {ECO:0000256|HAMAP-Rule:MF_04083, GN ECO:0000313|EMBL:QLL22438.1}; OS Human immunodeficiency virus 1. OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus. OX NCBI_TaxID=11676 {ECO:0000313|EMBL:QLL22438.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:QLL22438.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBJC495 {ECO:0000313|EMBL:QLL22438.1}; RA Sun S., Zhang D., Qi Z., Hu Y.; RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_04083}. CC -!- SUBUNIT: The mature envelope protein (Env) consists of a homotrimer of CC non-covalently associated gp120-gp41 heterodimers. The resulting CC complex protrudes from the virus surface as a spike. There seems to be CC as few as 10 spikes on the average virion. Surface protein gp120 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:0000256|HAMAP-Rule:MF_04083}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell CC membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane CC protein {ECO:0000256|ARBA:ARBA00004251}. Endosome membrane CC {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004481}. Endosome membrane CC {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004530}. Host cell membrane CC {ECO:0000256|ARBA:ARBA00004505}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004505}. Host cell membrane CC {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004402}. Host endosome membrane CC {ECO:0000256|ARBA:ARBA00004433}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004433}. Host endosome membrane CC {ECO:0000256|ARBA:ARBA00004578}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004578}. Membrane CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004650}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004650}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004563}. CC -!- SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane CC {ECO:0000256|HAMAP-Rule:MF_04083}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_04083}. Host cell membrane CC {ECO:0000256|HAMAP-Rule:MF_04083}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_04083}. Host endosome membrane CC {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_04083}. CC -!- SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane CC {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein CC {ECO:0000256|HAMAP-Rule:MF_04083}. Host cell membrane CC {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein CC {ECO:0000256|HAMAP-Rule:MF_04083}. Host endosome membrane CC {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein CC {ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_04083, ECO:0000256|RuleBase:RU363095}. CC -!- DOMAIN: The CD4-binding region is targeted by the antibody b12. CC {ECO:0000256|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:0000256|HAMAP-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:0000256|HAMAP- CC 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:0000256|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:0000256|HAMAP-Rule:MF_04083}. CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. CC Envelope glycoproteins are synthesized as a 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:0000256|HAMAP-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:0000256|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:0000256|HAMAP- CC Rule:MF_04083}. CC -!- SIMILARITY: Belongs to the HIV-1 env protein family. CC {ECO:0000256|HAMAP-Rule:MF_04083}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04083, CC ECO:0000256|RuleBase:RU363095}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MT436152; QLL22438.1; -; Genomic_DNA. DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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; IEA:UniProtKB-UniRule. 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; IEA:UniProtKB-UniRule. DR GO; GO:0030683; P:mitigation of host immune response by virus; IEA:UniProtKB-UniRule. 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; IEA:UniProtKB-UniRule. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule. 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; 2. DR Pfam; PF00517; GP41; 1. DR SUPFAM; SSF56502; SSF56502; 1. PE 3: Inferred from homology; KW Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|HAMAP-Rule:MF_04083, KW ECO:0000256|RuleBase:RU363095}; KW Clathrin-mediated endocytosis of virus by host KW {ECO:0000256|ARBA:ARBA00022570, ECO:0000256|HAMAP-Rule:MF_04083}; KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685, KW ECO:0000256|HAMAP-Rule:MF_04083, ECO:0000256|RuleBase:RU363095}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP- KW Rule:MF_04083}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP- KW Rule:MF_04083}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|ARBA:ARBA00022510, ECO:0000256|HAMAP-Rule:MF_04083}; KW Fusion of virus membrane with host membrane {ECO:0000256|HAMAP- KW Rule:MF_04083, ECO:0000256|RuleBase:RU363095}; KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04083}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP- KW Rule:MF_04083, ECO:0000256|RuleBase:RU363095}; KW Host endosome {ECO:0000256|ARBA:ARBA00023046, ECO:0000256|HAMAP- KW Rule:MF_04083, ECO:0000256|RuleBase:RU363095}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP- KW Rule:MF_04083, ECO:0000256|RuleBase:RU363095}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP- KW Rule:MF_04083, ECO:0000256|RuleBase:RU363095}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP- KW Rule:MF_04083}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04083, KW ECO:0000256|RuleBase:RU363095}; KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_04083}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_04083}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_04083, ECO:0000256|RuleBase:RU363095}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_04083, ECO:0000256|RuleBase:RU363095}; KW Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04083, KW ECO:0000256|RuleBase:RU363095}; KW Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04083, KW ECO:0000256|RuleBase:RU363095, ECO:0000313|EMBL:QLL22438.1}; KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280, ECO:0000256|HAMAP- KW Rule:MF_04083}; KW Viral penetration into host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04083, KW ECO:0000256|RuleBase:RU363095}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04083, ECO:0000256|RuleBase:RU363095}; KW Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890, KW ECO:0000256|HAMAP-Rule:MF_04083}; KW Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04083, KW ECO:0000256|RuleBase:RU363095}. FT CHAIN 32..843 FT /note="Envelope glycoprotein gp160" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT /id="PRO_5028547606" FT CHAIN 502..843 FT /note="Transmembrane protein gp41" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT /id="PRO_5028547607" FT TRANSMEM 20..41 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363095" FT TRANSMEM 502..526 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363095" FT TRANSMEM 669..696 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363095" FT TOPO_DOM 697..843 FT /note="Cytoplasmic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT DOMAIN 33..144 FT /note="GP120" FT /evidence="ECO:0000259|Pfam:PF00516" FT DOMAIN 146..501 FT /note="GP120" FT /evidence="ECO:0000259|Pfam:PF00516" FT DOMAIN 521..709 FT /note="GP41" FT /evidence="ECO:0000259|Pfam:PF00517" FT REGION 357..367 FT /note="CD4-binding loop" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT REGION 444..464 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 565..583 FT /note="Immunosuppression" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT REGION 653..674 FT /note="MPER; binding to GalCer" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT REGION 710..733 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 624..658 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT MOTIF 703..706 FT /note="YXXL motif; contains endocytosis signal" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT MOTIF 842..843 FT /note="Di-leucine internalization motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT COMPBIAS 444..461 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 501..502 FT /note="Cleavage; by host furin" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT LIPID 755 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT DISULFID 53..73 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT DISULFID 212..241 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT DISULFID 222..233 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" FT DISULFID 589..595 FT /evidence="ECO:0000256|HAMAP-Rule:MF_04083" SQ SEQUENCE 843 AA; 95588 MW; B0DC775613A432B7 CRC64; MRVTGTRKNY QHLWRWGTML LGMLMICSAA ENLWVTVYYG VPVWKEATTT LFCASDAKAY ATEAHNIWAT HACVPTDPNP QEVVLGNVTE NFNMWKNNMV EQMHEDIISL WDQSLKPCVK LTPLCVILNC TNLNNTSSNS NSTTEGGEMK NCSFNINTSI RTKVTDYALF YKLDIAPISN DNISYRLISC NTSVITQACP KVSFEPIPIH YCTPAGFAIL KCNNKTFKGT GPCTNVSTVQ CTHGIRPVVS TQLLLNGSLA EEEVVIRSSN FTDNARVIIV QLNESIEINC TRPNNNTRKS IQLGLGRAWH ATGQIIGDIR QAHCNLSRTK WNDTLKQITE KLREQFGNNK TIIFNQSSGG DLEIEMHSFN CGGEFFYCNT SQLFNSTWNN NSAWSGPTGN DTITLPCRIK QVVNMWQEVG KAMYAPPIEG QIRCSSNITG MLLTRDGGNN GNETTETFRP GGGNMKDNWR SELYKYKVVK IKPLGVAPTR AKRRVVQREK RAVGTIGAMF LGFLGAAGST MGAASITLTV QARQLLSGIV QQQRNLLRAI EAQQHMLQLT VWGIKQLQAR VLAVERYLKD QQLLGIWGCS GKLICTTAVP WNVSWSNKSL SEIWDNMTWM EWEREIDNYT KEIYTLIKAS QNQQEKNELE LLELDNWASL WNWFDITNWL WYIKIFIMIV GGLIGLRIVF AVLSIVNRVR QGYSPLSLQT RFPAQRGPGR PEGIEGEGGE RDRDRSERLV AGLLTLIWED LRNLCLFSYH HLRDLLLIVT RIVELLGRRG WEALKYWWNL LQYWIQELKN STISLFNTAA EGIARVIELV QRAYRAFIHI PTRIRQGLER ALL //