ID   VGP_EBOG4               Reviewed;         676 AA.
AC   O11457; Q913A3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Envelope glycoprotein;
DE   AltName: Full=GP1,2;
DE            Short=GP;
DE   Contains:
DE     RecName: Full=GP1;
DE   Contains:
DE     RecName: Full=GP2;
DE   Contains:
DE     RecName: Full=Shed GP;
DE     AltName: Full=GP1,2-delta;
DE   Flags: Precursor;
GN   Name=GP;
OS   Zaire ebolavirus (strain Gabon-94) (ZEBOV) (Zaire Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Orthoebolavirus;
OC   Orthoebolavirus zairense; Zaire ebolavirus.
OX   NCBI_TaxID=128947;
OH   NCBI_TaxID=77231; Epomops franqueti (Franquet's epauletted fruit bat) (Epomophorus franqueti).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9185597; DOI=10.1006/viro.1997.8529;
RA   Volchkov V., Volchkova V., Eckel C., Klenk H.-D., Bouloy M., Leguenno B.,
RA   Feldmann H.;
RT   "Emergence of subtype Zaire Ebola virus in Gabon.";
RL   Virology 232:139-144(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate Bouee-96;
RX   PubMed=11752702; DOI=10.1099/0022-1317-83-1-67;
RA   Leroy E.M., Baize S., Mavoungou E., Apetrei C.;
RT   "Sequence analysis of the GP, NP, VP40 and VP24 genes of Ebola virus
RT   isolated from deceased, surviving and asymptomatically infected individuals
RT   during the 1996 outbreak in Gabon: comparative studies and phylogenetic
RT   characterization.";
RL   J. Gen. Virol. 83:67-73(2002).
RN   [3]
RP   FUNCTION (GP1).
RX   PubMed=17005688; DOI=10.1128/jvi.01157-06;
RA   Shimojima M., Takada A., Ebihara H., Neumann G., Fujioka K., Irimura T.,
RA   Jones S., Feldmann H., Kawaoka Y.;
RT   "Tyro3 family-mediated cell entry of Ebola and Marburg viruses.";
RL   J. Virol. 80:10109-10116(2006).
RN   [4] {ECO:0007744|PDB:1EBO}
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 552-650, AND DISULFIDE BONDS.
RX   PubMed=9844633; DOI=10.1016/s1097-2765(00)80159-8;
RA   Weissenhorn W., Carfi A., Lee K.H., Skehel J.J., Wiley D.C.;
RT   "Crystal structure of the Ebola virus membrane fusion subunit, GP2, from
RT   the envelope glycoprotein ectodomain.";
RL   Mol. Cell 2:605-616(1998).
CC   -!- FUNCTION: [Envelope glycoprotein]: Trimeric GP1,2 complexes form the
CC       virion surface spikes and mediate the viral entry processes, with GP1
CC       acting as the receptor-binding subunit and GP2 as the membrane fusion
CC       subunit. At later times of infection, down-regulates the expression of
CC       various host cell surface molecules that are essential for immune
CC       surveillance and cell adhesion. Down-modulates several integrins
CC       including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1.
CC       This decrease in cell adhesion molecules may lead to cell detachment,
CC       contributing to the disruption of blood vessel integrity and
CC       hemorrhages developed during infection (cytotoxicity). Interacts with
CC       host TLR4 and thereby stimulates the differentiation and activation of
CC       monocytes leading to bystander death of T-lymphocytes. Down-regulates
CC       as well the function of host natural killer cells. Counteracts the
CC       antiviral effect of host BST2/tetherin that restricts release of
CC       progeny virions from infected cells. However, cooperates with VP40 and
CC       host BST2 to activate canonical NF-kappa-B pathway in a manner
CC       dependent on neddylation. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- FUNCTION: [Shed GP]: Functions as a decoy for anti-GP1,2 antibodies
CC       thereby contributing to viral immune evasion. Interacts and activates
CC       host macrophages and dendritic cells inducing up-regulation of cytokine
CC       transcription. This effect is mediated throught activation of host
CC       TLR4. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- FUNCTION: [GP1]: Responsible for binding to the receptor(s) on target
CC       cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as
CC       cofactors for virus entry into dendritic cells (DCs) and endothelial
CC       cells (By similarity). Binding to the macrophage specific lectin
CC       CLEC10A also seems to enhance virus infectivity (By similarity).
CC       Interaction with FOLR1/folate receptor alpha may be a cofactor for
CC       virus entry in some cell types, although results are contradictory (By
CC       similarity). Members of the Tyro3 receptor tyrosine kinase family also
CC       seem to be cell entry factors in filovirus infection (PubMed:17005688).
CC       Once attached, the virions are internalized through clathrin-dependent
CC       endocytosis and/or macropinocytosis. After internalization of the virus
CC       into the endosomes of the host cell, proteolysis of GP1 by two cysteine
CC       proteases, CTSB/cathepsin B and CTSL/cathepsin L removes the glycan cap
CC       and allows GP1 binding to the host entry receptor NPC1. NPC1-binding,
CC       Ca(2+) and acidic pH induce a conformational change of GP2, which
CC       unmasks its fusion peptide and permit membranes fusion (By similarity).
CC       {ECO:0000250|UniProtKB:Q05320, ECO:0000250|UniProtKB:Q66814,
CC       ECO:0000269|PubMed:17005688}.
CC   -!- FUNCTION: [GP2]: Acts as a class I viral fusion protein. Under the
CC       current model, the protein has at least 3 conformational states: pre-
CC       fusion native state, pre-hairpin intermediate state, and post-fusion
CC       hairpin state. During viral and target cell membrane fusion, the coiled
CC       coil regions (heptad repeats) assume a trimer-of-hairpins structure,
CC       positioning the fusion peptide in close proximity to the C-terminal
CC       region of the ectodomain. The formation of this structure appears to
CC       drive apposition and subsequent fusion of viral and target cell
CC       membranes. Responsible for penetration of the virus into the cell
CC       cytoplasm by mediating the fusion of the membrane of the endocytosed
CC       virus particle with the endosomal membrane. Low pH in endosomes induces
CC       an irreversible conformational change in GP2, releasing the fusion
CC       hydrophobic peptide. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBUNIT: [Envelope glycoprotein]: Homotrimer; each monomer consists of
CC       a GP1 and a GP2 subunit linked by disulfide bonds. The resulting
CC       peplomers (GP1,2) protrude from the virus surface as spikes. Interacts
CC       with host integrin alpha-V/ITGAV. Interacts with host CLEC10A. Binds
CC       also to host CD209 and CLEC4M/DC-SIGN(R). Interacts with host FOLR1.
CC       Interacts with BST2; this interaction inhibits the antiviral effect of
CC       BST2 and this allows viral release from infected cells. Interacts with
CC       host FCN1; this interaction enhances viral entry. Interacts with host
CC       TLR4; this interaction induces cell death in T-lymphocytes or
CC       proinflammatory cytokines and SOCS1 production in monocytes.
CC       {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBUNIT: [GP1]: Interacts with host entry receptor NPC1.
CC       {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBUNIT: [Shed GP]: GP1 and GP2delta are part of GP1,2delta soluble
CC       complexes released by ectodomain shedding.
CC       {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBCELLULAR LOCATION: [GP2]: Virion membrane
CC       {ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane protein
CC       {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:Q05320};
CC       Single-pass type I membrane protein {ECO:0000255}. Note=In the cell,
CC       localizes to the plasma membrane lipid rafts, which probably represent
CC       the assembly and budding site. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBCELLULAR LOCATION: [GP1]: Virion membrane
CC       {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q05320}. Host cell membrane
CC       {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q05320}. Note=GP1 is not anchored to the viral
CC       envelope, but forms a disulfid-linked complex with the extravirion
CC       surface GP2. In the cell, both GP1 and GP2 localize to the plasma
CC       membrane lipid rafts, which probably represent the assembly and budding
CC       site. GP1 can also be shed after proteolytic processing.
CC       {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBCELLULAR LOCATION: [Shed GP]: Secreted
CC       {ECO:0000250|UniProtKB:Q05320}. Note=GP2-delta bound to GP1 (GP1,2-
CC       delta) is produced by proteolytic cleavage of GP1,2 by host ADAM17 and
CC       shed by the virus. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- DOMAIN: The mucin-like region seems to be involved in the cytotoxic
CC       function. This region is also involved in binding to human CLEC10A (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The coiled coil regions play a role in oligomerization and
CC       fusion activity. {ECO:0000250}.
CC   -!- PTM: The signal peptide region modulates GP's high mannose
CC       glycosylation, thereby determining the efficiency of the interactions
CC       with DC-SIGN(R). {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- PTM: O-glycosylated in the mucin-like region. {ECO:0000250}.
CC   -!- PTM: Palmitoylation of GP2 is not required for its function.
CC       {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC       precursor is processed into GP1 and GP2 by host cell furin in the trans
CC       Golgi, and maybe by other host proteases, to yield the mature GP1 and
CC       GP2 proteins. The cleavage site corresponds to the furin optimal
CC       cleavage sequence [KR]-X-[KR]-R. This cleavage does not seem to be
CC       required for function. After the internalization of the virus into cell
CC       endosomes, GP1 C-terminus is removed by the endosomal proteases
CC       cathepsin B, cathepsin L, or both, leaving a 19-kDa N-terminal fragment
CC       which is further digested by cathepsin B. Proteolytic processing of
CC       GP1,2 by host ADAM17 can remove the transmembrane anchor of GP2 and
CC       leads to shedding of complexes consisting in GP1 and truncated GP2
CC       (GP1,2delta) (By similarity). {ECO:0000250}.
CC   -!- RNA EDITING: Modified_positions=295 {ECO:0000250}; Note=Partially
CC       edited. RNA editing at this position consists of an insertion of one
CC       adenine nucleotide. The sequence displayed here is the full-length
CC       transmembrane glycoprotein, derived from the edited RNA. The unedited
CC       RNA gives rise to the small secreted glycoprotein (AC O11458) (By
CC       similarity). {ECO:0000250};
CC   -!- MISCELLANEOUS: Filoviruses entry requires functional lipid rafts at the
CC       host cell surface. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Essential for infectivity, as it is the sole viral
CC       protein expressed at the virion surface.
CC   -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; U77384; AAC57989.1; -; Genomic_RNA.
DR   EMBL; AY058898; AAL25818.1; -; mRNA.
DR   PDB; 1EBO; X-ray; 3.00 A; A/B/C/D/E/F=552-650.
DR   PDB; 6EA7; X-ray; 4.25 A; B/D/F=502-612.
DR   PDBsum; 1EBO; -.
DR   PDBsum; 6EA7; -.
DR   BMRB; O11457; -.
DR   EMDB; EMD-25471; -.
DR   SMR; O11457; -.
DR   GlyCosmos; O11457; 17 sites, No reported glycans.
DR   EvolutionaryTrace; O11457; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd09850; Ebola-like_HR1-HR2; 1.
DR   Gene3D; 1.10.287.210; -; 1.
DR   InterPro; IPR014625; GPC_FiloV.
DR   InterPro; IPR002561; GPC_filovir-type_extra_dom.
DR   Pfam; PF01611; Filo_glycop; 1.
DR   PIRSF; PIRSF036874; GPC_FiloV; 1.
DR   SUPFAM; SSF58069; Virus ectodomain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 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 membrane; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host tetherin by virus; Lipoprotein; Membrane; Palmitate;
KW   RNA editing; Secreted; Signal; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral attachment to host entry receptor;
KW   Viral envelope protein; Viral immunoevasion;
KW   Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW   Virus entry into host cell.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..676
FT                   /note="Envelope glycoprotein"
FT                   /id="PRO_0000037464"
FT   CHAIN           33..501
FT                   /note="GP1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037465"
FT   CHAIN           502..676
FT                   /note="GP2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037466"
FT   CHAIN           502..637
FT                   /note="Shed GP"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000245055"
FT   TOPO_DOM        33..650
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        651..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        672..676
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          54..201
FT                   /note="Receptor-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          305..485
FT                   /note="Mucin-like region"
FT                   /evidence="ECO:0000250"
FT   REGION          314..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..539
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250"
FT   COILED          554..595
FT                   /evidence="ECO:0000255"
FT   COILED          615..634
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        415..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            57
FT                   /note="Involved in receptor recognition and/or post-binding
FT                   events"
FT                   /evidence="ECO:0000255"
FT   SITE            63
FT                   /note="Involved in receptor recognition and/or post-binding
FT                   events"
FT                   /evidence="ECO:0000255"
FT   SITE            64
FT                   /note="Involved in receptor recognition and/or post-binding
FT                   events"
FT                   /evidence="ECO:0000255"
FT   SITE            88
FT                   /note="Involved in receptor recognition and/or post-binding
FT                   events"
FT                   /evidence="ECO:0000255"
FT   SITE            95
FT                   /note="Involved in receptor recognition and/or post-binding
FT                   events"
FT                   /evidence="ECO:0000255"
FT   SITE            170
FT                   /note="Involved in receptor recognition and/or post-binding
FT                   events"
FT                   /evidence="ECO:0000255"
FT   SITE            501..502
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250"
FT   SITE            637..638
FT                   /note="Cleavage; by host ADAM17"
FT                   /evidence="ECO:0000250"
FT   LIPID           670
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q05320"
FT   LIPID           672
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q05320"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        563
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        618
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..609
FT                   /note="Interchain (between GP1 and GP2 chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..135
FT                   /evidence="ECO:0000255"
FT   DISULFID        121..147
FT                   /evidence="ECO:0000255"
FT   DISULFID        511..556
FT                   /evidence="ECO:0000255"
FT   DISULFID        601..608
FT                   /evidence="ECO:0000269|PubMed:9844633"
FT   VARIANT         219
FT                   /note="R -> K (in strain: Isolate Bouee-96)"
FT   VARIANT         260
FT                   /note="R -> I (in strain: Isolate Bouee-96)"
FT   VARIANT         368
FT                   /note="L -> P (in strain: Isolate Bouee-96)"
FT   VARIANT         376
FT                   /note="R -> Q (in strain: Isolate Bouee-96)"
FT   VARIANT         379
FT                   /note="I -> T (in strain: Isolate Bouee-96)"
FT   VARIANT         474
FT                   /note="A -> T (in strain: Isolate Bouee-96)"
FT   VARIANT         544
FT                   /note="I -> T (in strain: Isolate Bouee-96)"
FT   HELIX           540..548
FT                   /evidence="ECO:0007829|PDB:1EBO"
FT   HELIX           549..551
FT                   /evidence="ECO:0007829|PDB:1EBO"
FT   HELIX           554..593
FT                   /evidence="ECO:0007829|PDB:1EBO"
FT   HELIX           595..597
FT                   /evidence="ECO:0007829|PDB:1EBO"
FT   HELIX           600..604
FT                   /evidence="ECO:0007829|PDB:1EBO"
FT   HELIX           605..609
FT                   /evidence="ECO:0007829|PDB:1EBO"
FT   HELIX           616..630
FT                   /evidence="ECO:0007829|PDB:1EBO"
SQ   SEQUENCE   676 AA;  74577 MW;  5E8EB143E5E86E41 CRC64;
     MGVTGILQLP RDRFKRTSFF LWVIILFQRT FSIPLGVIHN STLQVSDVDK LVCRDKLSST
     NQLRSVGLNL EGNGVATDVP SATKRWGFRS GVPPKVVNYE AGEWAENCYN LEIKKPDGSE
     CLPAAPDGIR GFPRCRYVHK VSGTGPCAGD FAFHKEGAFF LYDRLASTVI YRGTTFAEGV
     VAFLILPQAK KDFFSSHPLR EPVNATEDPS SGYYSTTIRY QATGFGTNET EYLFEVDNLT
     YVQLESRFTP QFLLQLNETR YTSGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKNLTRK
     IRSEELSFTA VSNRAKNISG QSPARTSSDP GTNTTTEDHK IMASENSSAM VQVHSQGREA
     AVSHLTTLAT ISTSLRPPIT KPGPDNSTHN TPVYKLDISE ATQVEQHHRR TDNASTTSDT
     PPATTAAGPL KAENTNTSKG TDLLDPATTT SPQNHSETAG NNNTHHQDTG EESASSGKLG
     LITNTIAGVA GLITGGRRTR REAIVNAQPK CNPNLHYWTT QDEGAAIGLA WIPYFGPAAE
     GIYIEGLMHN QDGLICGLRQ LANETTQALQ LFLRATTELR TFSILNRKAI DFLLQRWGGT
     CHILGPDCCI EPHDWTKNIT DKIDQIIHDF VDKTLPDQGD NDNWWTGWRQ WIPAGIGVTG
     VIIAVIALFC ICKFVF
//