GLYC_LYCVA
ID GLYC_LYCVA Reviewed; 498 AA.
AC P09991; Q27V72; Q49K87;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Pre-glycoprotein polyprotein GP complex {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=Pre-GP-C {ECO:0000255|HAMAP-Rule:MF_04084};
DE Contains:
DE RecName: Full=Stable signal peptide {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=SSP {ECO:0000255|HAMAP-Rule:MF_04084};
DE Contains:
DE RecName: Full=Glycoprotein G1 {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=GP1 {ECO:0000255|HAMAP-Rule:MF_04084};
DE Contains:
DE RecName: Full=Glycoprotein G2 {ECO:0000255|HAMAP-Rule:MF_04084};
DE Short=GP2 {ECO:0000255|HAMAP-Rule:MF_04084};
GN Name=GPC {ECO:0000255|HAMAP-Rule:MF_04084}; Synonyms=GP-C;
GN OrderedLocusNames=Segment S;
OS Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11624;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10036; Mesocricetus auratus (Golden hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3824905; DOI=10.1016/0042-6822(87)90323-0;
RA Southern P.J., Singh M.K., Riviere Y., Jacoby D.R., Buchmeier M.J.,
RA Oldstone M.B.A.;
RT "Molecular characterization of the genomic S RNA segment from lymphocytic
RT choriomeningitis virus.";
RL Virology 157:145-155(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate CTL+, and Isolate CTL-;
RX PubMed=3259346; DOI=10.1016/0042-6822(88)90566-1;
RA Salvato M., Shimomaye E., Southern P.J., Oldstone M.B.A.;
RT "Virus-lymphocyte interactions. IV. Molecular characterization of LCMV
RT Armstrong (CTL+) small genomic segment and that of its variant, Clone 13
RT (CTL-).";
RL Virology 164:517-522(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Armstrong 53b;
RX PubMed=16051837; DOI=10.1128/jvi.79.16.10451-10459.2005;
RA Grande-Perez A., Gomez-Mariano G., Lowenstein P.R., Domingo E.;
RT "Mutagenesis-induced, large fitness variations with an invariant arenavirus
RT consensus genomic nucleotide sequence.";
RL J. Virol. 79:10451-10459(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Armstrong-derived variant Cl13;
RX PubMed=16537369; DOI=10.1073/pnas.0600652103;
RA Flatz L., Bergthaler A., de la Torre J.C., Pinschewer D.D.;
RT "Recovery of an arenavirus entirely from RNA polymerase I/II-driven cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:4663-4668(2006).
RN [5]
RP FUNCTION IN FUSION.
RX PubMed=8291229; DOI=10.1006/viro.1994.1057;
RA Di Simone C., Zandonatti M.A., Buchmeier M.J.;
RT "Acidic pH triggers LCMV membrane fusion activity and conformational change
RT in the glycoprotein spike.";
RL Virology 198:455-465(1994).
RN [6]
RP FUNCTION, AND INTERACTION WITH HOST DAG1.
RX PubMed=9851928; DOI=10.1126/science.282.5396.2079;
RA Cao W., Henry M.D., Borrow P., Yamada H., Elder J.H., Ravkov E.V.,
RA Nichol S.T., Compans R.W., Campbell K.P., Oldstone M.B.A.;
RT "Identification of alpha-dystroglycan as a receptor for lymphocytic
RT choriomeningitis virus and Lassa fever virus.";
RL Science 282:2079-2081(1998).
RN [7]
RP SUBUNIT.
RX PubMed=16731928; DOI=10.1128/jvi.00008-06;
RA Eschli B., Quirin K., Wepf A., Weber J., Zinkernagel R., Hengartner H.;
RT "Identification of an N-terminal trimeric coiled-coil core within
RT arenavirus glycoprotein 2 permits assignment to class I viral fusion
RT proteins.";
RL J. Virol. 80:5897-5907(2006).
RN [8]
RP FUNCTION OF STABLE SIGNAL PEPTIDE, AND MUTAGENESIS OF PRO-12; ASP-16;
RP GLU-17; ASN-20; LYS-33; ASN-37; PHE-49 AND GLY-54.
RX PubMed=17376927; DOI=10.1128/jvi.02759-06;
RA Saunders A.A., Ting J.P.C., Meisner J., Neuman B.W., Perez M.,
RA de la Torre J.C., Buchmeier M.J.;
RT "Mapping the landscape of the lymphocytic choriomeningitis virus stable
RT signal peptide reveals novel functional domains.";
RL J. Virol. 81:5649-5657(2007).
RN [9]
RP INTERACTION WITH Z PROTEIN.
RX PubMed=17581989; DOI=10.1128/jvi.00499-07;
RA Capul A.A., Perez M., Burke E., Kunz S., Buchmeier M.J., de la Torre J.C.;
RT "Arenavirus Z-glycoprotein association requires Z myristoylation but not
RT functional RING or late domains.";
RL J. Virol. 81:9451-9460(2007).
RN [10]
RP FUNCTION.
RX PubMed=17761532; DOI=10.1091/mbc.e07-04-0374;
RA Rojek J.M., Campbell K.P., Oldstone M.B., Kunz S.;
RT "Old World arenavirus infection interferes with the expression of
RT functional alpha-dystroglycan in the host cell.";
RL Mol. Biol. Cell 18:4493-4507(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 92-101.
RX PubMed=29253009; DOI=10.1371/journal.pone.0189584;
RA Hafstrand I., Badia-Martinez D., Josey B.J., Norstroem M., Buratto J.,
RA Pellegrino S., Duru A.D., Sandalova T., Achour A.;
RT "Crystal structures of H-2Db in complex with the LCMV-derived peptides GP92
RT and GP392 explain pleiotropic effects of glycosylation on antigen
RT presentation and immunogenicity.";
RL PLoS ONE 12:E0189584-E0189584(2017).
CC -!- FUNCTION: [Glycoprotein G2]: Class I viral fusion protein that directs
CC fusion of viral and host endosomal membranes, leading to delivery of
CC the nucleocapsid into the cytoplasm. Membrane fusion is mediated by
CC irreversible conformational changes induced upon acidification in the
CC endosome. {ECO:0000255|HAMAP-Rule:MF_04084,
CC ECO:0000269|PubMed:8291229}.
CC -!- FUNCTION: Stable signal peptide (SSP): cleaved and functions as a
CC signal peptide. In addition, it is also retained as the third component
CC of the GP complex. The SSP is required for efficient glycoprotein
CC expression, post-translational maturation cleavage of GP1 and GP2,
CC glycoprotein transport to the cell surface plasma membrane, formation
CC of infectious virus particles, and acid pH-dependent glycoprotein-
CC mediated cell fusion. {ECO:0000255|HAMAP-Rule:MF_04084,
CC ECO:0000269|PubMed:17376927}.
CC -!- FUNCTION: [Glycoprotein G1]: Interacts with the host receptor (By
CC similarity). Mediates virus attachment to host receptor alpha-
CC dystroglycan DAG1. This attachment induces virion internalization
CC predominantly through clathrin- and caveolin-independent endocytosis
CC (PubMed:9851928). {ECO:0000255|HAMAP-Rule:MF_04084,
CC ECO:0000269|PubMed:9851928}.
CC -!- SUBUNIT: [Glycoprotein G1]: Homotetramer; disulfide-linked (By
CC similarity). Interacts with host DAG1 (PubMed:9851928).
CC {ECO:0000255|HAMAP-Rule:MF_04084, ECO:0000269|PubMed:9851928}.
CC -!- SUBUNIT: [Glycoprotein G2]: Homotetramer. GP2 homotetramers bind
CC through ionic interactions with GP1 homotetramers to form the GP
CC complex together with the stable signal peptide. The GP-C polyprotein
CC interacts with the host protease MBTPS1/SKI-1 resulting in the
CC polyprotein processing. GP-complex interacts with protein Z, which
CC interacts with ribonucleocapsid; these interactions may induce virion
CC budding (PubMed:17581989). {ECO:0000255|HAMAP-Rule:MF_04084,
CC ECO:0000269|PubMed:16731928, ECO:0000269|PubMed:17581989}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Note=Binding to the stable signal
CC peptide masks endogenous ER localization signals in the cytoplasmic
CC domain of G2 to ensure that only the fully assembled, tripartite GP
CC complex is transported for virion assembly. {ECO:0000255|HAMAP-
CC Rule:MF_04084}.
CC -!- SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04084}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- DOMAIN: The cytoplasmic domain of GP2 plays a role in ER location. It
CC also contains a zinc-binding domain that allows SSP retention in the
CC GPC complex by accepting a cysteine from SSP as the fourth ligand.
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. GP-C
CC polyprotein is cleaved in the endoplasmic reticulum by the host
CC protease MBTPS1. Only cleaved glycoprotein is incorporated into
CC virions. {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- PTM: The SSP remains stably associated with the GP complex following
CC cleavage by signal peptidase and plays crucial roles in the trafficking
CC of GP through the secretory pathway. {ECO:0000255|HAMAP-Rule:MF_04084}.
CC -!- SIMILARITY: Belongs to the arenaviridae GPC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04084}.
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DR EMBL; M20869; AAA46256.1; -; Genomic_RNA.
DR EMBL; AY847350; AAX49341.1; -; Genomic_RNA.
DR EMBL; DQ361065; ABC96001.2; -; Genomic_RNA.
DR PIR; A28920; VGXPLA.
DR PIR; B26345; VGXPLM.
DR RefSeq; NP_694851.1; NC_004294.1.
DR PDB; 5JWD; X-ray; 2.50 A; C=392-400.
DR PDB; 5JWE; X-ray; 2.40 A; P/Q/R/S=92-101.
DR PDB; 7P0A; X-ray; 2.43 A; C/F=33-41.
DR PDBsum; 5JWD; -.
DR PDBsum; 5JWE; -.
DR PDBsum; 7P0A; -.
DR SMR; P09991; -.
DR TCDB; 1.G.8.1.1; the arenavirus fusion protein (av-fp) family.
DR GeneID; 956591; -.
DR KEGG; vg:956591; -.
DR Proteomes; UP000002474; Genome.
DR Proteomes; UP000121528; Genome.
DR Proteomes; UP000204492; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi 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:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 2.20.28.180; -; 1.
DR HAMAP; MF_04084; ARENA_GPC; 1.
DR InterPro; IPR001535; Arena_glycoprot.
DR InterPro; IPR043015; Arena_glycoprot_zinc-bd.
DR Pfam; PF00798; Arena_glycoprot; 1.
DR PIRSF; PIRSF004028; GPC_ArenaV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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 endoplasmic reticulum; Host Golgi apparatus;
KW Host membrane; Host-virus interaction; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Reference proteome; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell; Zinc.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CHAIN 2..498
FT /note="Pre-glycoprotein polyprotein GP complex"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000356255"
FT CHAIN 2..58
FT /note="Stable signal peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000356256"
FT CHAIN 59..265
FT /note="Glycoprotein G1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000036603"
FT CHAIN 266..498
FT /note="Glycoprotein G2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT /id="PRO_0000036604"
FT TOPO_DOM 2..17
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 18..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 54..58
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 59..438
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT TOPO_DOM 460..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 481
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT BINDING 483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT SITE 58..59
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT SITE 265..266
FT /note="Cleavage; by host MBTPS1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 92..239
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 123..160
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 184..220
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 285..298
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 307..316
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT DISULFID 370..391
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04084"
FT VARIANT 176
FT /note="D -> N (in strain: Isolate Armstrong 53b)"
FT VARIANT 260
FT /note="F -> L (in strain: Isolate CTL- and Isolate
FT Armstrong-derived variant Cl13)"
FT VARIANT 313
FT /note="A -> E (in strain: Isolate Armstrong 53b and Isolate
FT Armstrong-derived variant Cl13)"
FT MUTAGEN 12
FT /note="P->A: 99% loss of virus infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 12
FT /note="P->G: 96% loss of virus infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 16
FT /note="D->A: More than 99% loss of infectivity; when
FT associated with A-17."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 16
FT /note="D->K: More than 99% loss of infectivity; when
FT associated with K-17."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 17
FT /note="E->A: More than 99% loss of infectivity; when
FT associated with A-16."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 17
FT /note="E->K: More than 99% loss of infectivity; when
FT associated with K-16."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 20
FT /note="N->A: 99% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 20
FT /note="N->K: 91% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 20
FT /note="N->Q: 98% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 33
FT /note="K->A: More than 99% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 33
FT /note="K->D: More than 99% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 37
FT /note="N->A: 97% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 37
FT /note="N->K: 92% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 37
FT /note="N->Q: 7% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 49
FT /note="F->A: More than 99% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 49
FT /note="F->L: 95% loss of ionfectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT MUTAGEN 54
FT /note="G->A: More than 99% loss of infectivity."
FT /evidence="ECO:0000269|PubMed:17376927"
FT CONFLICT 177
FT /note="A -> R (in Ref. 2; AAA46256)"
SQ SEQUENCE 498 AA; 56131 MW; 11737E3555122CE6 CRC64;
MGQIVTMFEA LPHIIDEVIN IVIIVLIVIT GIKAVYNFAT CGIFALISFL LLAGRSCGMY
GLKGPDIYKG VYQFKSVEFD MSHLNLTMPN ACSANNSHHY ISMGTSGLEL TFTNDSIISH
NFCNLTSAFN KKTFDHTLMS IVSSLHLSIR GNSNYKAVSC DFNNGITIQY NLTFSDAQSA
QSQCRTFRGR VLDMFRTAFG GKYMRSGWGW TGSDGKTTWC SQTSYQYLII QNRTWENHCT
YAGPFGMSRI LLSQEKTKFF TRRLAGTFTW TLSDSSGVEN PGGYCLTKWM ILAAELKCFG
NTAVAKCNVN HDAEFCDMLR LIDYNKAALS KFKEDVESAL HLFKTTVNSL ISDQLLMRNH
LRDLMGVPYC NYSKFWYLEH AKTGETSVPK CWLVTNGSYL NETHFSDQIE QEADNMITEM
LRKDYIKRQG STPLALMDLL MFSTSAYLVS IFLHLVKIPT HRHIKGGSCP KPHRLTNKGI
CSCGAFKVPG VKTVWKRR
