Protein VP0
     (VP4-VP2)
Protein VP4
     (Virion protein 4)
     (P1A)
Protein VP2
     (Virion protein 2)
     (P1B)
Protein VP3
     (Virion protein 3)
     (P1C)
Protein VP1
     (Virion protein 1)
     (P1D)
Picornain 2A
     (Protein 2A)
     (P2A)
     (EC 3.4.22.29)
Protein 2B
     (P2B)
Protein 2C
     (P2C)
     (EC 3.6.1.15)
Protein 3A
     (P3A)
Protein 3B
     (P3B)
     (VPg)
Picornain 3C
     (EC 3.4.22.28)
     (Protease 3C)
     (P3C)
RNA-directed RNA polymerase 3D-POL
     (P3D-POL)
     (EC 2.7.7.48)

Gene name

None

From

Poliovirus type 1 (strain Mahoney)

[TaxID: 12081]

Taxonomy

Viruses; ssRNA positive-strand viruses, no DNA stage; Picornavirales; Picornaviridae; Enterovirus.

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. DOI=10.1038/291547a0; PubMed=6264310 [NCBI, ExPASy, EBI, Israel, Japan] Kitamura N., Semler B.L., Rothberg P.G., Larsen G.R., Adler C.J., Dorner A.J., Emini E.A., Hanecak R., Lee J.J., van der Werf S., Anderson C.W., Wimmer E.; "Primary structure, gene organization and polypeptide expression of poliovirus RNA."; Nature 291:547-553(1981).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC RNA]. PubMed=6272282 [NCBI, ExPASy, EBI, Israel, Japan] Racaniello V.R., Baltimore D.; "Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genome."; Proc. Natl. Acad. Sci. U.S.A. 78:4887-4891(1981).
[3]	PROTEIN SEQUENCE OF 2-69. PubMed=6284987 [NCBI, ExPASy, EBI, Israel, Japan] Dorner A.J., Dorner L.F., Larsen G.R., Wimmer E., Anderson C.W.; "Identification of the initiation site of poliovirus polyprotein synthesis."; J. Virol. 42:1017-1028(1982).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1539-1574, AND COVALENT RNA-LINKAGE OF VPG. DOI=10.1016/0092-8674(80)90137-3; PubMed=6250717 [NCBI, ExPASy, EBI, Israel, Japan] Kitamura N., Adler C.J., Rothberg P.G., Martinko J., Nathenson S.G., Wimmer E.; "The genome-linked protein of picornaviruses. VII. Genetic mapping of poliovirus VPg by protein and RNA sequence studies."; Cell 21:295-302(1980).
[5]	COVALENT RNA-LINKAGE OF VPG. PubMed=209034 [NCBI, ExPASy, EBI, Israel, Japan] Ambros V., Baltimore D.; "Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine."; J. Biol. Chem. 253:5263-5266(1978).
[6]	MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF ALA-3. PubMed=1850017 [NCBI, ExPASy, EBI, Israel, Japan] Moscufo N., Simons J., Chow M.; "Myristoylation is important at multiple stages in poliovirus assembly."; J. Virol. 65:2372-2380(1991).
[7]	CHARACTERIZATION OF PROTEIN 2C. PubMed=8385138 [NCBI, ExPASy, EBI, Israel, Japan] Rodriguez P.L., Carrasco L.; "Poliovirus protein 2C has ATPase and GTPase activities."; J. Biol. Chem. 268:8105-8110(1993).
[8]	FUNCTION OF PICORNAIN 2A. DOI=10.1016/S0014-5793(98)01027-8; PubMed=9755863 [NCBI, ExPASy, EBI, Israel, Japan] Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.; "Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F complex."; FEBS Lett. 435:79-83(1998).
[9]	INTERACTION WITH HUMAN RTN3. DOI=10.1074/jbc.M611145200; PubMed=17182608 [NCBI, ExPASy, EBI, Israel, Japan] Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H., Lin K.-H., Lai H.-C., Tang P., Horng J.-T.; "Reticulon 3 binds the 2C protein of enterovirus 71 and is required for viral replication."; J. Biol. Chem. 282:5888-5898(2007).
[10]	TOPOLOGY. DOI=10.1021/bi6024758; PubMed=17417822 [NCBI, ExPASy, EBI, Israel, Japan] Fujita K., Krishnakumar S.S., Franco D., Paul A.V., London E., Wimmer E.; "Membrane topography of the hydrophobic anchor sequence of poliovirus 3A and 3AB proteins and the functional effect of 3A/3AB membrane association upon RNA replication."; Biochemistry 46:5185-5199(2007).
[11]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881. PubMed=2994218 [NCBI, ExPASy, EBI, Israel, Japan] Hogle J.M., Chow M., Filman D.J.; "Three-dimensional structure of poliovirus at 2.9-A resolution."; Science 229:1358-1365(1985).
[12]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-881. DOI=10.1016/S0960-9822(00)00176-7; PubMed=7820548 [NCBI, ExPASy, EBI, Israel, Japan] Grant R.A., Hiremath C.N., Filman D.J., Syed R., Andries K., Hogle J.M.; "Structures of poliovirus complexes with anti-viral drugs: implications for viral stability and drug design."; Curr. Biol. 4:784-797(1994).
[13]	STRUCTURE BY ELECTRON MICROSCOPY (2.0 ANGSTROMS) OF 1-881. DOI=10.1073/pnas.97.1.79; PubMed=10618374 [NCBI, ExPASy, EBI, Israel, Japan] He Y., Bowman V.D., Mueller S., Bator C.M., Bella J., Peng X., Baker T.S., Wimmer E., Kuhn R.J., Rossmann M.G.; "Interaction of the poliovirus receptor with poliovirus."; Proc. Natl. Acad. Sci. U.S.A. 97:79-84(2000).

Comments

FUNCTION: Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. The interaction of five VP1 proteins in the fivefold axes results in a prominent protusion extending to about 25 Angstroms from the capsid shell. The resulting structure appears as a steep plateau encircled by a valley or cleft. This depression also termed canyon is the receptor binding site. The capsid interacts with human PVR at this site to provide virion attachment to target cell.
FUNCTION: VP0 precursor is a component of immature procapsids (By similarity).
FUNCTION: Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription.
FUNCTION: Protein 2B affects membrane integrity and cause an increase in membrane permeability (By similarity).
FUNCTION: Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities.
FUNCTION: Protein 3A, via its hydrophobic domain, serves as membrane anchor. It also inhibits endoplasmic reticulum-to-Golgi transport (By similarity).
FUNCTION: Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).
FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
CATALYTIC ACTIVITY: NTP + H₂O = NDP + phosphate.
SUBUNIT: P2C N-terminus interacts with human RTN3. This interaction is important for viral replication (By similarity). Interacts with human PVR.
SUBCELLULAR LOCATION: Protein VP2: Virion. Cytoplasm (Potential).
SUBCELLULAR LOCATION: Protein VP3: Virion. Cytoplasm (Potential).
SUBCELLULAR LOCATION: Protein VP1: Virion. Cytoplasm (Potential).
SUBCELLULAR LOCATION: Protein 2B: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
SUBCELLULAR LOCATION: Protein 2C: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
SUBCELLULAR LOCATION: Protein 3A: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
SUBCELLULAR LOCATION: Protein 3B: Virion (Potential).
SUBCELLULAR LOCATION: Picornain 3C: Cytoplasm (Potential).
SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity).
PTM: VPg is covalently linked to the genomic RNA (By similarity).
PTM: Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle (By similarity).
SIMILARITY: Belongs to the picornaviruses polyprotein family.
SIMILARITY: Contains 2 peptidase C3 domains [view classification].
SIMILARITY: Contains 1 RdRp catalytic domain.
SIMILARITY: Contains 1 SF3 helicase domain.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure associated with cellular receptor; URL="http://viperdb.scripps.edu/info_page.php?VDB=1dgi";.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure associated with cellular receptor; URL="http://viperdb.scripps.edu/info_page.php?VDB=1nn8";.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure in complex with R80633, an inhibitor of viral replication; URL="http://viperdb.scripps.edu/info_page.php?VDB=1po1";.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure in complex with R77975, an inhibitor of viral replication; URL="http://viperdb.scripps.edu/info_page.php?VDB=1po2";.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral empty capsid structure; URL="http://viperdb.scripps.edu/info_page.php?VDB=1pov";.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure complexed with R78206; URL="http://viperdb.scripps.edu/info_page.php?VDB=1vbd";.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure; URL="http://viperdb.scripps.edu/info_page.php?VDB=2plv";.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure of 135S cell entry intermediate; URL="http://viperdb.scripps.edu/info_page.php?VDB=1xyr";.
WEB RESOURCE: Name=Virus Particle ExploreR db; Note= Icosahedral capsid structure; URL="http://viperdb.scripps.edu/info_page.php?VDB=1hxs";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

V01149; CAA24461.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V01148; CAA24446.1; -; Genomic_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A03898; GNNY2P.
A93258; GNNY1P.

RefSeq

NP_041277.1; -.

3D structure databases

PDB

1AL2; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.	[ExPASy / RCSB / EBI]
1AR6; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.	[ExPASy / RCSB / EBI]
1AR7; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.	[ExPASy / RCSB / EBI]
1AR8; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.	[ExPASy / RCSB / EBI]
1AR9; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.	[ExPASy / RCSB / EBI]
1ASJ; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.	[ExPASy / RCSB / EBI]
1DGI; EM; 22.00 A; 1=599-881, 2=74-341, 3=342-576, 4=2-69.	[ExPASy / RCSB / EBI]
1FPT; X-ray; 3.00 A; P=665-682.	[ExPASy / RCSB / EBI]
1HXS; X-ray; 2.20 A; 1=580-881, 2=70-341, 3=342-578, 4=2-69.	[ExPASy / RCSB / EBI]
1L1N; X-ray; 2.10 A; A/B=1566-1748.	[ExPASy / RCSB / EBI]
1NG7; NMR; -; A/B=1457-1515.	[ExPASy / RCSB / EBI]
1NN8; EM; 15.00 A; 1=580-881, 2=70-341, 3=342-576, 4=1-69.	[ExPASy / RCSB / EBI]
1PO1; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.	[ExPASy / RCSB / EBI]
1PO2; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.	[ExPASy / RCSB / EBI]
1POV; X-ray; 2.80 A; 0=25-341, 1=580-881, 3=342-579.	[ExPASy / RCSB / EBI]
1RA6; X-ray; 2.00 A; A=1749-2209.	[ExPASy / RCSB / EBI]
1RA7; X-ray; 2.35 A; A=1749-2209.	[ExPASy / RCSB / EBI]
1RAJ; X-ray; 2.50 A; A=1817-2209.	[ExPASy / RCSB / EBI]
1RDR; X-ray; 2.40 A; A=1749-2209.	[ExPASy / RCSB / EBI]
1TQL; X-ray; 2.30 A; A=1750-2209.	[ExPASy / RCSB / EBI]
1VBD; X-ray; 2.90 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.	[ExPASy / RCSB / EBI]
1XYR; EM; 11.00 A; 1=650-881, 2=97-333, 3=391-572, 5=342-353, 6=355-390, 7=82-95, 8=621-631.	[ExPASy / RCSB / EBI]
2BBL; NMR; -; A=1544-1565.	[ExPASy / RCSB / EBI]
2BBP; NMR; -; A=1544-1565.	[ExPASy / RCSB / EBI]
2IJD; X-ray; 3.40 A; 1/2=1566-2209.	[ExPASy / RCSB / EBI]
2IJF; X-ray; 3.00 A; A=1749-2209.	[ExPASy / RCSB / EBI]
2ILY; X-ray; 2.60 A; A=1749-2209.	[ExPASy / RCSB / EBI]
2ILZ; X-ray; 2.50 A; A=1749-2209.	[ExPASy / RCSB / EBI]
2IM0; X-ray; 2.25 A; A=1749-2209.	[ExPASy / RCSB / EBI]
2IM1; X-ray; 2.50 A; A=1749-2209.	[ExPASy / RCSB / EBI]
2IM2; X-ray; 2.35 A; A=1749-2209.	[ExPASy / RCSB / EBI]
2IM3; X-ray; 2.60 A; A=1749-2209.	[ExPASy / RCSB / EBI]
2PLV; X-ray; 2.88 A; 1=580-881, 2=70-341, 3=342-579, 4=2-69.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AL2; -.
1AR6; -.
1AR7; -.
1AR8; -.
1AR9; -.
1ASJ; -.
1DGI; -.
1FPT; -.
1HXS; -.
1L1N; -.
1NG7; -.
1NN8; -.
1PO1; -.
1PO2; -.
1POV; -.
1RA6; -.
1RA7; -.
1RAJ; -.
1RDR; -.
1TQL; -.
1VBD; -.
1XYR; -.
2BBL; -.
2BBP; -.
2IJD; -.
2IJF; -.
2ILY; -.
2ILZ; -.
2IM0; -.
2IM1; -.
2IM2; -.
2IM3; -.
2PLV; -.

SMR

P03300; 1566-2209.

ModBase

P03300.

Ontologies

GO:0031410;	Cellular component: cytoplasmic vesicle (inferred from electronic annotation from UniProtKB-KW).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003593; AAA+_ATPase_core.
IPR004004; Helicase/Pol/Pept_Calicivir.
IPR000605; Helicase_SF3_ssDNA/RNA_vir.
IPR014759; Helicase_SF3_ssRNA_vir.
IPR014838; P3A.
IPR000199; Pept_C3_picorn.
IPR000081; Peptidase_C3.
IPR003138; Pico_P1A.
IPR002527; Pico_P2B.
IPR001676; Picornavirus_capsid.
IPR001205; RNA_pol_P3D.
IPR007094; RNA_pol_PSvir.
Graphical view of domain structure.

Pfam

PF08727; P3A; 1.
PF00548; Peptidase_C3; 1.
PF02226; Pico_P1A; 1.
PF00947; Pico_P2A; 1.
PF01552; Pico_P2B; 1.
PF00680; RdRP_1; 1.
PF00073; Rhv; 3.
PF00910; RNA_helicase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00918; CALICVIRUSNS.

ProDom

PD001125; Pept_C3_picorn; 1.
PD001306; Peptidase_C3_2; 1.
PD001274; Pico_P2B; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00382; AAA; 1.
SMART graphical view of domain structure.

PROSITE

PS50507; RDRP_SSRNA_POS; 1.
PS51218; SF3_HELICASE_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

919920; -.

Other

LinkHub

P03300; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; ATP-binding; Capsid protein; Complete proteome; Covalent protein-RNA linkage; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Helicase; Host-virus interaction; Hydrolase; Lipoprotein; Membrane; Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein; Protease; RNA replication; RNA-binding; RNA-directed RNA polymerase; Thiol protease; Transferase; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed; by host (By similarity).`
`CHAIN`	`2 341`	`340`	`Protein VP0 (Potential).`	`PRO_0000311078`
`CHAIN`	`2 69`	`68`	`Protein VP4 (Potential).`	`PRO_0000040080`
`CHAIN`	`70 341`	`272`	`Protein VP2 (Potential).`	`PRO_0000040081`
`CHAIN`	`342 579`	`238`	`Protein VP3 (Potential).`	`PRO_0000040082`
`CHAIN`	`580 881`	`302`	`Protein VP1 (Potential).`	`PRO_0000040083`
`CHAIN`	`882 1030`	`149`	`Picornain 2A (Potential).`	`PRO_0000040084`
`CHAIN`	`1031 1127`	`97`	`Protein 2B (Potential).`	`PRO_0000040085`
`CHAIN`	`1128 1456`	`329`	`Protein 2C (Potential).`	`PRO_0000040086`
`CHAIN`	`1457 1543`	`87`	`Protein 3A (Potential).`	`PRO_0000040087`
`CHAIN`	`1544 1565`	`22`	`Protein 3B (Potential).`	`PRO_0000040088`
`CHAIN`	`1566 1747`	`182`	`Picornain 3C (Potential).`	`PRO_0000040089`
`CHAIN`	`1748 2209`	`462`	`RNA-directed RNA polymerase 3D-POL (Potential).`	`PRO_0000040090`
`TOPO_DOM`	`2 1520`	`1519`	`Cytoplasmic (Potential).`
`TOPO_DOM`	`1521 1536`	`16`	`In membrane (Potential).`
`TOPO_DOM`	`1537 2209`	`673`	`Cytoplasmic (Potential).`
`DOMAIN`	`1232 1388`	`157`	`SF3 helicase.`
`DOMAIN`	`1975 2090`	`116`	`RdRp catalytic.`
`NP_BIND`	`1256 1263`	`8`	`ATP (Potential).`
`ACT_SITE`	`901 901`		`For picornain 2A activity (By similarity).`
`ACT_SITE`	`919 919`		`For picornain 2A activity (By similarity).`
`ACT_SITE`	`990 990`		`For picornain 2A activity (By similarity).`
`ACT_SITE`	`1605 1605`		`For picornain 3C activity (Potential).`
`ACT_SITE`	`1636 1636`		`For picornain 3C activity (Potential).`
`ACT_SITE`	`1712 1712`		`For picornain 3C activity (Potential).`
`SITE`	`25 25`	`1`	`Involved in the interaction with human RTN3 (By similarity).`
`SITE`	`69 70`	`2`	`Cleavage (Potential).`
`SITE`	`341 342`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`881 882`	`2`	`Cleavage; by picornain 2A (Potential).`
`SITE`	`1030 1031`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`1127 1128`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`1456 1457`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`1543 1544`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`1565 1566`	`2`	`Cleavage; by picornain 3C (Potential).`
`SITE`	`1748 1749`	`2`	`Cleavage; by picornain 3C (Potential).`
`MOD_RES`	`1546 1546`		`O-(5'-phospho-RNA)-tyrosine.`
`LIPID`	`2 2`		`N-myristoyl glycine; by host (Probable).`
`MUTAGEN`	`3 3`		`A->D: 50% loss of myristoylation. Severe reduction in specific infectivity.`
`MUTAGEN`	`3 3`		`A->G,L,V: No effect on myristoylation and virus growth.`
`MUTAGEN`	`3 3`		`A->H: No effect on myristoylation. Severe reduction in specific infectivity.`
`CONFLICT`	`242 264`		`RFCPVDYLLGNGTLLGNAFVFPH -> SSARWITSLEMARCWGMPLCSA (in Ref. 2; CAA24446).`
`CONFLICT`	`287 287`		`I -> L (in Ref. 2; CAA24446).`
`CONFLICT`	`309 309`		`A -> V (in Ref. 2; CAA24446).`
`CONFLICT`	`420 422`		`DDP -> AAS (in Ref. 2; CAA24446).`
`CONFLICT`	`464 464`		`F -> S (in Ref. 2; CAA24446).`
`CONFLICT`	`515 515`		`T -> S (in Ref. 2; CAA24446).`
`CONFLICT`	`855 856`		`AV -> QL (in Ref. 2; CAA24446).`
`CONFLICT`	`972 972`		`A -> V (in Ref. 2; CAA24446).`
`CONFLICT`	`985 985`		`A -> E (in Ref. 2; CAA24446).`
`CONFLICT`	`1140 1141`		`NA -> QR (in Ref. 2; CAA24446).`
`CONFLICT`	`1619 1619`		`V -> A (in Ref. 2; CAA24446).`
`CONFLICT`	`1626 1627`		`AL -> VF (in Ref. 2; CAA24446).`
`CONFLICT`	`1635 1635`		`L -> F (in Ref. 2; CAA24446).`
`CONFLICT`	`1682 1682`		`G -> R (in Ref. 2; CAA24446).`
`CONFLICT`	`1722 1730`		`VIGMHVGGN -> SSGCMLVD (in Ref.`