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Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

 POLG_POL3L              Reviewed;        2206 AA.
P03302; Q84783; Q84784; Q84785; Q84786; Q84787; Q84788; Q84789; Q84790;
Q98592; Q98593; Q98594;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
02-JUN-2021, entry version 203.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=P1;
Contains:
RecName: Full=Capsid protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Capsid protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Capsid protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Capsid protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Capsid protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=P2;
Contains:
RecName: Full=Protease 2A;
Short=P2A;
EC=3.4.22.29 {ECO:0000250|UniProtKB:P03300};
AltName: Full=Picornain 2A;
AltName: Full=Protein 2A;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15 {ECO:0000250|UniProtKB:P03300};
Contains:
RecName: Full=P3;
Contains:
RecName: Full=Protein 3AB;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Viral protein genome-linked;
Short=VPg;
AltName: Full=Protein 3B;
Short=P3B;
Contains:
RecName: Full=Protein 3CD;
EC=3.4.22.28;
Contains:
RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222};
AltName: Full=Picornain 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
Contains:
RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
Short=RdRp;
EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
AltName: Full=3D polymerase;
Short=3Dpol;
AltName: Full=Protein 3D;
Short=3D;
Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B).
Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
Picornavirales; Picornaviridae; Enterovirus; Enterovirus C.
NCBI_TaxID=12088;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=P3/Leon/37;
PubMed=6324200; DOI=10.1073/pnas.81.5.1539;
Stanway G., Hughes P.J., Mountford R.C., Reeve P., Minor P.D., Schild G.C.,
Almond J.W.;
"Comparison of the complete nucleotide sequences of the genomes of the
neurovirulent poliovirus P3/Leon/37 and its attenuated Sabin vaccine
derivative P3/Leon 12a1b.";
Proc. Natl. Acad. Sci. U.S.A. 81:1539-1543(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=P3/Leon 12A[1]B;
PubMed=6310508; DOI=10.1093/nar/11.16.5629;
Stanway G., Cann A.J., Hauptmann R., Hughes P.J., Clarke L.D.,
Mountford R.C., Minor P.D., Schild G.C., Almond J.W.;
"The nucleotide sequence of poliovirus type 3 Leon 12 a1b: comparison with
poliovirus type 1.";
Nucleic Acids Res. 11:5629-5643(1983).
[3]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-878.
PubMed=7820548; DOI=10.1016/s0960-9822(00)00176-7;
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).
[4]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-878.
PubMed=15299834; DOI=10.1107/s090744499401084x;
Hiremath C.N., Grant R.A., Filman D.J., Hogle J.M.;
"Binding of the antiviral drug win51711 to the Sabin strain of type-3
poliovirus -structural comparison with drug-binding in rhinovirus-14.";
Acta Crystallogr. D 51:473-489(1995).
-!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
capsid is 300 Angstroms in diameter, composed of 60 copies of each
capsid protein and enclosing the viral positive strand RNA genome (By
similarity). Capsid protein VP1 mainly forms the vertices of the capsid
(By similarity). Capsid protein VP1 interacts with host cell receptor
PVR to provide virion attachment to target host cells (By similarity).
This attachment induces virion internalization predominantly through
clathrin- and caveolin-independent endocytosis in Hela cells and
through caveolin-mediated endocytosis in brain microvascular
endothelial cells (By similarity). Tyrosine kinases are probably
involved in the entry process (By similarity). Virus binding to PVR
induces increased junctional permeability and rearrangement of
junctional proteins (By similarity). Modulation of endothelial tight
junctions, as well as cytolytic infection of endothelial cells
themselves, may result in loss of endothelial integrity which may help
the virus to reach the CNS (By similarity). After binding to its
receptor, the capsid undergoes conformational changes (By similarity).
Capsid protein VP1 N-terminus (that contains an amphipathic alpha-
helix) and capsid protein VP4 are externalized (By similarity).
Together, they shape a pore in the host membrane through which viral
genome is translocated to host cell cytoplasm (By similarity).
{ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo
T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
capsid is 300 Angstroms in diameter, composed of 60 copies of each
capsid protein and enclosing the viral positive strand RNA genome (By
similarity). {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The
capsid is 300 Angstroms in diameter, composed of 60 copies of each
capsid protein and enclosing the viral positive strand RNA genome (By
similarity). {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid
shell (By similarity). After binding to the host receptor, the capsid
undergoes conformational changes (By similarity). Capsid protein VP4 is
released, Capsid protein VP1 N-terminus is externalized, and together,
they shape a pore in the host membrane through which the viral genome
is translocated into the host cell cytoplasm (By similarity).
{ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which
is cleaved into capsid proteins VP4 and VP2 after maturation (By
similarity). Allows the capsid to remain inactive before the maturation
step (By similarity). {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Protease 2A]: Cysteine protease that cleaves viral
polyprotein and specific host proteins (By similarity). It is
responsible for the autocatalytic cleavage between the P1 and P2
regions, which is the first cleavage occurring in the polyprotein (By
similarity). Cleaves also the host translation initiation factor
EIF4G1, in order to shut down the capped cellular mRNA translation (By
similarity). Inhibits the host nucleus-cytoplasm protein and RNA
trafficking by cleaving host members of the nuclear pores including
NUP98, NUP62 and NUP153 (By similarity). Counteracts stress granule
formation probably by antagonizing its assembly or promoting its
dissassembly (By similarity). Cleaves and inhibits host IFIH1/MDA5,
thereby inhibiting the type-I IFN production and the establishment of
the antiviral state (By similarity). Cleaves and inhibits host MAVS,
thereby inhibiting the type-I IFN production and the establishment of
the antiviral state (By similarity). {ECO:0000250|UniProtKB:P03300,
ECO:0000250|UniProtKB:P03301}.
-!- FUNCTION: [Protein 2B]: Plays an essential role in the virus
replication cycle by acting as a viroporin. Creates a pore in the host
reticulum endoplasmic and as a consequence releases Ca2+ in the
cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium
may trigger membrane trafficking and transport of viral ER-associated
proteins to viroplasms, sites of viral genome replication.
{ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Protein 2C]: Induces and associates with structural
rearrangements of intracellular membranes. Displays RNA-binding,
nucleotide binding and NTPase activities. May play a role in virion
morphogenesis and viral RNA encapsidation by interacting with the
capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Protein 3AB]: Localizes the viral replication complex to the
surface of membranous vesicles. Together with protein 3CD binds the
Cis-Active RNA Element (CRE) which is involved in RNA synthesis
initiation. Acts as a cofactor to stimulate the activity of 3D
polymerase, maybe through a nucleid acid chaperone activity.
{ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Protein 3A]: Localizes the viral replication complex to the
surface of membranous vesicles (By similarity). It inhibits host cell
endoplasmic reticulum-to-Golgi apparatus transport and causes the
disassembly of the Golgi complex, possibly through GBF1 interaction (By
similarity). This would result in depletion of MHC, trail receptors and
IFN receptors at the host cell surface (By similarity). Plays an
essential role in viral RNA replication by recruiting ACBD3 and PI4KB
at the viral replication sites, thereby allowing the formation of the
rearranged membranous structures where viral replication takes place
(By similarity). {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA
replication and remains covalently bound to viral genomic RNA. VPg is
uridylylated prior to priming replication into VPg-pUpU (By
similarity). The oriI viral genomic sequence may act as a template for
this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by
the RNA-dependent RNA polymerase to replicate the viral genome (By
similarity). Following genome release from the infecting virion in the
cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By
similarity). During the late stage of the replication cycle, host TDP2
is excluded from sites of viral RNA synthesis and encapsidation,
allowing for the generation of progeny virions (By similarity).
{ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Protein 3CD]: Involved in the viral replication complex and
viral polypeptide maturation. It exhibits protease activity with a
specificity and catalytic efficiency that is different from protease
3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the
5'UTR of the viral genome. {ECO:0000250|UniProtKB:P03300}.
-!- FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic
processing of the polyprotein (By similarity). Cleaves host EIF5B,
contributing to host translation shutoff (By similarity). Cleaves also
host PABPC1, contributing to host translation shutoff (By similarity).
Cleaves host DDX58/RIG-I and thus contributes to the inhibition of type
I interferon production (By similarity). Cleaves host NLRP1, triggers
host N-glycine-mediated degradation of the autoinhibitory NLRP1 N-
terminal fragment (By similarity). {ECO:0000250|UniProtKB:P03300,
ECO:0000250|UniProtKB:P03303}.
-!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genomic
RNA on the surface of intracellular membranes. May form linear arrays
of subunits that propagate along a strong head-to-tail interaction
called interface-I. Covalently attaches UMP to a tyrosine of VPg, which
is used to prime RNA synthesis. The positive stranded RNA genome is
first replicated at virus induced membranous vesicles, creating a dsRNA
genomic replication form. This dsRNA is then used as template to
synthesize positive stranded RNA genomes. ss(+)RNA genomes are either
translated, replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}.
-!- CATALYTIC ACTIVITY: [Protein 2C]:
Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
Evidence={ECO:0000250|UniProtKB:P03300};
-!- CATALYTIC ACTIVITY: [Protease 2A]:
Reaction=Selective cleavage of Tyr-|-Gly bond in the picornavirus
polyprotein.; EC=3.4.22.29; Evidence={ECO:0000250|UniProtKB:P03300};
-!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
-!- CATALYTIC ACTIVITY: [Protease 3C]:
Reaction=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.; EC=3.4.22.28;
Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
-!- COFACTOR: [RNA-directed RNA polymerase]:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P03300};
Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal
center (By similarity). The magnesium ions are not prebound but only
present for catalysis (By similarity). Requires the presence of 3CDpro
or 3CPro (By similarity). {ECO:0000250|UniProtKB:P03300,
ECO:0000250|UniProtKB:P03313};
-!- ACTIVITY REGULATION: [RNA-directed RNA polymerase]: Replication or
transcription is subject to high level of random mutations by the
nucleotide analog ribavirin. {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 and
capsid protein VP3 to form heterotrimeric protomers.
{ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0, and
capsid protein VP3 to form heterotrimeric protomers (By similarity).
Interacts with human PVR (By similarity). Five protomers subsequently
associate to form pentamers which serve as building blocks for the
capsid (By similarity). Interacts with capsid protein VP2, capsid
protein VP3 and capsid protein VP4 following cleavage of capsid protein
VP0 (By similarity). {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Capsid protein VP2]: Interacts with capsid protein VP1 and
capsid protein VP3 in the mature capsid.
{ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0 and
capsid protein VP1 to form heterotrimeric protomers (By similarity).
Five protomers subsequently associate to form pentamers which serve as
building blocks for the capsid (By similarity). Interacts with capsid
protein VP4 in the mature capsid (By similarity). Interacts with
protein 2C; this interaction may be important for virion morphogenesis
(By similarity). {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Capsid protein VP4]: Interacts with capsid protein VP1 and
capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Protease 2A]: Homodimer. {ECO:0000250|UniProtKB:P04936}.
-!- SUBUNIT: [Protein 2C]: Homohexamer; forms a hexameric ring structure
with 6-fold symmetry characteristic of AAA+ ATPases (By similarity).
Interacts (via N-terminus) with host RTN3 (via reticulon domain); this
interaction is important for viral replication (By similarity).
Interacts with capsid protein VP3; this interaction may be important
for virion morphogenesis (By similarity).
{ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Protein 3AB]: Interacts with protein 3CD.
{ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Protein 3A]: Homodimer (By similarity). Interacts with host
GBF1 (By similarity). Interacts (via GOLD domain) with host ACBD3 (via
GOLD domain); this interaction allows the formation of a viral protein
3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate
the recruitment of host PI4KB in order to synthesize PI4P at the viral
RNA replication sites (By similarity). {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Viral protein genome-linked]: Interacts with RNA-directed RNA
polymerase. {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [Protein 3CD]: Interacts with protein 3AB and with RNA-
directed RNA polymerase. {ECO:0000250|UniProtKB:P03300}.
-!- SUBUNIT: [RNA-directed RNA polymerase]: Interacts with Viral protein
genome-linked and with protein 3CD. {ECO:0000250|UniProtKB:P03300}.
-!- SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.
-!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion
{ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
{ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
{ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. 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.
-!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. 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.
-!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. 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.
-!- SUBCELLULAR LOCATION: [Protein 3AB]: Host cytoplasmic vesicle membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. 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.
-!- SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion
{ECO:0000250|UniProtKB:P03300}. Host cytoplasm
{ECO:0000250|UniProtKB:Q66478}.
-!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm.
-!- SUBCELLULAR LOCATION: [Protein 3CD]: Host nucleus
{ECO:0000250|UniProtKB:P03300}. Host cytoplasm
{ECO:0000250|UniProtKB:P03300}. Host cytoplasmic vesicle membrane
{ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
side {ECO:0000305}. 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.
-!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
vesicle membrane {ECO:0000305}; Peripheral membrane protein
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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.
-!- DOMAIN: [Protein 2C]: The N-terminus has membrane-binding (By
similarity). The N-terminus also displays RNA-binding properties (By
similarity). The N-terminus is involved in oligomerization (By
similarity). The central part contains an ATPase domain and a C4-type
zinc-finger (By similarity). The C-terminus is involved in RNA-binding
(By similarity). The extreme C-terminus contains a region involved in
oligomerization (By similarity). {ECO:0000250|UniProtKB:P03300}.
-!- PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the
viral proteases yield processing intermediates and the mature proteins.
{ECO:0000250|UniProtKB:P03300}.
-!- PTM: [Capsid protein VP0]: Myristoylation is required for the formation
of pentamers during virus assembly. Further assembly of 12 pentamers
and a molecule of genomic RNA generates the provirion.
{ECO:0000250|UniProtKB:P03300}.
-!- PTM: [Capsid protein VP0]: During virion maturation, immature virions
are rendered infectious following cleavage of VP0 into VP4 and VP2.
This maturation seems to be an autocatalytic event triggered by the
presence of RNA in the capsid and it is followed by a conformational
change infectious virion. {ECO:0000250|UniProtKB:P03300}.
-!- PTM: [Capsid protein VP4]: Myristoylation is required during RNA
encapsidation and formation of the mature virus particle.
{ECO:0000250|UniProtKB:P03300}.
-!- PTM: [Viral protein genome-linked]: VPg is uridylylated by the
polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for
the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}.
-!- MISCELLANEOUS: The sequence of strain Sabin vaccine P3/Leon/37 is
shown. {ECO:0000305}.
-!- MISCELLANEOUS: The strain Sabin vaccine P3/Leon/37 is the progenitor of
the strain Sabin vaccine P3/Leon 12a[1]b. {ECO:0000305}.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure in complex with antiviral compound R78206;
URL="http://viperdb.scripps.edu/Info_Page.php?VDB=1vba";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure in complex with antiviral compound R80633;
URL="http://viperdb.scripps.edu/Info_Page.php?VDB=1vbb";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure in complex with antiviral compound R77975;
URL="http://viperdb.scripps.edu/Info_Page.php?VDB=1vbc";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure of mutant F700L, F710L in complex with antiviral compound
R78206;
URL="http://viperdb.scripps.edu/Info_Page.php?VDB=1vbe";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure in complex with antiviral compound WIN51711;
URL="http://viperdb.scripps.edu/Info_Page.php?VDB=1piv";
-!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
structure;
URL="http://viperdb.scripps.edu/Info_Page.php?VDB=1pvc";
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EMBL; K01392; AAA46914.1; -; Genomic_RNA.
EMBL; X00925; CAA25444.1; -; Genomic_RNA.
PIR; A93987; GNNY4P.
PDB; 1PIV; X-ray; 2.90 A; 1=578-878, 2=70-340, 3=341-578, 4=2-69.
PDB; 1PVC; X-ray; 2.40 A; 1=578-878, 2=70-340, 3=341-578, 4=2-69.
PDB; 1VBA; X-ray; 2.90 A; 1=579-878, 2=70-340, 3=341-575, 4=2-69.
PDB; 1VBB; X-ray; 2.80 A; 1=579-878, 2=70-340, 3=341-575, 4=2-69.
PDB; 1VBC; X-ray; 2.80 A; 1=579-878, 2=70-340, 3=341-575, 4=2-69.
PDB; 1VBE; X-ray; 2.80 A; 1=579-878, 2=70-340, 3=341-575, 4=2-69.
PDB; 3EPD; EM; -; 1=600-878, 2=75-340, 3=341-575, 4=2-69.
PDB; 3IYB; EM; -; 2=83-96.
PDB; 3IYC; EM; -; 2=83-96.
PDB; 5O5B; EM; 3.60 A; 4=1-69.
PDB; 5O5P; EM; 4.10 A; 4=1-69.
PDBsum; 1PIV; -.
PDBsum; 1PVC; -.
PDBsum; 1VBA; -.
PDBsum; 1VBB; -.
PDBsum; 1VBC; -.
PDBsum; 1VBE; -.
PDBsum; 3EPD; -.
PDBsum; 3IYB; -.
PDBsum; 3IYC; -.
PDBsum; 5O5B; -.
PDBsum; 5O5P; -.
BMRB; P03302; -.
SMR; P03302; -.
DrugBank; DB08014; (METHYLPYRIDAZINE PIPERIDINE BUTYLOXYPHENYL)ETHYLACETATE.
DrugBank; DB08013; (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE.
DrugBank; DB08726; 5-(7-(4-(4,5-dihydro-2-oxazolyl)phenoxy)heptyl)-3-methyl isoxazole.
DrugBank; DB08231; Myristic acid.
DrugBank; DB08012; Pirodavir.
DrugBank; DB03203; Sphingosine.
MEROPS; C03.020; -.
EvolutionaryTrace; P03302; -.
Proteomes; UP000008147; Genome.
Proteomes; UP000008995; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:UniProtKB-EC.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075513; P:caveolin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
GO; GO:0039690; P:positive stranded viral RNA replication; ISS:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0039554; P:suppression by virus of host MDA-5 activity; IEA:UniProtKB-KW.
GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; ISS:UniProtKB.
GO; GO:0039540; P:suppression by virus of host RIG-I activity; IEA:UniProtKB-KW.
GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 3.
Gene3D; 1.10.10.870; -; 1.
Gene3D; 2.40.10.10; -; 4.
Gene3D; 2.60.120.20; -; 3.
Gene3D; 3.30.70.270; -; 1.
InterPro; IPR043502; DNA/RNA_pol_sf.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014838; P3A.
InterPro; IPR036203; P3A_soluble_dom.
InterPro; IPR044067; PCV_3C_PRO.
InterPro; IPR000081; Peptidase_C3.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
InterPro; IPR003138; Pico_P1A.
InterPro; IPR002527; Pico_P2B.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR029053; Viral_coat.
Pfam; PF08727; P3A; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF02226; Pico_P1A; 1.
Pfam; PF00947; Pico_P2A; 1.
Pfam; PF01552; Pico_P2B; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 3.
Pfam; PF00910; RNA_helicase; 1.
SUPFAM; SSF50494; SSF50494; 2.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF56672; SSF56672; 1.
SUPFAM; SSF89043; SSF89043; 1.
PROSITE; PS51874; PCV_3C_PRO; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure; Activation of host autophagy by virus; ATP-binding;
Autocatalytic cleavage; Capsid protein;
Caveolin-mediated endocytosis of virus by host;
Clathrin- and caveolin-independent endocytosis of virus by host;
Covalent protein-RNA linkage; DNA replication;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host transcription shutoff by virus;
Eukaryotic host translation shutoff by virus; Helicase; Host cytoplasm;
Host cytoplasmic vesicle; Host gene expression shutoff by virus;
Host membrane; Host mRNA suppression by virus; Host nucleus;
Host-virus interaction; Hydrolase;
Inhibition of eukaryotic host transcription initiation by virus;
Inhibition of host innate immune response by virus;
Inhibition of host MAVS by virus; Inhibition of host MDA5 by virus;
Inhibition of host mRNA nuclear export by virus;
Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
Ion channel; Ion transport; Lipoprotein; Magnesium; Membrane;
Metal-binding; Myristate; Nucleotide-binding; Nucleotidyltransferase;
Phosphoprotein; Pore-mediated penetration of viral genome into host cell;
Protease; Repeat; RNA-binding; RNA-directed RNA polymerase;
T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
Transport; Viral attachment to host cell; Viral immunoevasion;
Viral ion channel; Viral penetration into host cytoplasm;
Viral RNA replication; Virion; Virus endocytosis by host;
Virus entry into host cell; Zinc; Zinc-finger.
INIT_MET 1
/note="Removed; by host"
/evidence="ECO:0000250|UniProtKB:P03300"
CHAIN 2..2206
/note="Genome polyprotein"
/id="PRO_0000426656"
CHAIN 2..878
/note="P1"
/id="PRO_0000426657"
CHAIN 2..340
/note="Capsid protein VP0"
/id="PRO_0000426658"
CHAIN 2..69
/note="Capsid protein VP4"
/id="PRO_0000426659"
CHAIN 70..340
/note="Capsid protein VP2"
/id="PRO_0000426660"
CHAIN 341..578
/note="Capsid protein VP3"
/id="PRO_0000426661"
CHAIN 579..878
/note="Capsid protein VP1"
/id="PRO_0000426662"
CHAIN 879..1453
/note="P2"
/id="PRO_0000426663"
CHAIN 879..1027
/note="Protease 2A"
/id="PRO_0000426664"
CHAIN 1028..1124
/note="Protein 2B"
/id="PRO_0000040140"
CHAIN 1125..1453
/note="Protein 2C"
/id="PRO_0000040141"
CHAIN 1454..2206
/note="P3"
/id="PRO_0000426665"
CHAIN 1454..1562
/note="Protein 3AB"
/id="PRO_0000426666"
CHAIN 1454..1540
/note="Protein 3A"
/id="PRO_0000040142"
CHAIN 1541..1562
/note="Viral protein genome-linked"
/id="PRO_0000426667"
CHAIN 1563..2206
/note="Protein 3CD"
/id="PRO_0000426668"
CHAIN 1563..1745
/note="Protease 3C"
/id="PRO_0000426669"
CHAIN 1746..2206
/note="RNA-directed RNA polymerase"
/id="PRO_0000426670"
TOPO_DOM 2..1517
/note="Cytoplasmic"
/evidence="ECO:0000255"
INTRAMEM 1518..1533
/evidence="ECO:0000255"
TOPO_DOM 1534..2206
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 1229..1385
/note="SF3 helicase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
DOMAIN 1563..1741
/note="Peptidase C3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
DOMAIN 1972..2087
/note="RdRp catalytic"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
NP_BIND 1253..1260
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
ZN_FING 1393..1410
/note="C4-type"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 579..603
/note="Amphipatic alpha-helix"
/evidence="ECO:0000255"
REGION 579..599
/note="Amphipatic alpha-helix"
/evidence="ECO:0000255"
REGION 1125..1263
/note="Oligomerization"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 1125..1197
/note="Membrane-binding"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 1146..1150
/note="RNA-binding"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 1437..1444
/note="RNA-binding"
/evidence="ECO:0000250|UniProtKB:P03300"
REGION 1448..1453
/note="Oligomerization"
/evidence="ECO:0000250|UniProtKB:P03300"
ACT_SITE 898
/note="For protease 2A activity"
/evidence="ECO:0000250|UniProtKB:P03300"
ACT_SITE 916
/note="For protease 2A activity"
/evidence="ECO:0000250|UniProtKB:P03300"
ACT_SITE 987
/note="For protease 2A activity"
/evidence="ECO:0000250|UniProtKB:P03300"
ACT_SITE 1602
/note="For protease 3C activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
ACT_SITE 1633
/note="For protease 3C activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
ACT_SITE 1709
/note="For protease 3C activity"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
METAL 933
/note="Zinc; structural"
/evidence="ECO:0000250|UniProtKB:Q9QF31"
METAL 935
/note="Zinc; structural"
/evidence="ECO:0000250|UniProtKB:Q9QF31"
METAL 993
/note="Zinc; structural"
/evidence="ECO:0000250|UniProtKB:Q9QF31"
METAL 995
/note="Zinc; via pros nitrogen; structural"
/evidence="ECO:0000250|UniProtKB:Q9QF31"
METAL 1393
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 1396
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 1405
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 1410
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 1978
/note="Magnesium 1; catalytic; for RdRp activity"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 1978
/note="Magnesium 2; catalytic; for RdRp activity"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 2073
/note="Magnesium 1; catalytic; for RdRp activity"
/evidence="ECO:0000250|UniProtKB:P03300"
METAL 2073
/note="Magnesium 2; catalytic; for RdRp activity"
/evidence="ECO:0000250|UniProtKB:P03300"
SITE 69..70
/note="Cleavage; by autolysis"
/evidence="ECO:0000250|UniProtKB:P03300"
SITE 340..341
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 878..879
/note="Cleavage; by autolysis"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1027..1028
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1124..1125
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1149
/note="Involved in the interaction with host RTN3"
/evidence="ECO:0000250|UniProtKB:Q66478"
SITE 1453..1454
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1540..1541
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1562..1563
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
SITE 1745..1746
/note="Cleavage; by protease 3C"
/evidence="ECO:0000250|UniProtKB:P03301"
MOD_RES 1543
/note="O-(5'-phospho-RNA)-tyrosine"
/evidence="ECO:0000250|UniProtKB:P03300"
LIPID 2
/note="N-myristoyl glycine; by host"
/evidence="ECO:0000250|UniProtKB:P03300"
VARIANT 431
/note="S -> F (in strain: P3/Leon 12a[1]b)"
VARIANT 864
/note="K -> R (in strain: P3/Leon 12a[1]b)"
VARIANT 908
/note="T -> A (in strain: P3/Leon 12a[1]b)"
STRAND 4..8
/evidence="ECO:0007829|PDB:1PVC"
STRAND 25..29
/evidence="ECO:0007829|PDB:1PVC"
HELIX 36..38
/evidence="ECO:0007829|PDB:1PVC"
HELIX 51..54
/evidence="ECO:0007829|PDB:1PVC"
STRAND 57..59
/evidence="ECO:0007829|PDB:1PVC"
STRAND 83..87
/evidence="ECO:0007829|PDB:1PVC"
STRAND 90..96
/evidence="ECO:0007829|PDB:1PVC"
HELIX 103..105
/evidence="ECO:0007829|PDB:1PVC"
TURN 113..115
/evidence="ECO:0007829|PDB:1PVC"
HELIX 126..128
/evidence="ECO:0007829|PDB:1PVC"
STRAND 138..141
/evidence="ECO:0007829|PDB:1PVC"
STRAND 147..151
/evidence="ECO:0007829|PDB:1PVC"
HELIX 153..155
/evidence="ECO:0007829|PDB:1PVC"
HELIX 159..167
/evidence="ECO:0007829|PDB:1PVC"
STRAND 168..180
/evidence="ECO:0007829|PDB:1PVC"
STRAND 187..197
/evidence="ECO:0007829|PDB:1PVC"
STRAND 203..207
/evidence="ECO:0007829|PDB:1PVC"
HELIX 213..216
/evidence="ECO:0007829|PDB:1PVC"
HELIX 219..221
/evidence="ECO:0007829|PDB:1PVC"
STRAND 226..228
/evidence="ECO:0007829|PDB:1PVC"
HELIX 246..248
/evidence="ECO:0007829|PDB:1PVC"
TURN 249..252
/evidence="ECO:0007829|PDB:1PVC"
HELIX 255..260
/evidence="ECO:0007829|PDB:1PVC"
STRAND 261..267
/evidence="ECO:0007829|PDB:1PVC"
TURN 268..270
/evidence="ECO:0007829|PDB:1PVC"
STRAND 272..278
/evidence="ECO:0007829|PDB:1PVC"
STRAND 282..287
/evidence="ECO:0007829|PDB:1PVC"
TURN 289..291
/evidence="ECO:0007829|PDB:1PVC"
STRAND 295..307
/evidence="ECO:0007829|PDB:1PVC"
STRAND 314..331
/evidence="ECO:0007829|PDB:1PVC"
TURN 348..351
/evidence="ECO:0007829|PDB:1PVC"
STRAND 363..365
/evidence="ECO:0007829|PDB:1PVC"
STRAND 379..382
/evidence="ECO:0007829|PDB:1PVC"
HELIX 384..387
/evidence="ECO:0007829|PDB:1PVC"
TURN 399..403
/evidence="ECO:0007829|PDB:1PVC"
HELIX 405..408
/evidence="ECO:0007829|PDB:1PVC"
STRAND 410..413
/evidence="ECO:0007829|PDB:1PVC"
STRAND 422..427
/evidence="ECO:0007829|PDB:1PVC"
TURN 429..431
/evidence="ECO:0007829|PDB:1PVC"
TURN 433..437
/evidence="ECO:0007829|PDB:1PVC"
HELIX 439..444
/evidence="ECO:0007829|PDB:1PVC"
STRAND 447..452
/evidence="ECO:0007829|PDB:1PVC"
STRAND 454..460
/evidence="ECO:0007829|PDB:1PVC"
STRAND 469..475
/evidence="ECO:0007829|PDB:1PVC"
STRAND 477..479
/evidence="ECO:0007829|PDB:1PVC"
HELIX 485..488
/evidence="ECO:0007829|PDB:1PVC"
STRAND 491..497
/evidence="ECO:0007829|PDB:1PVC"
STRAND 499..501
/evidence="ECO:0007829|PDB:1PVC"
STRAND 503..508
/evidence="ECO:0007829|PDB:1PVC"
STRAND 513..520
/evidence="ECO:0007829|PDB:1PVC"
HELIX 523..525
/evidence="ECO:0007829|PDB:1PVC"
STRAND 529..536
/evidence="ECO:0007829|PDB:1PVC"
STRAND 546..556
/evidence="ECO:0007829|PDB:1PVC"
STRAND 561..565
/evidence="ECO:0007829|PDB:1PVC"
HELIX 623..625
/evidence="ECO:0007829|PDB:1PVC"
HELIX 633..635
/evidence="ECO:0007829|PDB:1PVC"
HELIX 649..651
/evidence="ECO:0007829|PDB:1PVC"
HELIX 653..657
/evidence="ECO:0007829|PDB:1PVC"
STRAND 661..671
/evidence="ECO:0007829|PDB:1PVC"
STRAND 675..677
/evidence="ECO:0007829|PDB:1VBB"
STRAND 680..685
/evidence="ECO:0007829|PDB:1PVC"
STRAND 690..692
/evidence="ECO:0007829|PDB:1PVC"
HELIX 693..698
/evidence="ECO:0007829|PDB:1PVC"
STRAND 701..718
/evidence="ECO:0007829|PDB:1PVC"
STRAND 730..736
/evidence="ECO:0007829|PDB:1PVC"
HELIX 749..752
/evidence="ECO:0007829|PDB:1PVC"
STRAND 754..756
/evidence="ECO:0007829|PDB:1PVC"
STRAND 758..762
/evidence="ECO:0007829|PDB:1PVC"
STRAND 768..772
/evidence="ECO:0007829|PDB:1PVC"
STRAND 777..783
/evidence="ECO:0007829|PDB:1PVC"
TURN 799..802
/evidence="ECO:0007829|PDB:1PVC"
STRAND 810..812
/evidence="ECO:0007829|PDB:1VBC"
STRAND 816..821
/evidence="ECO:0007829|PDB:1PVC"
STRAND 830..848
/evidence="ECO:0007829|PDB:1PVC"
STRAND 858..861
/evidence="ECO:0007829|PDB:1PVC"
SEQUENCE 2206 AA; 246165 MW; 4766B15C861F66D3 CRC64;
MGAQVSSQKV GAHENSNRAY GGSTINYTTI NYYKDSASNA ASKQDYSQDP SKFTEPLKDV
LIKTAPALNS PNVEACGYSD RVLQLTLGNS TITTQEAANS VVAYGRWPEF IRDDEANPVD
QPTEPDVATC RFYTLDTVMW GKESKGWWWK LPDALRDMGL FGQNMYYHYL GRSGYTVHVQ
CNASKFHQGA LGVFAIPEYC LAGDSDKQRY TSYANANPGE RGGKFYSQFN KDNAVTSPKR
EFCPVDYLLG CGVLLGNAFV YPHQIINLRT NNSATIVLPY VNALAIDSMV KHNNWGIAIL
PLSPLDFAQD SSVEIPITVT IAPMCSEFNG LRNVTAPKFQ GLPVLNTPGS NQYLTSDNHQ
SPCAIPEFDV TPPIDIPGEV KNMMELAEID TMIPLNLEST KRNTMDMYRV TLSDSADLSQ
PILCLSLSPA SDPRLSHTML GEVLNYYTHW AGSLKFTFLF CGSMMATGKI LVAYAPPGAQ
PPTSRKEAML GTHVIWDLGL QSSCTMVVPW ISNVTYRQTT QDSFTEGGYI SMFYQTRIVV
PLSTPKSMSM LGFVSACNDF SVRLLRDTTH ISQSALPQGI EDLISEVAQG ALTLSLPKQQ
DSLPDTKASG PAHSKEVPAL TAVETGATNP LAPSDTVQTR HVVQRRSRSE STIESFFARG
ACVAIIEVDN EQPTTRAQKL FAMWRITYKD TVQLRRKLEF FTYSRFDMEF TFVVTANFTN
ANNGHALNQV YQIMYIPPGA PTPKSWDDYT WQTSSNPSIF YTYGAAPARI SVPYVGLANA
YSHFYDGFAK VPLKTDANDQ IGDSLYSAMT VDDFGVLAVR VVNDHNPTKV TSKVRIYMKP
KHVRVWCPRP PRAVPYYGPG VDYKNNLDPL SEKGLTTYGF GHQNKAVYTA GYKICNYHLA
TKEDLQNTVS IMWNRDLLVV ESKAQGTDSI ARCNCNAGVY YCESRRKYYP VSFVGPTFQY
MEANDYYPAR YQSHMLIGHG FASPGDCGGI LRCQHGVIGI VTAGGEGLVA FSDIRDLYAY
EEEAMEQGIS NYIESLGAAF GSGFTQQIGD KISELTSMVT STITEKLLKN LIKIISSLVI
ITRNYEDTTT VLATLALLGC DVSPWQWLKK KACDTLEIPY VIRQGDSWLK KFTEACNAAK
GLEWVSNKIS KFIDWLRERI IPQARDKLEF VTKLKQLEML ENQISTIHQS CPSQEHQEIL
FNNVRWLSIQ SKRFAPLYAL EAKRIQKLEH TINNYIQFKS KHRIEPVCLL VHGSPGTGKS
VATNLIARAI AEKENTSTYS LPPDPSHFDG YKQQGVVIMD DLNQNPDGAD MKLFCQMVST
VEFIPPMASL EEKGILFTSN YVLASTNSSR ITPPTVAHSD ALARRFAFDM DIQVMGEYSR
DGKLNMAMAT ETCKDCHQPA NFKRCCPLVC GKAIQLMDKS SRVRYSVDQI TTMIINERNR
RSNIGNCMEA LFQGPLQYKD LKIDIKTRPP PECINDLLQA VDSQEVRDYC EKKGWIVNIT
SQVQTERNIN RAMTILQAVT TFAAVAGVVY VMYKLFAGHQ GAYTGLPNKR PNVPTIRAAK
VQGPGFDYAV AMAKRNIVTA TTSKGEFTML GVHDNVAILP THASPGESIV IDGKEVEILD
AKALEDQAGT NLEITIITLK RNEKFRDIRQ HIPTQITETN DGVLIVNTSK YPNMYVPVGA
VTEQGYLNLG GRQTARILMY NFPTRAGQCG GVITCTGKVI GMHVGGNGSH GFAAALKRSY
FTQSQGEIQW MRPSKEAGYP IINAPTKTKL EPSAFHYVFE GVKEPAVLTK NDPRLKTDFE
EAIFSKYVGN KITEVDEYMK EAVDHYAGQL MSLDISTEQM CLEDAMYGTD GLEALDLSTS
AGYPYVAMGK KKRDILNKQT RDTKEMQRLL DAYGINLPLV TYVKDELRSK TKVEQGKSRL
IEASSLNDSV AMRMAFGNLY AAFHRNPGVV TGSAVGCDPD LFWSKIPVLM EEKLFAFDYT
GYDASLSPAW FEALKMVLEK IGFGDRVDYI DYLNHSHHLY KNKIYCVKGG MPSGCSGTSI
FNSMINNLII RTLLLKTYKG IDLDHLKMIA YGDDVIASYP HEVDASLLAQ SGKDYGLTMT
PADKSATFET VTWENVTFLK RFFRADEKYP FLIHPVMPMK EIHESIRWTK DPRNTQDHVR
SLCLLAWHNG EEEYNKFLAK IRSVPIGRAL LLPEYSTLYR RWLDSF


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SCH-OBT0882 MOUSE ANTI ROTAVIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity ROTAVIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2, Applications E, WB 0.1 mg
OBT0882 MOUSE ANTI ROTAVIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity ROTAVIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG2, Applications E, WB 0.1 mg
MCA2830 MOUSE ANTI RUBELLA VIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity RUBELLA VIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Application 0.2 mg
SCH-MCA2830 MOUSE ANTI RUBELLA VIRUS CAPSID PROTEIN, Product Type Monoclonal Antibody, Specificity RUBELLA VIRUS CAPSID PROTEIN, Target Species Viral, Host Mouse, Format Purified, Isotypes IgG1, Application 0.2 mg
orb81775 Rubella Virus Capsid C protein The E.coli derived recombinant protein contains the Rubella Virus Capsid regions, 1-123 amino acids. For research use only. 100
EIAAB43299 HIV-1 Nef-interacting protein,Homo sapiens,Human,hVAN,KIAA0113,Naf1,NAF1,Nef-associated factor 1,Nip40-1,TNFAIP3-interacting protein 1,TNIP1,VAN,Virion-associated nuclear shuttling protein
EIAAB35745 A34.5,Anti-sense to ERCC-1 protein,Ase1,ASE-1,Cd3eap,CD3E-associated protein,CD3-epsilon-associated protein,DNA-directed RNA polymerase I subunit RPA34,Mouse,Mus musculus,Paf49,RNA polymerase I-associ
EIAAB43298 A20-binding inhibitor of NF-kappa-B activation,ABIN,Abin,Mouse,Mus musculus,mVAN,Naf1,Naf1,Nef-associated factor 1,TNFAIP3-interacting protein 1,Tnip1,VAN,Virion-associated nuclear shuttling protein
AB2A241 Polyclonal Antibodies: Anti- Capsid protein VP1(N-terminal) Polyclonal Antibody; Specificity: Anti- Capsid protein VP1(N-terminal) Polyclonal Antibody ; Application: IHC 0.1mg
PAH-G1-2 Protein Arrays containing 234 Human Protein for simultaneous detection of Protein function, including Protein-protein interaction, Protein modification, antibody specificity, auto-antibody and small m 1 glass slide with 2 sub-arrays
29-844 RNF40 contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the 0.1 mg
29-850 The protein contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions.The protein encoded by this 0.1 mg
orb81838 Rubella RSVP (TM) Antigen (HPV77) protein Rubella RSVP (TM) (Strain HPV77) >90 percent Viral Protein, Capsid-Free is an infectious disease antigen_toxin. For research use only. 1 mg
EIAAB35746 A34.5,Antisense to ERCC-1 protein,ASE1,ASE-1,CAST,CAST,CD3EAP,CD3E-associated protein,CD3-epsilon-associated protein,DNA-directed RNA polymerase I subunit RPA34,Homo sapiens,Human,PAF49,RNA polymerase
EIAAB44668 Dap12,DNAX-activation protein 12,Karap,KAR-associated protein,Killer-activating receptor-associated protein,Mouse,Mus musculus,TYRO protein tyrosine kinase-binding protein,Tyrobp
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3
EIAAB44667 DAP12,DNAX-activation protein 12,Homo sapiens,Human,KARAP,KAR-associated protein,Killer-activating receptor-associated protein,TYRO protein tyrosine kinase-binding protein,TYROBP
18-003-43520 HSPB1-associated protein 1 - 27 KdA heat shock protein-associated protein 1; Protein associated with small stress protein 1 Polyclonal 0.05 mg Aff Pur
AB2A242 Polyclonal Antibodies: Anti-Capsid protein VP1(Middle residues) Polyclonal Antibody; Specificity: Anti-Capsid protein VP1(Middle residues) Polyclonal Antibody ; Application: IHC 0.1mg
EIAAB25665 AML1T1,CBFA2T1,CDR,Cyclin-D-related protein,Eight twenty one protein,ETO,Homo sapiens,Human,MTG8,Protein CBFA2T1,Protein ETO,Protein MTG8,RUNX1T1,Zinc finger MYND domain-containing protein 2,ZMYND2
EIAAB46018 C6orf55,Dopamine-responsive gene 1 protein,DRG-1,Homo sapiens,HSPC228,Human,LIP5,LYST-interacting protein 5,My012,SBP1,SKD1-binding protein 1,Vacuolar protein sorting-associated protein VTA1 homolog,V
orb82441 Rubella Virus Capsid, recombinant protein Rubella Capsid (C), Recombinant is an infectious disease antigen_toxin. For research use only. 1 mg
18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
EIAAB45903 ERVK6,HERV-K(C7) Pro protein,HERV-K(HML-2.HOM) Pro protein,HERV-K_7p22.1 provirus ancestral Pro protein,HERV-K108 Pro protein,Homo sapiens,Human,PR,Protease,Proteinase
U1773h CLIA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
Pathways :
WP1663: Homologous recombination
WP1694: Pyrimidine metabolism
WP2199: Seed Development
WP1672: Mismatch repair
WP1693: Purine metabolism
WP1438: Influenza A virus infection
WP1644: DNA replication
WP1049: G Protein Signaling Pathways
WP1657: Glycerolipid metabolism
WP2203: TSLP Signaling Pathway
WP2292: Chemokine signaling pathway
WP1371: G Protein Signaling Pathways
WP1714: Tyrosine metabolism
WP1502: Mitochondrial biogenesis
WP1892: Protein folding
WP1673: Naphthalene and anthracene degradation
WP2371: Parkinsons Disease Pathway
WP1678: Nucleotide excision repair
WP1613: 1,4-Dichlorobenzene degradation
WP1909: Signal regulatory protein (SIRP) family interactions
WP1625: Base excision repair
WP210: Cytoplasmic Ribosomal Proteins
WP1690: Propanoate metabolism
WP73: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways

Related Genes :

Bibliography :
[30443749] Structural disorder in the proteome and interactome of Alkhurma virus (ALKV).
[29541253] Toll-like receptor 9 activation by CpG oligodeoxynucleotide 7909 enhances the radiosensitivity of A549 lung cancer cells via the p53 signaling pathway.
[27273223] First isolation of West Nile virus from a dromedary camel.
[18807167] Role of genetic recombination in the molecular architecture of Papaya ringspot virus.
[14698672] An adenine-to-guanine nucleotide change in the IRES SL-IV domain of picornavirus/hepatitis C chimeric viruses leads to a nonviable phenotype.
[7503676] Evaluation of complete genome sequences and sequences of individual gene products for the classification of hepatitis C viruses.