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Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Protein VP2 (P1B) (Virion protein 2); Protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (PX); Protein VP1 (P1D) (Virion protein 1); Protein 2A; Protein 2B; Protein 2BC] (Fragment)

 POLG_HAVSC              Reviewed;         839 AA.
P31788;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
12-SEP-2018, entry version 87.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=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=Protein VP1-2A;
AltName: Full=VPX;
Contains:
RecName: Full=Capsid protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Assembly signal 2A;
AltName: Full=pX {ECO:0000250|UniProtKB:P08617};
Contains:
RecName: Full=Protein 2BC;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Flags: Fragment;
Simian hepatitis A virus genotype IV (isolate CY-145) (SHAV) (Simian
hepatitis A virus (isolate Macaca/Philippines/CY-145/1988)).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Hepatovirus.
NCBI_TaxID=31707;
NCBI_TaxID=9481; Callithrix.
NCBI_TaxID=9536; Cercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey).
NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
NCBI_TaxID=9539; Macaca (macaques).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1649902; DOI=10.1099/0022-1317-72-7-1685;
Nainan O.V., Margolis H.S., Robertson B.H., Balayan M., Brinton M.A.;
"Sequence analysis of a new hepatitis A virus naturally infecting
cynomolgus macaques (Macaca fascicularis).";
J. Gen. Virol. 72:1685-1689(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 764-818.
PubMed=1318940; DOI=10.1099/0022-1317-73-6-1365;
Robertson B.H., Jansen R.W., Khanna B., Totsuka A., Nainan O.V.,
Siegl G., Widell A., Margolis H.S., Isomura S., Ito K., Ishizu T.,
Moritsugu Y., Lemon S.M.;
"Genetic relatedness of hepatitis A virus strains recovered from
different geographical regions.";
J. Gen. Virol. 73:1365-1377(1992).
-!- FUNCTION: Capsid protein VP1: Capsid proteins VP1, VP2, and VP3
form a closed capsid enclosing the viral positive strand RNA
genome. All these 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 naked capsid interacts with the host receptor
HAVCR1 to provide virion attachment to and probably entry into the
target cell. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Capsid protein VP2: Capsid proteins VP1, VP2, and VP3
form a closed capsid enclosing the viral positive strand RNA
genome. All these 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 naked capsid interacts with the host receptor
HAVCR1 to provide virion attachment to and probably entry into the
target cell. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Capsid protein VP3: Capsid proteins VP1, VP2, and VP3
form a closed capsid enclosing the viral positive strand RNA
genome. All these 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 naked capsid interacts with the host receptor
HAVCR1 to provide virion attachment to and probably entry into the
target cell. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein VP0: VP0 precursor is a component of the
immature procapsids. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein VP4: Plays a role in the assembly of the 12
pentamers into an icosahedral structure. Has not been detected in
mature virions, supposedly owing to its small size.
{ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein VP1-2A: Precursor component of immature
procapsids that corresponds to an extended form of the structural
protein VP1. After maturation, possibly by the host Cathepsin L,
the assembly signal 2A is cleaved to give rise to the mature VP1
protein. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein 2BC: Affects membrane integrity and causes an
increase in membrane permeability. {ECO:0000250|UniProtKB:P08617}.
-!- FUNCTION: Protein 2B: Function as a viroporin. Affects membrane
integrity and causes an increase in membrane permeability.
Involved in host intracellular membrane rearrangements probably to
give rise to the viral factories. Does not disrupt calcium
homeostasis or glycoprotein trafficking. Antagonizes the innate
immune response of the host by suppressing IFN-beta synthesis,
which it achieves by interfering with the DDX58/IFIH1 (RIG-I/MDA5)
pathway. {ECO:0000250|UniProtKB:P08617}.
-!- SUBUNIT: Protein 2B: Homodimer. Homomultimer; probably interacts
with membranes in a multimeric form. Seems to assemble into
amyloid-like fibers. Protein VP1-2A: Homopentamer. Protein VP1-2A:
Homooligomer. Capsid protein VP1: Interacts with capsid protein
VP2. Capsid protein VP1: Interacts with capsid protein VP3. Capsid
protein VP2: Interacts with capsid protein VP1. Capsid protein
VP2: Interacts with capsid protein VP3. Capsid protein VP3:
Interacts with capsid protein VP1. Capsid protein VP3: Interacts
with capsid protein VP2. {ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion
{ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular
body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly
formed virions occurs through an exosome-like mechanism involving
endosomal budding of viral capsids into multivesicular bodies.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion
{ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular
body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly
formed virions occurs through an exosome-like mechanism involving
endosomal budding of viral capsids into multivesicular bodies.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Capsid protein VP1: Virion
{ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular
body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly
formed virions occurs through an exosome-like mechanism involving
endosomal budding of viral capsids into multivesicular bodies.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Protein VP4: Virion
{ECO:0000250|UniProtKB:P08617}. Note=Present in the full mature
virion. The egress of newly formed virions occurs through an
exosome-like mechanism involving endosomal budding of viral
capsids into multivesicular bodies.
{ECO:0000250|UniProtKB:P08617}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host membrane
{ECO:0000250|UniProtKB:P08617}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P08617}. Note=Probably localizes to
intracellular membrane vesicles that are induced after virus
infection as the site for viral RNA replication.
{ECO:0000250|UniProtKB:P08617}.
-!- DOMAIN: Protein VP1-2A: The assembly signal 2A region mediates
pentamerization of P1-2A. {ECO:0000250|UniProtKB:P08617}.
-!- DOMAIN: Genome polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle budding. They
recruit proteins of the host ESCRT machinery (Endosomal Sorting
Complex Required for Transport) or ESCRT-associated proteins. The
genome polyprotein contains two L domains: a tandem of (L)YPX(n)L
domain which is known to bind the PDCD6IP/ALIX adaptater protein.
{ECO:0000250|UniProtKB:P08617}.
-!- DOMAIN: Capsid protein VP2: Late-budding domains (L domains) are
short sequence motifs essential for viral particle budding. They
recruit proteins of the host ESCRT machinery (Endosomal Sorting
Complex Required for Transport) or ESCRT-associated proteins.
Capsid protein VP2 contains two L domains: a tandem of (L)YPX(n)L
domain which is known to bind the Alix adaptater protein.
{ECO:0000250|UniProtKB:P08617}.
-!- DOMAIN: Protein 2B: The C-terminus displays a membrane-penetrating
ability. {ECO:0000250|UniProtKB:P08617}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages by viral
protease in vivo yield a variety of precursors and mature
proteins. Polyprotein processing intermediates are produced, such
as P1-2A which is a functional precursor of the structural
proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC
precursor which is a stable and catalytically active precursor of
3A, 3B and 3C proteins, 3AB and 3CD precursors. The assembly
signal 2A is removed from VP1-2A by a host protease, possibly host
Cathepsin L. This cleavage occurs over a region of 3 amino-acids
probably generating VP1 proteins with heterogeneous C-termini.
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.
{ECO:0000250|UniProtKB:P08617}.
-!- PTM: Protein VP1-2A: The assembly signal 2A is removed from VP1-2A
by a host protease, possibly host Cathepsin L in nacked virions.
This cleavage does not occur in enveloped virions. This cleavage
occurs over a region of 3 amino-acids probably generating VP1
proteins with heterogeneous C-termini.
{ECO:0000250|UniProtKB:P08617}.
-!- PTM: Protein VP4: Unlike other picornaviruses, does not seem to be
myristoylated. {ECO:0000250|UniProtKB:P08617}.
-!- MISCELLANEOUS: Genome polyprotein: The need for an intact eIF4G
factor for the initiation of translation of HAV results in an
inability to shut off host protein synthesis by a mechanism
similar to that of other picornaviruses.
{ECO:0000250|UniProtKB:P08617}.
-!- MISCELLANEOUS: Genome polyprotein: During infection, enveloped
virions (eHAV) are released from cells. These eHAV are cloaked in
host-derived membranes and resemble exosomes. The membrane of eHAV
is devoid of viral proteins and thus prevents their neutralization
by antibodies. eHAV budding is dependent on ESCRT-associated
proteins VPS4B and PDCD6IP/ALIX. eHAV are produced and released in
the serum and plasma, but not in bile and feces which only contain
the naked, nonenveloped virions. It is likely that eHAV also use
HAVCR1 as a functional receptor to infect cells, an evolutionary
trait that may enhance HAV infectivity.
{ECO:0000250|UniProtKB:P08617}.
-!- SIMILARITY: Belongs to the picornaviridae polyprotein family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
{ECO:0000250|UniProtKB:P08617}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M59286; AAA45473.1; -; Genomic_RNA.
EMBL; L07732; -; NOT_ANNOTATED_CDS; Genomic_RNA.
PIR; JQ1180; GNNYS2.
ProteinModelPortal; P31788; -.
SMR; P31788; -.
PRIDE; P31788; -.
OrthoDB; VOG090000CY; -.
Proteomes; UP000007633; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 2.
Gene3D; 2.60.120.20; -; 3.
InterPro; IPR024354; Hepatitis_A_VP1-2A.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR029053; Viral_coat.
Pfam; PF12944; HAV_VP; 1.
Pfam; PF00073; Rhv; 2.
3: Inferred from homology;
Capsid protein; Complete proteome; Host endosome; Host membrane;
Host-virus interaction; Ion channel; Ion transport; Membrane;
Transport; Viral attachment to host cell; Viral ion channel; Virion;
Virus entry into host cell.
CHAIN 1 >839 Genome polyprotein.
/FTId=PRO_0000311031.
CHAIN 1 245 Protein VP0.
/FTId=PRO_0000311032.
CHAIN 1 23 Protein VP4.
/FTId=PRO_0000039990.
CHAIN 24 245 Capsid protein VP2.
/FTId=PRO_0000039991.
CHAIN 246 491 Capsid protein VP3.
/FTId=PRO_0000039992.
CHAIN 492 835 Protein VP1-2A.
/FTId=PRO_0000311033.
CHAIN 492 765 Capsid protein VP1.
/FTId=PRO_0000039993.
CHAIN 766 835 Assembly signal 2A.
/FTId=PRO_0000039994.
CHAIN 836 >839 Protein 2B.
/FTId=PRO_0000311034.
CHAIN 836 >839 Protein 2BC.
/FTId=PRO_0000311035.
REGION 766 836 Involved in P1-2A pentamerization.
{ECO:0000250|UniProtKB:P08617}.
MOTIF 167 171 (L)YPX(n)L motif.
{ECO:0000250|UniProtKB:P08617}.
MOTIF 200 205 (L)YPX(n)L motif.
{ECO:0000250|UniProtKB:P08617}.
SITE 23 24 Cleavage. {ECO:0000255}.
SITE 245 246 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
SITE 491 492 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
SITE 765 766 Cleavage; partial; by host.
{ECO:0000250|UniProtKB:P08617}.
SITE 769 769 Important for VP1 folding and capsid
assembly. {ECO:0000250|UniProtKB:P08617}.
SITE 835 836 Cleavage; by protease 3C.
{ECO:0000250|UniProtKB:P08617}.
NON_TER 839 839
SEQUENCE 839 AA; 93825 MW; 2CACC4BD1E192DBC CRC64;
MNMARQGLFQ TVGSGLDHIL SLADVEEEQM IQSVDRTAVT GASYFTSVDQ SSVHTAEVGS
HQSEPLKTSV DKPGSKKTQG EKFFLIHSAD WLSTHALFHE VAKLDVVSLL YNEQFAVQGL
LRYHTYARFG IEIQVQINPT PFQQGGLICA MVPGDQGYGS IASLTVYPHG LLNCNINNVV
RIKVPFIYTR GAYHFKDPQY PVWELTIRVW SEFNIGTGTS AYTSLNVLAR FTDLELHGLT
PLSTQMMRNE FRVSTTENVV NLSNYEDARA KMSFALDQEN WRSDPSEGGG IKITHFSTWT
SIPTLAAQFA FNASASVGQQ IKVIPVDPYF YQMTNSNPDQ KYITALASIC QMFCFWRGDL
VFDFQVFPTK YHSGRLQFCF VPGNELIEVT SITLKQATTA PCAVMDITGV QSTLRFRVPW
ISDTPYRVNC YIKSSHQKGE YTAIEKLIVY CYNRLTSPSN VASHVRVNVY LSAINLECFA
PLYHAMDVTS QTGDDSGGFS TTVSTEQNVP DPQVGITTPK DLKGKANKGK MDVSGVQAPV
GAITTIEDPV LAKKVPETFP ELKPGESRHT SDHMSVYKFM GRSHFLCTFT FNANNREYTF
PITLSSTSNP PHGSPSTLRW FFNLFQLYRG PLDLTIIITG ATDVDGMAWF TPVGLAVDTP
WVEKQSALTI DYKTALGAIR FNTRRTGNIQ IRLPWYSYLY AVSGALDGLG DTTDSTFGLV
SIQIANYNHS DEYLSFSCYL SVTEQSEFFF PRAPLNSSAM MTSENMLDRI AGGDLESSVD
DPRTDEDRRF ESHIEKKPYK ELRLEVGKQR FKYAREELSN EILPPPRKLK GLFSQSKIS


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