POLG_HAVSJ
ID POLG_HAVSJ Reviewed; 56 AA.
AC P0C5S8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Capsid protein VP1-2A;
DE AltName: Full=VPX;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=Assembly signal 2A;
DE AltName: Full=pX {ECO:0000250|UniProtKB:P08617};
DE Flags: Fragment;
OS Simian hepatitis A virus genotype VI (isolate JM55) (SHAV) (Simian
OS hepatitis A virus (isolate Macaca/Indonesia/JM55/1985)).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Hepatovirus.
OX NCBI_TaxID=470594;
OH NCBI_TaxID=9481; Callithrix.
OH NCBI_TaxID=9536; Cercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey).
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9539; Macaca (macaques).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1318940; DOI=10.1099/0022-1317-73-6-1365;
RA Robertson B.H., Jansen R.W., Khanna B., Totsuka A., Nainan O.V., Siegl G.,
RA Widell A., Margolis H.S., Isomura S., Ito K., Ishizu T., Moritsugu Y.,
RA Lemon S.M.;
RT "Genetic relatedness of hepatitis A virus strains recovered from different
RT geographical regions.";
RL J. Gen. Virol. 73:1365-1377(1992).
CC -!- FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form
CC a closed capsid enclosing the viral positive strand RNA genome. All
CC these proteins contain a beta-sheet structure called beta-barrel jelly
CC roll. Together they form an icosahedral capsid (T=3) composed of 60
CC copies of each VP1, VP2, and VP3, with a diameter of approximately 300
CC Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3
CC are located at the quasi-sixfold axes. The naked capsid interacts with
CC the host receptor HAVCR1 to provide virion attachment to and probably
CC entry into the target cell. {ECO:0000250|UniProtKB:P08617}.
CC -!- FUNCTION: [Capsid protein VP1-2A]: Precursor component of immature
CC procapsids that corresponds to an extended form of the structural
CC protein VP1. After maturation, possibly by the host Cathepsin L, the
CC assembly signal 2A is cleaved to give rise to the mature VP1 protein.
CC {ECO:0000250|UniProtKB:P08617}.
CC -!- SUBUNIT: [Capsid protein VP1-2A]: Homopentamer. Homooligomer.
CC {ECO:0000250|UniProtKB:P08617}.
CC -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP2.
CC Interacts with capsid protein VP3. {ECO:0000250|UniProtKB:P08617}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body
CC {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions
CC occurs through an exosome-like mechanism involving endosomal budding of
CC viral capsids into multivesicular bodies.
CC {ECO:0000250|UniProtKB:P08617}.
CC -!- DOMAIN: [Capsid protein VP1-2A]: The assembly signal 2A region mediates
CC pentamerization of P1-2A. {ECO:0000250|UniProtKB:P08617}.
CC -!- DOMAIN: [Genome polyprotein]: Late-budding domains (L domains) are
CC short sequence motifs essential for viral particle budding. They
CC recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex
CC Required for Transport) or ESCRT-associated proteins. The genome
CC polyprotein contains two L domains: a tandem of (L)YPX(n)L domain which
CC is known to bind the PDCD6IP/ALIX adaptater protein.
CC {ECO:0000250|UniProtKB:P08617}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral
CC protease in vivo yield a variety of precursors and mature proteins.
CC Polyprotein processing intermediates are produced, such as P1-2A which
CC is a functional precursor of the structural proteins, VP0 which is a
CC VP4-VP2 precursor, VP1-2A precursor, 3ABC precursor which is a stable
CC and catalytically active precursor of 3A, 3B and 3C proteins, 3AB and
CC 3CD precursors. The assembly signal 2A is removed from VP1-2A by a host
CC protease, possibly host Cathepsin L. This cleavage occurs over a region
CC of 3 amino-acids probably generating VP1 proteins with heterogeneous C-
CC termini. {ECO:0000250|UniProtKB:P08617}.
CC -!- PTM: [Capsid protein VP1-2A]: The assembly signal 2A is removed from
CC VP1-2A by a host protease, possibly host Cathepsin L in naked virions.
CC This cleavage does not occur in enveloped virions. This cleavage occurs
CC over a region of 3 amino-acids probably generating VP1 proteins with
CC heterogeneous C-termini. {ECO:0000250|UniProtKB:P08617}.
CC -!- MISCELLANEOUS: [Genome polyprotein]: The need for an intact eIF4G
CC factor for the initiation of translation of HAV results in an inability
CC to shut off host protein synthesis by a mechanism similar to that of
CC other picornaviruses. {ECO:0000250|UniProtKB:P08617}.
CC -!- MISCELLANEOUS: [Genome polyprotein]: During infection, enveloped
CC virions (eHAV) are released from cells. These eHAV are cloaked in host-
CC derived membranes and resemble exosomes. The membrane of eHAV is devoid
CC of viral proteins and thus prevents their neutralization by antibodies.
CC eHAV budding is dependent on ESCRT-associated proteins VPS4B and
CC PDCD6IP/ALIX. eHAV are produced and released in the serum and plasma,
CC but not in bile and feces which only contain the naked, nonenveloped
CC virions. It is likely that eHAV also use HAVCR1 as a functional
CC receptor to infect cells, an evolutionary trait that may enhance HAV
CC infectivity. {ECO:0000250|UniProtKB:P08617}.
CC -!- SIMILARITY: Belongs to the picornaviridae polyprotein family.
CC {ECO:0000305}.
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DR EMBL; L07731; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0C5S8; -.
DR GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Capsid protein; Host endosome; Host-virus interaction; Ion channel;
KW Ion transport; T=pseudo3 icosahedral capsid protein; Transport;
KW Viral attachment to host cell; Viral ion channel; Virion;
KW Virus entry into host cell.
FT CHAIN <1..>56
FT /note="Capsid protein VP1-2A"
FT /id="PRO_0000445069"
FT CHAIN <1..>56
FT /note="Genome polyprotein"
FT /id="PRO_0000455812"
FT CHAIN <1..2
FT /note="Capsid protein VP1"
FT /id="PRO_0000314779"
FT CHAIN 3..>56
FT /note="Assembly signal 2A"
FT /id="PRO_0000310691"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 2..3
FT /note="Cleavage; partial; by host"
FT /evidence="ECO:0000250|UniProtKB:P08617"
FT SITE 6
FT /note="Important for VP1 folding and capsid assembly"
FT /evidence="ECO:0000250|UniProtKB:P08617"
FT NON_TER 1
FT NON_TER 56
SQ SEQUENCE 56 AA; 6485 MW; C693DB4D101EF285 CRC64;
ETMLDRIASG DLESSVDDPR SAEDKRFESH IEQGKPYKEL RMEVGKQTLK YAQEEL
