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Database: UniProt
Entry: G3E5I3_HBV
LinkDB: G3E5I3_HBV
Original site: G3E5I3_HBV 
ID   G3E5I3_HBV              Unreviewed;       212 AA.
AC   G3E5I3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   22-FEB-2023, entry version 47.
DE   RecName: Full=Capsid protein {ECO:0000256|HAMAP-Rule:MF_04076};
DE   AltName: Full=Core antigen {ECO:0000256|HAMAP-Rule:MF_04076};
DE   AltName: Full=Core protein {ECO:0000256|HAMAP-Rule:MF_04076};
DE   AltName: Full=HBcAg {ECO:0000256|HAMAP-Rule:MF_04076};
DE   AltName: Full=p21.5 {ECO:0000256|HAMAP-Rule:MF_04076};
GN   Name=C {ECO:0000256|HAMAP-Rule:MF_04076,
GN   ECO:0000256|RuleBase:RU361253, ECO:0000313|EMBL:AEO21589.1};
OS   Hepatitis B virus (HBV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX   NCBI_TaxID=10407 {ECO:0000313|EMBL:AEO21589.1, ECO:0000313|Proteomes:UP000152560};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN   [1] {ECO:0000313|EMBL:AEO21589.1, ECO:0000313|Proteomes:UP000152560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nin-2008 {ECO:0000313|EMBL:AEO21589.1};
RA   Sa-Nguanmoo P., Ratanakorn P., Tatematsu K., Naganuma H., Payungporn S.,
RA   Sommanustweechai A., Tanaka Y., Mizokami M., Poovorawan Y.;
RT   "Cross-species transmission of gibbon and orangutan hepatitis B virus to
RT   transgenic severe combined immunodeficiency mice with human hepatocytes.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May regulate immune response to the intracellular capsid in
CC       acting as a T-cell tolerogen, by having an immunoregulatory effect
CC       which prevents destruction of infected cells by cytotoxic T-cells.
CC       {ECO:0000256|RuleBase:RU361253}.
CC   -!- FUNCTION: Self assembles to form an icosahedral capsid. Most capsids
CC       appear to be large particles with an icosahedral symmetry of T=4 and
CC       consist of 240 copies of capsid protein, though a fraction forms
CC       smaller T=3 particles consisting of 180 capsid proteins. Entering
CC       capsids are transported along microtubules to the nucleus.
CC       Phosphorylation of the capsid is thought to induce exposure of nuclear
CC       localization signal in the C-terminal portion of the capsid protein
CC       that allows binding to the nuclear pore complex via the importin
CC       (karyopherin-) alpha and beta. Capsids are imported in intact form
CC       through the nuclear pore into the nuclear basket, where it probably
CC       binds NUP153. Only capsids that contain the mature viral genome can
CC       release the viral DNA and capsid protein into the nucleoplasm. Immature
CC       capsids get stuck in the basket. Capsids encapsulate the pre-genomic
CC       RNA and the P protein. Pre-genomic RNA is reverse-transcribed into DNA
CC       while the capsid is still in the cytoplasm. The capsid can then either
CC       be directed to the nucleus, providing more genomes for transcription,
CC       or bud through the endoplasmic reticulum to provide new virions.
CC       {ECO:0000256|HAMAP-Rule:MF_04076}.
CC   -!- SUBUNIT: Homodimerizes, then multimerizes. Interacts with cytosol
CC       exposed regions of viral L glycoprotein present in the reticulum-to-
CC       Golgi compartment. Interacts with human FLNB. Phosphorylated form
CC       interacts with host importin alpha; this interaction depends on the
CC       exposure of the NLS, which itself depends upon genome maturation and/or
CC       phosphorylation of the capsid protein. Interacts with host NUP153.
CC       {ECO:0000256|HAMAP-Rule:MF_04076}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361253}. Virion
CC       {ECO:0000256|HAMAP-Rule:MF_04076}. Host cytoplasm {ECO:0000256|HAMAP-
CC       Rule:MF_04076}.
CC   -!- PTM: Cleaved by host furin. {ECO:0000256|RuleBase:RU361253}.
CC   -!- PTM: Phosphorylated by host SRPK1, SRPK2, and maybe protein kinase C or
CC       GAPDH. Phosphorylation is critical for pregenomic RNA packaging.
CC       Protein kinase C phosphorylation is stimulated by HBx protein and may
CC       play a role in transport of the viral genome to the nucleus at the late
CC       step during the viral replication cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_04076}.
CC   -!- SIMILARITY: Belongs to the orthohepadnavirus core antigen family.
CC       {ECO:0000256|HAMAP-Rule:MF_04076}.
CC   -!- SIMILARITY: Belongs to the orthohepadnavirus precore antigen family.
CC       {ECO:0000256|RuleBase:RU361253}.
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DR   EMBL; HQ603078; AEO21589.1; -; Genomic_DNA.
DR   Proteomes; UP000152560; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0019049; P:mitigation of host antiviral defense response; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR   GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.4090.10; Viral capsid, core domain supefamily, Hepatitis B virus; 1.
DR   HAMAP; MF_04076; HBV_HBEAG; 1.
DR   InterPro; IPR013195; Hepatitis_B_virus_capsid_N.
DR   InterPro; IPR002006; Hepatitis_core.
DR   InterPro; IPR036459; Viral_capsid_core_dom_sf_HBV.
DR   Pfam; PF08290; Hep_core_N; 1.
DR   Pfam; PF00906; Hepatitis_core; 3.
DR   SUPFAM; SSF47852; Hepatitis B viral capsid (hbcag); 1.
PE   3: Inferred from homology;
KW   Capsid protein {ECO:0000256|HAMAP-Rule:MF_04076};
KW   Cytoplasmic inwards viral transport {ECO:0000256|HAMAP-Rule:MF_04076};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_04076};
KW   Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04076};
KW   Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04076,
KW   ECO:0000256|RuleBase:RU361253};
KW   Microtubular inwards viral transport {ECO:0000256|HAMAP-Rule:MF_04076};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_04076};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_04076};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_04076};
KW   T=4 icosahedral capsid protein {ECO:0000256|HAMAP-Rule:MF_04076};
KW   Viral immunoevasion {ECO:0000256|RuleBase:RU361253};
KW   Viral penetration into host nucleus {ECO:0000256|HAMAP-Rule:MF_04076};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04076};
KW   Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04076}.
FT   DOMAIN          1..27
FT                   /note="Hepatitis B virus capsid N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08290"
FT   REGION          165..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..212
FT                   /note="RNA binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT   MOTIF           187..204
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT   COMPBIAS        181..202
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         184
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT   MOD_RES         191
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT   MOD_RES         199
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
SQ   SEQUENCE   212 AA;  24062 MW;  796F63A76D522EF0 CRC64;
     MQLFHLCLII SCSCPTVQAS KLCLGWLLGM DIDPYKEFGA SVELLSFLPS DFFPSVTDLL
     DTASALYREA LESPEHCSPN HTALRQAILC WGELMSLASW VGNNLEDPAS RELVVNYVNT
     NMGLKIRQLL WFHISCLTFG RETVLEYLVS FGVWIRTPPA YRPPNAPILS TLPETTVVRR
     RGRSPRRRTP SPRRRRSQSP RRRRSQSPAS QC
//
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