ID K7QJE2_HBV Unreviewed; 214 AA.
AC K7QJE2;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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:AFU54726.1};
OS Hepatitis B virus (HBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10407 {ECO:0000313|EMBL:AFU54726.1, ECO:0000313|Proteomes:UP000104564};
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:AFU54726.1, ECO:0000313|Proteomes:UP000104564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1160 {ECO:0000313|EMBL:AFU54726.1};
RX PubMed=23092209;
RA Alvarado-Mora M.V., Romano C.M., Gomes-Gouvea M.S., Gutierrez M.F.,
RA Carrilho F.J., R Pinho J.R.;
RT "Phylogenetic analysis of complete genome sequences of hepatitis B virus
RT from an Afro-Colombian community: presence of HBV F3/A1 recombinant
RT strain.";
RL Virol. J. 9:244-244(2012).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQ023660; AFU54726.1; -; Genomic_DNA.
DR Proteomes; UP000104564; 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:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0019049; P:virus-mediated perturbation of host defense response; IEA:UniProtKB-KW.
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; 2.
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..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..214
FT /note="RNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT MOTIF 189..206
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT COMPBIAS 182..204
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT MOD_RES 193
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT MOD_RES 201
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
SQ SEQUENCE 214 AA; 24722 MW; 2B584E6385678132 CRC64;
MQLFHLCLII SCTCPTFQAS KLCLGWLWGM DIDPYKEFGA TVELLSFLPS DFFPSVRDLL
DTASALYRED LESPEHCSPH HTALRQAILC WGELMTLATW VGNNLEDPAS RDLVVNYVNT
NMGLKIRQLL WFHISCLTFG RETVLEYLVS FGVWIRTPPA YRPPKAPILS TLPETTVVRR
RDRGKSPRRR TPSPRRRRSQ SPRRRRSQSR ESQC
//
