ID   Q9QMH8_HBV              Unreviewed;       212 AA.
AC   Q9QMH8;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 104.
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:BAA85376.1};
GN   Synonyms=preC {ECO:0000313|EMBL:BAA85376.1};
OS   Hepatitis B virus (HBV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX   NCBI_TaxID=10407 {ECO:0000313|EMBL:BAA85376.1, ECO:0000313|Proteomes:UP000115088};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN   [1] {ECO:0000313|EMBL:BAA85376.1, ECO:0000313|Proteomes:UP000115088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Genotype D {ECO:0000313|EMBL:BAA85376.1};
RX   PubMed=3171552;
RA   Okamoto H., Tsuda F., Sakugawa H., Sastrosoewignjo R.I., Imai M.,
RA   Miyakawa Y., Mayumi M.;
RT   "Typing hepatitis B virus by homology in nucleotide sequence: comparison of
RT   surface antigen subtypes.";
RL   J. Gen. Virol. 69:2575-2583(1988).
RN   [2] {ECO:0000313|EMBL:BAA85376.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Genotype D {ECO:0000313|EMBL:BAA85376.1};
RA   Turner S.L.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000100292, ECO:0000313|Proteomes:UP000119845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D_Tonga_BB6995_2000 {ECO:0000313|EMBL:AJF41506.1},
RC   D_Tonga_BQ3450_2001 {ECO:0000313|EMBL:AJF41520.1}, and
RC   D_Tonga_JF5498_2004 {ECO:0000313|EMBL:AJF41527.1};
RA   Harrison G.L.A., Moyes C., Abbott W., Pryor J., Malani J., Supuri M.,
RA   Masta A., Teriboriuk B., Toatu T., Shapiro B., Lemey P., Hurles M.,
RA   Penny D.;
RT   "Phylogeography of Hepatitis B virus in South Pacific Island Countries.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AGB97618.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=D_F109C_2004 {ECO:0000313|EMBL:AGB97618.1}, D_KI387C_2005
RC   {ECO:0000313|EMBL:AGB97895.1}, D_PNG_P043PF_2004
RC   {ECO:0000313|EMBL:AGB97795.1}, D_PNG_P054PF_2004
RC   {ECO:0000313|EMBL:AGB97802.1}, D_Samoa_Fa_1991
RC   {ECO:0000313|EMBL:AGB97645.1}, and D_Tonga_Ng_1992
RC   {ECO:0000313|EMBL:AGB97659.1};
RA   Teixeira M., Theodoro R.C., da Derengowsky L.S., Bagagli E., Felipe M.S.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|Proteomes:UP000111582, ECO:0000313|Proteomes:UP000116163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D_F109C_2004 {ECO:0000313|EMBL:AGB97618.1}, D_KI387C_2005
RC   {ECO:0000313|EMBL:AGB97895.1}, D_PNG_P043PF_2004
RC   {ECO:0000313|EMBL:AGB97795.1}, D_PNG_P054PF_2004
RC   {ECO:0000313|EMBL:AGB97802.1}, D_Samoa_Fa_1991
RC   {ECO:0000313|EMBL:AGB97645.1}, and D_Tonga_Ng_1992
RC   {ECO:0000313|EMBL:AGB97659.1};
RX   PubMed=21765983; DOI=10.3390/v3020083;
RA   Harrison A., Lemey P., Hurles M., Moyes C., Horn S., Pryor J., Malani J.,
RA   Supuri M., Masta A., Teriboriki B., Toatu T., Penny D., Rambaut A.,
RA   Shapiro B.;
RT   "Genomic analysis of hepatitis B virus reveals antigen state and genotype
RT   as sources of evolutionary rate variation.";
RL   Viruses 3:83-101(2011).
RN   [6] {ECO:0007829|PDB:3V6Z}
RP   X-RAY CRYSTALLOGRAPHY (3.34 ANGSTROMS) OF 20-178, AND DISULFIDE BONDS.
RX   PubMed=23219881; DOI=10.1016/j.str.2012.10.017;
RA   DiMattia M.A., Watts N.R., Stahl S.J., Grimes J.M., Steven A.C.,
RA   Stuart D.I., Wingfield P.T.;
RT   "Antigenic switching of hepatitis B virus by alternative dimerization of
RT   the capsid protein.";
RL   Structure 21:133-142(2013).
RN   [7] {ECO:0000313|EMBL:AJA30208.1, ECO:0000313|Proteomes:UP000174133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MK082_EP-CHB {ECO:0000313|EMBL:AJA30208.1};
RA   Mondal R.K., Khatun M., Ghosh S., Banerjee P., Datta S., Sarkar S.,
RA   Saha B., Santra A., Banerjee S., Chowdhury A., Datta S.;
RT   "Immune driven adaptation of HBV genotype D pertains to preferential
RT   alteration in B-cell epitopes and attenuation in replicative capacity- an
RT   insight from HIV-HBV co-infection.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:AIW67997.1, ECO:0000313|Proteomes:UP000131616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cuba9 {ECO:0000313|EMBL:AIW67997.1};
RX   PubMed=25742179;
RA   Loureiro C.L., Aguilar J.C., Aguiar J., Muzio V., Penton E., Garcia D.,
RA   Guillen G., Pujol F.H.;
RT   "HBV genotypic variability in cuba.";
RL   PLoS ONE 10:E0118959-E0118959(2015).
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; HQ700497; AGB97618.1; -; Genomic_DNA.
DR   EMBL; HQ700501; AGB97645.1; -; Genomic_DNA.
DR   EMBL; HQ700503; AGB97659.1; -; Genomic_DNA.
DR   EMBL; HQ700524; AGB97795.1; -; Genomic_DNA.
DR   EMBL; HQ700525; AGB97802.1; -; Genomic_DNA.
DR   EMBL; HQ700541; AGB97895.1; -; Genomic_DNA.
DR   EMBL; KM606744; AIW67997.1; -; Genomic_DNA.
DR   EMBL; KM524345; AJA30208.1; -; Genomic_DNA.
DR   EMBL; HQ700581; AJF41506.1; -; Genomic_DNA.
DR   EMBL; HQ700583; AJF41520.1; -; Genomic_DNA.
DR   EMBL; HQ700584; AJF41527.1; -; Genomic_DNA.
DR   EMBL; AB033559; BAA85376.1; -; Genomic_DNA.
DR   PIR; C94409; NKVLA3.
DR   PIR; S33686; S33686.
DR   PDB; 3V6Z; X-ray; 3.34 A; E/F=20-178.
DR   PDBsum; 3V6Z; -.
DR   SMR; Q9QMH8; -.
DR   Proteomes; UP000100292; Genome.
DR   Proteomes; UP000111582; Genome.
DR   Proteomes; UP000115088; Genome.
DR   Proteomes; UP000116163; Genome.
DR   Proteomes; UP000119845; Genome.
DR   Proteomes; UP000131616; Genome.
DR   Proteomes; UP000137274; Genome.
DR   Proteomes; UP000137845; Genome.
DR   Proteomes; UP000154625; Genome.
DR   Proteomes; UP000160519; Genome.
DR   Proteomes; UP000167433; Genome.
DR   Proteomes; UP000174133; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3V6Z};
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"
FT   DISULFID        23..90
FT                   /evidence="ECO:0007829|PDB:3V6Z"
SQ   SEQUENCE   212 AA;  24322 MW;  36D77976FBB61196 CRC64;
     MQLFHLCLII SCSCPTVQAS KLCLGWLWGM DIDPYKEFGA TVELLSFLPS DFFPSVRDLL
     DTAAALYRDA LESPEHCSPH HTALRQAILC WGELMTLATW VGTNLEDPAS RDLVVSYVNT
     NMGLKFRQLL WFHISCLTFG RETVLEYLVS FGVWIRTPPA YRPPNAPILS TLPETTVVRR
     RGRSPRRRTP SPRRRRSQSP RRRRSQSRES QC
//