ID B3VAR5_HBV Unreviewed; 212 AA. AC B3VAR5; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-DEC-2022, entry version 53. 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}; OS Hepatitis B virus (HBV). OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Blubervirales; Hepadnaviridae; Orthohepadnavirus. OX NCBI_TaxID=10407 {ECO:0000313|EMBL:ACE76045.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee). RN [1] {ECO:0000313|EMBL:ACE76045.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IR-RCGLD-7064 {ECO:0000313|EMBL:ACE76045.1}; RA Mohebbi S.R., Amini-Bavil-Olyaee S., Zali N., Derakhshan F., Chiani M., RA Rostami Nejad M., Sabahi F., Zali M.R.; RT "Molecular Epidemiology of Hepatitis B Virus in Iran."; RL Submitted (MAY-2008) 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}. 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; EU726883; ACE76045.1; -; Genomic_DNA. 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; -; 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="Hep_core_N" 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; 24338 MW; AFAC42A2B26A7FE6 CRC64; MQLFHLCLII SCSCPTIQAS KLCLGWLWGM DIDAYKEFGA TVELLSFLPS DFFPSVRDLL DTASALYREA LESPEHCSPH HTALRQAILC WGELMTLATW VGGNLEDPIS RDLVVSYVNT NMGLKFRQLL WFHISCLTFG RETVIEYLVS FGVWIRTPPA YRPPNAPILS TLPETTVVRR RGRSPRRRTP SPRRRRSQSP RRRRSQSRES QC //