ID A6YJZ8_HBV Unreviewed; 181 AA.
AC A6YJZ8;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-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};
OS Hepatitis B virus (HBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10407 {ECO:0000313|EMBL:ABR32141.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:ABR32141.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I15 {ECO:0000313|EMBL:ABR32141.1};
RA Zhou F., Ren J., Dong J.;
RT "A novel mutation to HBeAg-negative chronic hepatitis B (CHB).";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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: Virion {ECO:0000256|HAMAP-Rule:MF_04076}. Host
CC cytoplasm {ECO:0000256|HAMAP-Rule:MF_04076}.
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04076}.
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DR EMBL; EF608593; ABR32141.1; -; Genomic_DNA.
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 Gene3D; 1.10.4090.10; Viral capsid, core domain supefamily, Hepatitis B virus; 1.
DR HAMAP; MF_04076; HBV_HBEAG; 1.
DR InterPro; IPR002006; Hepatitis_core.
DR InterPro; IPR036459; Viral_capsid_core_dom_sf_HBV.
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 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 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 REGION 136..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 158..175
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT COMPBIAS 152..172
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT MOD_RES 162
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT MOD_RES 170
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
SQ SEQUENCE 181 AA; 20749 MW; D0C2E06FFFD2A006 CRC64;
MDIDPYKEFG ASVELLSFLP SDFFPAIRDL LDTASALYRE ALESPEHCSP HHTALRQAIL
CWGELMNLAT WVGSNLEDPA SRELVVSYVN VNMGLKIRQL LWFHISCLTF GRETVLEYLV
SFGVWIRTPP AYRPPNAPIL STLPETTVVR RRGRSPRRRT PSPRRRRSQS PRRGRSQSRE
S
//
