ID Q91IP2_HBV Unreviewed; 325 AA.
AC Q91IP2;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 22-FEB-2023, entry version 81.
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:AAK59314.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:AAK59314.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XC-957-31 {ECO:0000313|EMBL:AAK59314.1};
RA Liu Y., Dong J., Huangfu J.K., Cheng J., Wang L., Wang G., Li L.;
RT "Effect of hepatitis B virus X gene heterogeneity on its transcription.";
RL Jie Fang Jun Yi Xue Za Zhi 27:125-127(2002).
RN [2] {ECO:0000313|EMBL:AAK59314.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=XC-957-31 {ECO:0000313|EMBL:AAK59314.1};
RA Dong J., Shi S.S., Huangfu J.K., Cheng J., Wang Q.H., Li L., Si C.W.;
RT "The preliminary study on hepatitis B virus quasispecies: X gene and its
RT mutants.";
RL Zhongguo Bing Du Xue 17:22-26(2002).
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}.
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DR EMBL; AF384370; AAK59314.1; -; 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:0019079; P:viral genome replication; IEA:InterPro.
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; IPR000236; Transactivation_prot_X.
DR InterPro; IPR036459; Viral_capsid_core_dom_sf_HBV.
DR Pfam; PF08290; Hep_core_N; 1.
DR Pfam; PF00906; Hepatitis_core; 3.
DR Pfam; PF00739; X; 1.
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 DOMAIN 114..140
FT /note="Hepatitis B virus capsid N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08290"
FT REGION 278..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..325
FT /note="RNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT MOTIF 300..317
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT COMPBIAS 294..315
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 297
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT MOD_RES 304
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
FT MOD_RES 312
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04076"
SQ SEQUENCE 325 AA; 36156 MW; ADBEF4FEF644E5B5 CRC64;
MAARVCCQLD PARDVLCLRP VGAESRGRPV SGPFGPLSSP SSSAVPADHG AHLSLRGLPV
CAFSSAGPCA LRFTSARRME TTVNAHQVLP KVLHKRTLGL SAMSTTDLEA YFNMQLFHLC
LIISCSCPTV QASKLCLGWL WGMDIGPYKE FGASVELLSF LPSDFFPSIR DLLDTASALY
REALESPEHC SPHHTALRQA ILCWGELMNL ATWVGSNLED PASRELVVSY VNVNMGLKIR
QLLWFHISCL TFGRETVLEY LVSFGVWIRT PPAYRPPNAP ILSTLPETTV VRRRGRSPRR
RTPSPRRRRS QSPRRRRSQS RESQC
//
