CAPSD_HBVA2
ID CAPSD_HBVA2 Reviewed; 185 AA.
AC P03149;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Capsid protein {ECO:0000255|HAMAP-Rule:MF_04076};
DE AltName: Full=Core antigen {ECO:0000255|HAMAP-Rule:MF_04076};
DE AltName: Full=Core protein {ECO:0000255|HAMAP-Rule:MF_04076};
DE AltName: Full=HBcAg {ECO:0000255|HAMAP-Rule:MF_04076};
DE AltName: Full=p21.5 {ECO:0000255|HAMAP-Rule:MF_04076};
GN Name=C {ECO:0000255|HAMAP-Rule:MF_04076};
OS Hepatitis B virus genotype A2 subtype adw (isolate Japan/Nishioka/1983)
OS (HBV-A).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=482134;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6300776; DOI=10.1093/nar/11.6.1747;
RA Ono Y., Onda H., Sasada R., Igarashi K., Sugino Y., Nishioka K.;
RT "The complete nucleotide sequences of the cloned hepatitis B virus DNA;
RT subtype adr and adw.";
RL Nucleic Acids Res. 11:1747-1757(1983).
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:0000255|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:0000255|HAMAP-Rule:MF_04076}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04076}. Host
CC cytoplasm {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Capsid protein;
CC IsoId=P03149-1; Sequence=Displayed;
CC Name=External core antigen;
CC IsoId=P0C692-1; Sequence=External;
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:0000255|HAMAP-
CC Rule:MF_04076}.
CC -!- SIMILARITY: Belongs to the orthohepadnavirus core antigen family.
CC {ECO:0000255|HAMAP-Rule:MF_04076}.
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; V00866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 3J2V; EM; 3.50 A; A/B/C/D=1-185.
DR PDB; 6UI6; EM; 3.53 A; A/B/C=1-143.
DR PDB; 6UI7; EM; 3.65 A; A/B/C/D=1-143.
DR PDBsum; 3J2V; -.
DR PDBsum; 6UI6; -.
DR PDBsum; 6UI7; -.
DR SMR; P03149; -.
DR PRIDE; P03149; -.
DR Proteomes; UP000007906; Genome.
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; -; 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; SSF47852; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Capsid protein;
KW Cytoplasmic inwards viral transport; DNA-binding; Host cytoplasm;
KW Host-virus interaction; Microtubular inwards viral transport;
KW Phosphoprotein; Repeat; RNA-binding; T=4 icosahedral capsid protein;
KW Viral penetration into host nucleus; Virion; Virus entry into host cell.
FT CHAIN 1..185
FT /note="Capsid protein"
FT /id="PRO_0000222314"
FT REPEAT 157..163
FT /note="1; half-length"
FT REPEAT 164..171
FT /note="2"
FT REPEAT 172..179
FT /note="3"
FT REGION 136..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..179
FT /note="3 X 8 AA repeats of S-P-R-R-R-[PR]-S-Q"
FT REGION 179..185
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT MOTIF 160..177
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT COMPBIAS 153..175
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT MOD_RES 164
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT MOD_RES 172
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3J2V"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:3J2V"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:3J2V"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3J2V"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3J2V"
FT HELIX 50..74
FT /evidence="ECO:0007829|PDB:3J2V"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:3J2V"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:3J2V"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:3J2V"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3J2V"
SQ SEQUENCE 185 AA; 21394 MW; B86A90D541BA70F9 CRC64;
MDIDPYKEFG ATVELLSFLP SDFFPSVRDL LDTASALYRE ALESPEHCSP HHTALRQAIL
CWGELMTLAT WVGNNLQDPA SRDLVVNYVN TNMGLKIRQL LWFHISCLTF GRETVLEYLV
SFGVWIRTPP AYRPPNAPIL STLPETTVVR RRDRGRSPRR RTPSPRRRRS QSPRRRRSQS
RESQC
