CAPSD_HBVD1
ID CAPSD_HBVD1 Reviewed; 183 AA.
AC P03147;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 118.
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 D subtype adw (isolate United Kingdom/adyw/1979)
OS (HBV-D).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10419;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=399329; DOI=10.1038/282575a0;
RA Pasek M., Goto T., Gilbert W., Zink B., Schaller H., McKay P.,
RA Leadbetter G., Murray K.;
RT "Hepatitis B virus genes and their expression in E. coli.";
RL Nature 282:575-579(1979).
RN [2]
RP CHARACTERIZATION.
RX PubMed=7041126; DOI=10.1073/pnas.79.5.1606;
RA Stahl S., MacKay P., Magazin M., Bruce S.A., Murray K.;
RT "Hepatitis B virus core antigen: synthesis in Escherichia coli and
RT application in diagnosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1606-1610(1982).
RN [3]
RP FUNCTION.
RX PubMed=7711014; DOI=10.1021/bi00015a003;
RA Wingfield P.T., Stahl S.J., Williams R.W., Steven A.C.;
RT "Hepatitis core antigen produced in Escherichia coli: subunit composition,
RT conformational analysis, and in vitro capsid assembly.";
RL Biochemistry 34:4919-4932(1995).
RN [4]
RP CAPSID MORPHOGENESIS.
RX PubMed=11867516; DOI=10.1093/emboj/21.5.876;
RA Watts N.R., Conway J.F., Cheng N., Stahl S.J., Belnap D.M., Steven A.C.,
RA Wingfield P.T.;
RT "The morphogenic linker peptide of HBV capsid protein forms a mobile array
RT on the interior surface.";
RL EMBO J. 21:876-884(2002).
RN [5]
RP CAPSID ASSEMBLY.
RX PubMed=12269796; DOI=10.1021/bi0261645;
RA Ceres P., Zlotnick A.;
RT "Weak protein-protein interactions are sufficient to drive assembly of
RT hepatitis B virus capsids.";
RL Biochemistry 41:11525-11531(2002).
RN [6]
RP MUTAGENESIS OF PHE-97.
RX PubMed=15308745; DOI=10.1128/jvi.78.17.9538-9543.2004;
RA Ceres P., Stray S.J., Zlotnick A.;
RT "Hepatitis B virus capsid assembly is enhanced by naturally occurring
RT mutation F97L.";
RL J. Virol. 78:9538-9543(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.96 ANGSTROMS) OF 0-149.
RX PubMed=16943288; DOI=10.1128/jvi.00933-06;
RA Bourne C.R., Finn M.G., Zlotnick A.;
RT "Global structural changes in hepatitis B virus capsids induced by the
RT assembly effector HAP1.";
RL J. Virol. 80:11055-11061(2006).
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 -!- INTERACTION:
CC P03147; P03147: C; NbExp=7; IntAct=EBI-15711833, EBI-15711833;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04076}. Host
CC cytoplasm {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_04076}.
CC -!- SIMILARITY: Belongs to the orthohepadnavirus core antigen family.
CC {ECO:0000255|HAMAP-Rule:MF_04076}.
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DR EMBL; J02202; AAA45486.1; -; Genomic_RNA.
DR PIR; B93217; NKVLA2.
DR PDB; 2G33; X-ray; 3.96 A; A/B/C/D=1-149.
DR PDB; 2G34; X-ray; 5.05 A; A/B/C/D=1-149.
DR PDB; 2QIJ; X-ray; 8.90 A; A/B/C/D=3-148.
DR PDB; 3KXS; X-ray; 2.25 A; A/B/C/D/E/F=1-143.
DR PDB; 4BMG; X-ray; 3.00 A; A/B/C/D/E/F=1-149.
DR PDB; 4G93; X-ray; 4.20 A; A/B/C/D=1-149.
DR PDB; 5D7Y; X-ray; 3.89 A; A/B/C/D=1-149.
DR PDB; 5E0I; X-ray; 1.95 A; A/B/C/D/E/F=1-149.
DR PDB; 5GMZ; X-ray; 1.70 A; A/B/C/D/E/F=1-149.
DR PDB; 5WTW; X-ray; 2.62 A; A/B=1-142.
DR PDB; 6BVF; EM; 4.00 A; A/B/C/D=1-149.
DR PDB; 6BVN; EM; 4.00 A; A/B/C=1-149.
DR PDB; 6CWD; X-ray; 3.33 A; C/D/F/H=1-149.
DR PDB; 6CWT; X-ray; 3.15 A; E/F=1-149.
DR PDB; 6J10; X-ray; 2.30 A; A/B/C/D/E/F=1-149.
DR PDB; 6VZP; EM; 3.60 A; A/B/C/D=1-149.
DR PDB; 6W0K; EM; 4.60 A; A/B/C/D=1-149.
DR PDB; 6WFS; EM; 4.60 A; A/B/C/D=1-149.
DR PDB; 7K5M; X-ray; 2.65 A; A/B/C/D/E/F=1-149.
DR PDBsum; 2G33; -.
DR PDBsum; 2G34; -.
DR PDBsum; 2QIJ; -.
DR PDBsum; 3KXS; -.
DR PDBsum; 4BMG; -.
DR PDBsum; 4G93; -.
DR PDBsum; 5D7Y; -.
DR PDBsum; 5E0I; -.
DR PDBsum; 5GMZ; -.
DR PDBsum; 5WTW; -.
DR PDBsum; 6BVF; -.
DR PDBsum; 6BVN; -.
DR PDBsum; 6CWD; -.
DR PDBsum; 6CWT; -.
DR PDBsum; 6J10; -.
DR PDBsum; 6VZP; -.
DR PDBsum; 6W0K; -.
DR PDBsum; 6WFS; -.
DR PDBsum; 7K5M; -.
DR BMRB; P03147; -.
DR SMR; P03147; -.
DR DIP; DIP-60476N; -.
DR ABCD; P03147; 2 sequenced antibodies.
DR EvolutionaryTrace; P03147; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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; Capsid protein; Cytoplasmic inwards viral transport;
KW DNA-binding; Host cytoplasm; Host-virus interaction;
KW Microtubular inwards viral transport; Phosphoprotein; Repeat; RNA-binding;
KW T=4 icosahedral capsid protein; Viral penetration into host nucleus;
KW Virion; Virus entry into host cell.
FT CHAIN 1..183
FT /note="Capsid protein"
FT /id="PRO_0000222318"
FT REPEAT 155..161
FT /note="1; half-length"
FT REPEAT 162..169
FT /note="2"
FT REPEAT 170..177
FT /note="3"
FT REGION 136..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..177
FT /note="3 X 8 AA repeats of S-P-R-R-R-[PR]-S-Q"
FT REGION 177..183
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT MOTIF 158..175
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT COMPBIAS 152..173
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT MOD_RES 162
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT MOD_RES 170
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT MUTAGEN 97
FT /note="F->L: Enhances capsid assembly."
FT /evidence="ECO:0000269|PubMed:15308745"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:5GMZ"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:5GMZ"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:5GMZ"
FT HELIX 27..43
FT /evidence="ECO:0007829|PDB:5GMZ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5GMZ"
FT HELIX 50..74
FT /evidence="ECO:0007829|PDB:5GMZ"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:5GMZ"
FT HELIX 93..110
FT /evidence="ECO:0007829|PDB:5GMZ"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:5GMZ"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:5GMZ"
SQ SEQUENCE 183 AA; 21042 MW; 545ED0E55527F26C CRC64;
MDIDPYKEFG ATVELLSFLP SDFFPSVRDL LDTAAALYRD ALESPEHCSP HHTALRQAIL
CWGDLMTLAT WVGTNLEDPA SRDLVVSYVN TNVGLKFRQL LWFHISCLTF GRETVLEYLV
SFGVWIRTPP AYRPPNAPIL STLPETTVVR RRGRSPRRRT PSPRRRRSQS PRRRRSQSRE
SQC
