ID CAPSD_HBVD3 Reviewed; 183 AA.
AC P03146;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 24-JAN-2024, entry version 125.
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 ayw (isolate France/Tiollais/1979)
OS (HBV-D).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus; Hepatitis B virus;
OC hepatitis B virus genotype D.
OX NCBI_TaxID=490133;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=399327; DOI=10.1038/281646a0;
RA Galibert F., Mandart E., Fitoussi F., Tiollais P., Charnay P.;
RT "Nucleotide sequence of the hepatitis B virus genome (subtype ayw) cloned
RT in E. coli.";
RL Nature 281:646-650(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Latvia;
RX PubMed=3996597; DOI=10.1016/0014-5793(85)80771-7;
RA Bichko V., Pushko P., Dreilina D., Pumpen P., Gren E.Y.;
RT "Subtype ayw variant of hepatitis B virus. DNA primary structure
RT analysis.";
RL FEBS Lett. 185:208-212(1985).
RN [3]
RP CAPSID STRUCTURE.
RX PubMed=8589996; DOI=10.1016/s0969-2126(01)00237-4;
RA Kenney J.M., von Bonsdorff C.H., Nassal M., Fuller S.D.;
RT "Evolutionary conservation in the hepatitis B virus core structure:
RT comparison of human and duck cores.";
RL Structure 3:1009-1019(1995).
RN [4]
RP PHOSPHORYLATION.
RX PubMed=9557662; DOI=10.1128/jvi.72.5.3796-3803.1998;
RA Kau J.H., Ting L.P.;
RT "Phosphorylation of the core protein of hepatitis B virus by a 46-
RT kilodalton serine kinase.";
RL J. Virol. 72:3796-3803(1998).
RN [5]
RP NATURALLY OCCURRING MUTATION.
RX PubMed=10559327; DOI=10.1128/jvi.73.12.10122-10128.1999;
RA Yuan T.T., Tai P.C., Shih C.;
RT "Subtype-independent immature secretion and subtype-dependent replication
RT deficiency of a highly frequent, naturally occurring mutation of human
RT hepatitis B virus core antigen.";
RL J. Virol. 73:10122-10128(1999).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=12134018; DOI=10.1128/jvi.76.16.8124-8137.2002;
RA Daub H., Blencke S., Habenberger P., Kurtenbach A., Dennenmoser J.,
RA Wissing J., Ullrich A., Cotten M.;
RT "Identification of SRPK1 and SRPK2 as the major cellular protein kinases
RT phosphorylating hepatitis B virus core protein.";
RL J. Virol. 76:8124-8137(2002).
RN [7]
RP PHOSPHORYLATION AT SER-155; SER-162 AND SER-170, AND MUTAGENESIS OF
RP SER-155; SER-162 AND SER-170.
RX PubMed=16014942; DOI=10.1128/jvi.79.15.9810-9820.2005;
RA Melegari M., Wolf S.K., Schneider R.J.;
RT "Hepatitis B virus DNA replication is coordinated by core protein serine
RT phosphorylation and HBx expression.";
RL J. Virol. 79:9810-9820(2005).
RN [8]
RP REVIEW.
RX PubMed=15567498; DOI=10.1016/j.virusres.2004.08.016;
RA Bruss V.;
RT "Envelopment of the hepatitis B virus nucleocapsid.";
RL Virus Res. 106:199-209(2004).
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=P03146-1; Sequence=Displayed;
CC Name=External core antigen;
CC IsoId=P0C573-1; 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 -!- SEQUENCE CAUTION:
CC Sequence=CAA24706.1; Type=Erroneous initiation;
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DR EMBL; V01460; CAA24706.1; ALT_INIT; Genomic_DNA.
DR EMBL; X02496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; YP_009173857.1; NC_003977.2.
DR PDB; 6HTX; EM; 2.66 A; A/B/C/D=1-183.
DR PDB; 6HU4; EM; 2.64 A; A/B/C/D/E/F/G/H=1-183.
DR PDB; 6HU7; EM; 2.80 A; A/B/C/D/F/G/H=1-183.
DR PDB; 7OCO; EM; 3.20 A; A/B/C/D=1-183.
DR PDB; 7OCW; EM; 3.20 A; A/B/C/D=1-183.
DR PDB; 7OD4; EM; 2.80 A; A/B/C/D=1-183.
DR PDB; 7OD6; EM; 3.00 A; A/B/C/D=1-183.
DR PDB; 7OD7; EM; 2.80 A; A/B/C/D=1-183.
DR PDB; 7OD8; EM; 3.00 A; A/B/C/D=1-183.
DR PDB; 7OEN; EM; 3.20 A; A/B/C/D=1-183.
DR PDB; 7OEV; EM; 3.10 A; A/B/C/D=1-183.
DR PDB; 7OEW; EM; 2.90 A; A/B/C/D=1-183.
DR PDB; 7PZ9; EM; 2.80 A; A/B/C/D=1-183.
DR PDB; 7PZI; EM; 2.90 A; A/B/C/D=1-183.
DR PDB; 7PZK; EM; 3.10 A; A/B/C/D=1-183.
DR PDB; 7PZL; EM; 2.80 A; A/B/C/D=1-183.
DR PDB; 7PZM; EM; 2.90 A; A/B/C/D=1-183.
DR PDB; 7PZN; EM; 3.20 A; A/B/C/D=1-183.
DR PDBsum; 6HTX; -.
DR PDBsum; 6HU4; -.
DR PDBsum; 6HU7; -.
DR PDBsum; 7OCO; -.
DR PDBsum; 7OCW; -.
DR PDBsum; 7OD4; -.
DR PDBsum; 7OD6; -.
DR PDBsum; 7OD7; -.
DR PDBsum; 7OD8; -.
DR PDBsum; 7OEN; -.
DR PDBsum; 7OEV; -.
DR PDBsum; 7OEW; -.
DR PDBsum; 7PZ9; -.
DR PDBsum; 7PZI; -.
DR PDBsum; 7PZK; -.
DR PDBsum; 7PZL; -.
DR PDBsum; 7PZM; -.
DR PDBsum; 7PZN; -.
DR BMRB; P03146; -.
DR EMDB; EMD-0271; -.
DR EMDB; EMD-0272; -.
DR EMDB; EMD-0273; -.
DR EMDB; EMD-12810; -.
DR EMDB; EMD-12815; -.
DR EMDB; EMD-12820; -.
DR EMDB; EMD-12821; -.
DR EMDB; EMD-12822; -.
DR EMDB; EMD-13726; -.
DR EMDB; EMD-13728; -.
DR EMDB; EMD-13731; -.
DR EMDB; EMD-13732; -.
DR EMDB; EMD-13733; -.
DR EMDB; EMD-13734; -.
DR SMR; P03146; -.
DR iPTMnet; P03146; -.
DR KEGG; vg:944568; -.
DR Proteomes; UP000007930; Segment.
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 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; Reference proteome; 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_0000222315"
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 ECO:0000269|PubMed:16014942"
FT MOD_RES 162
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076,
FT ECO:0000269|PubMed:16014942"
FT MOD_RES 170
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076,
FT ECO:0000269|PubMed:16014942"
FT VARIANT 33
FT /note="T -> N (in strain: Latvia)"
FT VARIANT 80
FT /note="A -> I (in strain: Latvia)"
FT VARIANT 97
FT /note="F -> L (frequent mutation in chronic HBV carriers)"
FT MUTAGEN 155
FT /note="S->A: Complete loss of replication."
FT /evidence="ECO:0000269|PubMed:16014942"
FT MUTAGEN 162
FT /note="S->A: Complete loss of pregenomic RNA encapsidation
FT and replication."
FT /evidence="ECO:0000269|PubMed:16014942"
FT MUTAGEN 170
FT /note="S->A: Partial loss of replication."
FT /evidence="ECO:0000269|PubMed:16014942"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:6HU4"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:6HU4"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:7OD7"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6HU4"
FT HELIX 27..42
FT /evidence="ECO:0007829|PDB:6HU4"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6HU4"
FT HELIX 50..75
FT /evidence="ECO:0007829|PDB:6HU4"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:6HU4"
FT HELIX 92..109
FT /evidence="ECO:0007829|PDB:6HU4"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:6HU4"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6HU4"
SQ SEQUENCE 183 AA; 21116 MW; E0D9D9763F24E958 CRC64;
MDIDPYKEFG ATVELLSFLP SDFFPSVRDL LDTASALYRE ALESPEHCSP HHTALRQAIL
CWGELMTLAT WVGVNLEDPA SRDLVVSYVN TNMGLKFRQL LWFHISCLTF GRETVIEYLV
SFGVWIRTPP AYRPPNAPIL STLPETTVVR RRGRSPRRRT PSPRRRRSQS PRRRRSQSRE
SQC
//
