CAPSD_HBVCJ
ID CAPSD_HBVCJ Reviewed; 183 AA.
AC Q76R61;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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 C subtype ayr (isolate Human/Japan/Okamoto/-)
OS (HBV-C).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus;
OC hepatitis B virus genotype C.
OX NCBI_TaxID=928302;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3783127; DOI=10.1099/0022-1317-67-11-2305;
RA Okamoto H., Imai M., Shimozaki M., Hoshi Y., Iizuka H., Gotanda T.,
RA Tsuda F., Miyakawa Y., Mayumi M.;
RT "Nucleotide sequence of a cloned hepatitis B virus genome, subtype ayr:
RT comparison with genomes of the other three subtypes.";
RL J. Gen. Virol. 67:2305-2314(1986).
RN [2]
RP NUCLEAR LOCALIZATION SIGNAL, AND INTERACTION WITH HOST IMPORTIN ALPHA.
RX PubMed=10189367; DOI=10.1083/jcb.145.1.45;
RA Kann M., Sodeik B., Vlachou A., Gerlich W.H., Helenius A.;
RT "Phosphorylation-dependent binding of hepatitis B virus core particles to
RT the nuclear pore complex.";
RL J. Cell Biol. 145:45-55(1999).
RN [3]
RP FUNCTION.
RX PubMed=12909718; DOI=10.1073/pnas.1730940100;
RA Rabe B., Vlachou A., Pante N., Helenius A., Kann M.;
RT "Nuclear import of hepatitis B virus capsids and release of the viral
RT genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9849-9854(2003).
RN [4]
RP FUNCTION.
RX PubMed=15254201; DOI=10.1128/jvi.78.15.8289-8300.2004;
RA Funk A., Mhamdi M., Lin L., Will H., Sirma H.;
RT "Itinerary of hepatitis B viruses: delineation of restriction points
RT critical for infectious entry.";
RL J. Virol. 78:8289-8300(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH RAT NUP153.
RX PubMed=20126445; DOI=10.1371/journal.ppat.1000741;
RA Schmitz A., Schwarz A., Foss M., Zhou L., Rabe B., Hoellenriegel J.,
RA Stoeber M., Pante N., Kann M.;
RT "Nucleoporin 153 arrests the nuclear import of hepatitis B virus capsids in
RT the nuclear basket.";
RL PLoS Pathog. 6:E1000741-E1000741(2010).
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, ECO:0000269|PubMed:12909718,
CC ECO:0000269|PubMed:15254201, ECO:0000269|PubMed:20126445}.
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, ECO:0000269|PubMed:10189367,
CC ECO:0000269|PubMed:20126445}.
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=Q76R61-1; Sequence=Displayed;
CC Name=External core antigen;
CC IsoId=P0C767-1; 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}.
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DR EMBL; X04615; CAA28289.1; -; Genomic_DNA.
DR PDB; 5E00; X-ray; 1.70 A; C=123-131.
DR PDBsum; 5E00; -.
DR SMR; Q76R61; -.
DR BindingDB; Q76R61; -.
DR Proteomes; UP000008591; 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; 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_0000390308"
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"
SQ SEQUENCE 183 AA; 21095 MW; ED2DA1DB07FB596D CRC64;
MDIDPYKEFG ASVELLSFLP SDFFPSIRDL LDTASALYRE ALESPEHCSP HHTALRQAIL
CWGELMNLAT WVGSNLEDPA SRELVVSYVN VNMGLKIRQL LWFHISCLTF GRETVLEYLV
SFGVWIRTPP AYRPPNAPIL STLPETTVVR RRGRSPRRRT PSPRRRRSQS PRRRRSQSRE
SQC
