ID CAPSD_HBVC4 Reviewed; 183 AA. AC P0C6H6; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 1. DT 14-DEC-2022, entry version 62. 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 adr (isolate Korea/Kim/1989) (HBV-C). OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Blubervirales; Hepadnaviridae; Orthohepadnavirus. OX NCBI_TaxID=31512; OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2928116; DOI=10.1093/nar/17.5.2124; RA Rho H.M., Kim K., Hyun S.W., Kim Y.S.; RT "The nucleotide sequence and reading frames of a mutant hepatitis B virus RT subtype adr."; RL Nucleic Acids Res. 17:2124-2124(1989). 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=P0C6H6-1; Sequence=Displayed; CC Name=X-Core fused protein; CC IsoId=Q67863-1; 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; X14193; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; P0C6H6; -. DR Proteomes; UP000007924; 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; Hepatitis B viral capsid (hbcag); 1. PE 3: Inferred from homology; KW 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..183 FT /note="Capsid protein" FT /id="PRO_0000324365" FT REPEAT 155..160 FT /note="1; half-length" FT REPEAT 162..168 FT /note="2" FT REPEAT 170..176 FT /note="3" FT REGION 136..183 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 155..176 FT /note="3 X 7 AA repeats of S-P-R-R-R-[PR]-S" 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..172 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; 21096 MW; ED2DA1DB07FB4829 CRC64; MDIDPYKEFG ASVELLSFLP SDFFPSIRDL LDTASALYRE ALESPEHCSP HHTALRQAIL CWGELMNLAT WVGSNLEDPA SRELVVSYVN VNMGLKIRQL LWFHISCLTF GRETVLEYLV SFGVWIRTPP AYRPPNAPIL STLPETTVVR RRGRSPRRRT PSPRRRRSES PRRRRSQSRE SQC //