HBEAG_WHV1
ID HBEAG_WHV1 Reviewed; 218 AA.
AC P0C6J2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=External core antigen {ECO:0000255|HAMAP-Rule:MF_04076};
DE AltName: Full=HBeAg {ECO:0000255|HAMAP-Rule:MF_04076};
DE AltName: Full=Precore protein {ECO:0000255|HAMAP-Rule:MF_04076};
DE AltName: Full=p25 {ECO:0000255|HAMAP-Rule:MF_04076};
DE Flags: Precursor;
GN Name=C {ECO:0000255|HAMAP-Rule:MF_04076};
OS Woodchuck hepatitis B virus (isolate 1) (WHV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10430;
OH NCBI_TaxID=9995; Marmota monax (Woodchuck).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7086958; DOI=10.1128/jvi.41.1.51-65.1982;
RA Galibert F., Chen T.N., Mandart E.;
RT "Nucleotide sequence of a cloned woodchuck hepatitis virus genome:
RT comparison with the hepatitis B virus sequence.";
RL J. Virol. 41:51-65(1982).
CC -!- FUNCTION: May regulate immune response to the intracellular capsid in
CC acting as a T-cell tolerogen, by having an immunoregulatory effect
CC which prevents destruction of infected cells by cytotoxic T-cells. This
CC immune regulation may predispose to chronicity during perinatal
CC infections and prevent severe liver injury during adult infections.
CC {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- SUBUNIT: Homodimerizes. {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_04076}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=External core antigen;
CC IsoId=P0C6J2-1; Sequence=Displayed;
CC Name=Capsid protein;
CC IsoId=P69709-1; Sequence=External;
CC -!- PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- PTM: Cleaved by host furin. {ECO:0000255|HAMAP-Rule:MF_04076}.
CC -!- SIMILARITY: Belongs to the orthohepadnavirus precore antigen family.
CC {ECO:0000255|HAMAP-Rule:MF_04076}.
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DR EMBL; J02442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6ECS; X-ray; 2.90 A; A/B/C/D=31-179.
DR PDBsum; 6ECS; -.
DR SMR; P0C6J2; -.
DR Proteomes; UP000007631; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0042025; C:host cell nucleus; 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; IPR013195; Hepatitis_B_virus_capsid_N.
DR InterPro; IPR002006; Hepatitis_core.
DR InterPro; IPR036459; Viral_capsid_core_dom_sf_HBV.
DR Pfam; PF08290; Hep_core_N; 1.
DR Pfam; PF00906; Hepatitis_core; 3.
DR SUPFAM; SSF47852; SSF47852; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Disulfide bond; Host nucleus;
KW Host-virus interaction; Repeat; Secreted; Signal; Viral immunoevasion.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT CHAIN 21..218
FT /note="External core antigen"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT /id="PRO_0000324740"
FT PROPEP 190..218
FT /evidence="ECO:0000250"
FT /id="PRO_0000324741"
FT REPEAT 190..196
FT /note="1; half-length"
FT REPEAT 197..204
FT /note="2"
FT REPEAT 205..212
FT /note="3"
FT REGION 26..28
FT /note="HBEAG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT REGION 180..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..212
FT /note="3 X 8 AA repeats of S-P-R-R-R-R-S-Q"
FT COMPBIAS 183..208
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 189..190
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT DISULFID 78
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT DISULFID 91
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04076"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6ECS"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:6ECS"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6ECS"
FT HELIX 57..72
FT /evidence="ECO:0007829|PDB:6ECS"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6ECS"
FT HELIX 80..105
FT /evidence="ECO:0007829|PDB:6ECS"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:6ECS"
FT HELIX 123..140
FT /evidence="ECO:0007829|PDB:6ECS"
FT HELIX 142..157
FT /evidence="ECO:0007829|PDB:6ECS"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6ECS"
SQ SEQUENCE 218 AA; 25076 MW; 90D6126A799E5338 CRC64;
MYLFHLCLVF ACVPCPTVQA SKLCLGWLWG MDIDPYKEFG SSYQLLNFLP LDFFPDLNAL
VDTATALYEE ELTGREHCSP HHTAIRQALV CWDELTKLIA WMSSNITSEQ VRTIIVNHVN
DTWGLKVRQS LWFHLSCLTF GQHTVQEFLV SFGVWIRTPA PYRPPNAPIL STLPEHTVIR
RRGGARASRS PRRRTPSPRR RRSQSPRRRR SQSPSANC
