LHDAG_HDVTW
ID LHDAG_HDVTW Reviewed; 214 AA.
AC P0C6M4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 29-SEP-2021, entry version 50.
DE RecName: Full=Large delta antigen;
DE Short=L-HDAg;
DE AltName: Full=p27;
DE Flags: Precursor;
OS Hepatitis delta virus genotype II (isolate TW2476) (HDV).
OC Viruses; Ribozyviria; Kolmioviridae; Deltavirus.
OX NCBI_TaxID=261992;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX PubMed=10555293; DOI=10.1093/oxfordjournals.molbev.a026075;
RA Wu J.-C., Chiang T.-Y., Shiue W.-K., Wang S.-Y., Sheen I.-J., Huang Y.-H.,
RA Syu W.-J.;
RT "Recombination of hepatitis D virus RNA sequences and its implications.";
RL Mol. Biol. Evol. 16:1622-1632(1999).
RN [2]
RP REVIEW.
RX PubMed=16402678;
RA Husa P., Linhartova A., Nemecek V., Husova L.;
RT "Hepatitis D.";
RL Acta Virol. 49:219-225(2005).
RN [3]
RP REVIEW.
RX PubMed=16903222; DOI=10.1007/3-540-29802-9_5;
RA Huang W.H., Chen C.W., Wu H.L., Chen P.J.;
RT "Post-translational modification of delta antigen of hepatitis D virus.";
RL Curr. Top. Microbiol. Immunol. 307:91-112(2006).
CC -!- FUNCTION: Following virus entry into host cell, provides nuclear import
CC of HDV RNPs thanks to its nuclear localization signal. Needs co-
CC infection with hepatitis B virus to provide surface proteins, otherwise
CC there is no packaging or budding. Packages the HDV ribonucleoprotein in
CC hepatitis B virus empty particles. Interacts with both HDV genomic RNA
CC and cytoplasmic tail of HBsAg. May inhibit viral RNA replication (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Homooctamer. Interacts with HBV HBsAg. May interact
CC with clathrin to induce virion budding (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus, host nucleolus.
CC Note=isoprenylated in the cytoplasm, and translocates in the nucleus
CC possibly after phosphorylation. Translocates after to nuclear speckle,
CC then to the ER membrane where interaction with Hepatitis B virus
CC antigene takes place (By similarity). {ECO:0000250}.
CC -!- PTM: Prenylated by host farnesyl-transferase in the cytoplasm prior to
CC nucleus translocation. {ECO:0000250}.
CC -!- PTM: Phosphorylated at serines by host CK2 and other kinases.
CC phosphorylation does not seem to be important for its function (By
CC similarity). {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=196 {ECO:0000269|PubMed:10555293};
CC Note=Partially edited. RNA editing at this position occurs on the
CC antigenomic strand and consists of a conversion of A to G catalyzed by
CC the cellular enzyme ADAR1. The unedited RNA version gives rise to the
CC small delta antigen (AC Q9E925), which ends with a nonsense codon at
CC position 196. In the edited version, this amber codon is modified to a
CC tryptophan codon and gives rise to the large delta antigen protein. S-
CC HDAg suppresses editing of non-replicating antigenomic RNA, thereby
CC regulating the extent of editing (By similarity). {ECO:0000250};
CC -!- MISCELLANEOUS: This strains belongs to the genotype II found only in
CC East Asia.
CC -!- SIMILARITY: Belongs to the hepatitis delta antigen family.
CC {ECO:0000305}.
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DR EMBL; AF104264; AAG26088.1; -; Genomic_RNA.
DR SMR; P0C6M4; -.
DR Proteomes; UP000008113; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR Gene3D; 4.10.220.40; -; 1.
DR InterPro; IPR027403; Delta_antigen_N.
DR InterPro; IPR037517; HDAG_dom.
DR InterPro; IPR002506; HDV_ag.
DR Pfam; PF01517; HDV_ag; 1.
DR SUPFAM; SSF58108; SSF58108; 1.
DR PROSITE; PS51838; HDAG; 1.
PE 3: Inferred from homology;
KW Acetylation; Host nucleus; Lipoprotein; Methylation; Phosphoprotein;
KW Prenylation; RNA editing; RNA-binding; Viral penetration into host nucleus;
KW Virion; Virus entry into host cell.
FT CHAIN 1..211
FT /note="Large delta antigen"
FT /id="PRO_0000038148"
FT PROPEP 212..214
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT /id="PRO_0000396679"
FT DOMAIN 21..195
FT /note="HDAg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT REGION 13..60
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 59..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..107
FT /note="RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT REGION 130..195
FT /note="RNAPII-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT REGION 136..146
FT /note="RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT MOTIF 66..75
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT COMPBIAS 65..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT MOD_RES 14
FT /note="Omega-N-methylated arginine; by host"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT MOD_RES 72
FT /note="N6-acetyllysine; by host"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT MOD_RES 123
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT MOD_RES 177
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT MOD_RES 211
FT /note="Cysteine methyl ester; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
FT LIPID 211
FT /note="S-farnesyl cysteine; by host"
FT /evidence="ECO:0000250|UniProtKB:P29996"
SQ SEQUENCE 214 AA; 24132 MW; 9F54BDC48655BB0A CRC64;
MSQSESKKNR RGGREDILEK WITTRRKAEE LEKDLRKARK TIKKLEDENP WLGNIIGIIR
KGKDGEGAPP AKRPRTDQME IDSGTGKRPH KSGFTDKERE DHRRRKALEN KKKQLSSGGK
NLSREEEEEL GRLTVEDEER RRRVAGPRTG DVNLSGGGPR GAPGGGFVPR MEGVPESPFT
RTGEGLDIRG NQGFPWVRPS PPQQRLPLLE CTPQ
