SHDAG_HDVTW
ID SHDAG_HDVTW Reviewed; 195 AA.
AC Q9E925; Q9E924;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Small delta antigen;
DE Short=S-HDAg;
DE AltName: Full=p24;
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: Promotes both transcription and replication of genomic RNA.
CC Following virus entry into host cell, provides nuclear import of HDV
CC RNPs thanks to its nuclear localization signal. May interact with host
CC RNA polymerase II thereby changing its template requirement from DNA to
CC RNA. RNA pol II complex would then acts as an RNA-directed RNA
CC polymerase, and transcribe and replicate HDV genome (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Homooctamer. Interacts with host RNA polymerase II
CC complex, and with host NPM1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion. Host nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated at serines and threonines by host MAPK1/3, PKR, and
CC CK2. {ECO:0000250}.
CC -!- PTM: Acetylation modulates nuclear localization. Neo-synthesized
CC genomic RNA migrates from the nucleus to the cytoplasm, where they
CC interact with S-HDAg, which once acetylated redirect both partners to
CC the nucleus (By similarity). {ECO:0000250}.
CC -!- PTM: Methylation plays a role in viral genome replication.
CC {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, which ends with a nonsense codon at position 196.
CC In the edited version, this amber codon is modified to a tryptophan
CC codon and gives rise to the large delta antigen protein (AC P0C6M4). 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; AAG26089.1; -; Genomic_RNA.
DR SMR; Q9E925; -.
DR PRIDE; Q9E925; -.
DR Proteomes; UP000008113; Genome.
DR GO; GO:0042025; C:host cell nucleus; 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; Host-virus interaction; Methylation;
KW Phosphoprotein; RNA editing; RNA-binding;
KW Viral penetration into host nucleus; Virion; Virus entry into host cell.
FT CHAIN 1..195
FT /note="Small delta antigen"
FT /id="PRO_0000038149"
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..195
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:P0C6L3"
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 CK2"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT MOD_RES 14
FT /note="Omega-N-methylated arginine; by host PRMT1"
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:P0C6L3"
FT MOD_RES 177
FT /note="Phosphoserine; by host MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
FT MOD_RES 182
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000250|UniProtKB:P0C6L3"
SQ SEQUENCE 195 AA; 21905 MW; 8421C158B18259E4 CRC64;
MSQSESKKNR RGGREDILEK WITTRRKAEE LEKDLRKARK TIKKLEDENP WLGNIIGIIR
KGKDGEGAPP AKRPRTDQME IDSGTGKRPH KSGFTDKERE DHRRRKALEN KKKQLSSGGK
NLSREEEEEL GRLTVEDEER RRRVAGPRTG DVNLSGGGPR GAPGGGFVPR MEGVPESPFT
RTGEGLDIRG NQGFP
