SHDAG_HDV83
ID SHDAG_HDV83 Reviewed; 195 AA.
AC P69618; P25883;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 29-SEP-2021, entry version 58.
DE RecName: Full=Small delta antigen;
DE Short=S-HDAg;
DE AltName: Full=p24;
OS Hepatitis delta virus genotype II (isolate 7/18/83) (HDV).
OC Viruses; Ribozyviria; Kolmioviridae; Deltavirus.
OX NCBI_TaxID=10421;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1923832; DOI=10.1093/nar/19.19.5439;
RA Imazeki F., Omata M., Ohto M.;
RT "Complete nucleotide sequence of hepatitis delta virus RNA in Japan.";
RL Nucleic Acids Res. 19:5439-5439(1991).
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:0000250}; Note=Partially
CC edited. RNA editing at this position occurs on the antigenomic strand
CC and consists of a conversion of A to G catalyzed by the cellular enzyme
CC ADAR1. The unedited RNA version gives rise to the small delta antigen,
CC which ends with a nonsense codon at position 196. In the edited
CC version, this amber codon is modified to a tryptophan codon and gives
CC rise to the large delta antigen protein (AC P0C6L4). S-HDAg suppresses
CC editing of non-replicating antigenomic RNA, thereby regulating the
CC extent of editing (By similarity). {ECO:0000250};
CC -!- MISCELLANEOUS: This strain 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; X60193; CAA42749.1; -; Genomic_RNA.
DR PIR; B36409; SAVLDS.
DR SMR; P69618; -.
DR Proteomes; UP000008105; 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_0000038127"
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 58..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; 21928 MW; E40EE957E032C20A CRC64;
MSQSETRRGR RGTREETLEK WITARKKAEE LEKDLRKTRK TIKKLEEENP WLGNIVGIIR
KGKDGEGAPP AKRPRTDQME VDSGPGKRPH KSGFTDKERE DHRRRKALEN KKKQLSAGGK
ILSKEEEEEL RRLTDEDEER KRRVAGPRVG DVNPSRGGPR GAPGGGFVPQ MAGVPESPFS
RTGEGLDIRG TQGFP
