ID   SHDAG_HDVWO             Reviewed;         195 AA.
AC   P29997; Q999V2; Q999V3;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 3.
DT   29-SEP-2021, entry version 85.
DE   RecName: Full=Small delta antigen;
DE            Short=S-HDAg;
DE   AltName: Full=p24;
OS   Hepatitis delta virus genotype I (isolate Woodchuck) (HDV).
OC   Viruses; Ribozyviria; Kolmioviridae; Deltavirus.
OX   NCBI_TaxID=31764;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3367426; DOI=10.1128/jvi.62.6.1855-1861.1988;
RA   Kuo M.Y.P., Goldberg J., Coates L., Mason W., Gerin J., Taylor J.;
RT   "Molecular cloning of hepatitis delta virus RNA from an infected woodchuck
RT   liver: sequence, structure, and applications.";
RL   J. Virol. 62:1855-1861(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RC   STRAIN=Isolate Woodchuck5;
RX   PubMed=2005438; DOI=10.1099/0022-1317-72-3-735;
RA   Deny P., Zignego A.L., Rascalou N., Ponzetto A., Tiollais P., Brechot C.;
RT   "Nucleotide sequence analysis of three different hepatitis delta viruses
RT   isolated from a woodchuck and humans.";
RL   J. Gen. Virol. 72:735-739(1991).
RN   [3]
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   [4]
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:2005438};
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 P0C6M9). S-
CC       HDAg suppresses editing of non-replicating antigenomic RNA, thereby
CC       regulating the extent of editing (By similarity). {ECO:0000250};
CC   -!- MISCELLANEOUS: This strain belongs to the genotype I found in North
CC       America, Europe, Africa, East and West Asia and the South Pacific.
CC   -!- SIMILARITY: Belongs to the hepatitis delta antigen family.
CC       {ECO:0000305}.
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DR   EMBL; M21012; AAA45723.1; -; Genomic_RNA.
DR   EMBL; AJ307077; CAC32837.1; -; Genomic_RNA.
DR   PIR; A30054; SAVLWC.
DR   SMR; P29997; -.
DR   Proteomes; UP000008686; Genome.
DR   Proteomes; UP000129583; 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_0000038159"
FT   DOMAIN          20..195
FT                   /note="HDAg"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01183"
FT   REGION          12..60
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255"
FT   REGION          45..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        57..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..145
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         13
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"
FT   VARIANT         11
FT                   /note="G -> R (in strain: Isolate Woodchuck5)"
FT   VARIANT         86
FT                   /note="R -> G (in strain: Isolate Woodchuck5)"
FT   VARIANT         96
FT                   /note="D -> E (in strain: Isolate Woodchuck5)"
SQ   SEQUENCE   195 AA;  21895 MW;  2798B67BCEF16B44 CRC64;
     MSRSESRKNR GGREEILEQW VAGRKKLEEL ERDLRKTKKK LKKIEDENPW LGNIKGILGK
     KDKDGEGAPP AKRARTDQME VDSGPRKRPL RGGFTDKERQ DHRRRKALEN KKKQLSAGGK
     NLSKEEEEEL RRLTEEDERR ERRVAGPPVG GVNPLEGGSR GAPGGGFVPN LQGVPESPFS
     RTGEGLDIRG NQGFP