SHDAG_HDVAM
ID SHDAG_HDVAM Reviewed; 195 AA.
AC P25989;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 29-SEP-2021, entry version 95.
DE RecName: Full=Small delta antigen;
DE Short=S-HDAg;
DE AltName: Full=p24;
OS Hepatitis delta virus genotype I (isolate American) (HDV).
OC Viruses; Ribozyviria; Kolmioviridae; Deltavirus.
OX NCBI_TaxID=10422;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3627276; DOI=10.1038/329343a0;
RA Makino S., Chang M.F., Shieh C.K., Kamahora T., Vannier D.M.,
RA Govindarajan S., Lai M.M.C.;
RT "Molecular cloning and sequencing of a human hepatitis delta (delta) virus
RT RNA.";
RL Nature 329:343-346(1987).
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).
RN [4]
RP STRUCTURE BY NMR OF 24-50.
RX PubMed=10451556;
RX DOI=10.1002/(sici)1097-0134(19991001)37:1<121::aid-prot12>3.0.co;2-t;
RA Lin I.J., Lou Y.C., Pai M.T., Wu H.N., Cheng J.W.;
RT "Solution structure and RNA-binding activity of the N-terminal leucine-
RT repeat region of hepatitis delta antigen.";
RL Proteins 37:121-129(1999).
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 P0C6L5). 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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M28267; AAA98112.1; ALT_TERM; Genomic_RNA.
DR PDB; 1A92; X-ray; 1.80 A; A/B/C/D=12-60.
DR PDB; 1BY0; NMR; -; A=24-50.
DR PDBsum; 1A92; -.
DR PDBsum; 1BY0; -.
DR SMR; P25989; -.
DR PRIDE; P25989; -.
DR EvolutionaryTrace; P25989; -.
DR Proteomes; UP000007708; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Host nucleus; Host-virus interaction;
KW Methylation; 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_0000038129"
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 52..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 HELIX 13..47
FT /evidence="ECO:0007829|PDB:1A92"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:1A92"
SQ SEQUENCE 195 AA; 21962 MW; 32A13B0F464566F4 CRC64;
MSRSERRKDR GGREDILEQW VSGRKKLEEL ERDLRKLKKK IKKLEEDNPW LGNIKGIIGK
KDKDGEGAPP AKKLRMDQME IDAGPRKRPL RGGFTDKERQ DHRRRKALEN KRKQLSSGGK
SLSREEEEEL KRLTEEDEKR ERRIAGPSVG GVNPLEGGSR GAPGGGFVPS MQGVPESPFA
RTGEGLDIRG SQGFP
