TEG5_GAHVM
ID TEG5_GAHVM Reviewed; 808 AA.
AC Q9E6M8;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Tegument protein UL47 homolog;
GN Name=MDV060;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32999032; DOI=10.1128/jvi.01645-20;
RA Chuard A., Courvoisier-Guyader K., Remy S., Spatz S., Denesvre C.,
RA Pasdeloup D.;
RT "The tegument protein pUL47 of Marek's Disease Virus is necessary for
RT horizontal transmission and is important for expression of glycoprotein
RT gC.";
RL J. Virol. 0:0-0(2020).
CC -!- FUNCTION: Tegument protein that can bind to various RNA transcripts.
CC Plays a role in the attenuation of selective viral and cellular mRNA
CC degradation by modulating the activity of host shutoff RNase UL41/VHS.
CC Also plays a role in the primary envelopement of virions in the
CC perinuclear space, probably by interacting with two nuclear egress
CC proteins UL31 and UL34 (By similarity). Plays an important role in the
CC splicing of glycoprotein/gC transcripts and thereby participates in
CC bird-to-bird viral transmission (PubMed:32999032).
CC {ECO:0000250|UniProtKB:P10231, ECO:0000269|PubMed:32999032}.
CC -!- SUBUNIT: Interacts with US3 kinase. Interacts with UL31 and UL34; these
CC interactions seem important for efficient virion nuclear egress.
CC Interacts with UL41/VHS. {ECO:0000250|UniProtKB:P10231}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P10231}.
CC Host nucleus {ECO:0000250|UniProtKB:P10231}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P10231}. Note=Major tegument protein of the
CC virion. Undergoes nucleocytoplasmic shuttling during infection.
CC Localizes to the major sites of transcription in the infected cell
CC nucleus. {ECO:0000250|UniProtKB:P10231}.
CC -!- DOMAIN: The nuclear export signal is CRM1-dependent.
CC {ECO:0000250|UniProtKB:P10231}.
CC -!- PTM: Phosphorylated by US3. This phosphorylation is required for proper
CC nuclear localization. {ECO:0000250|UniProtKB:P10231}.
CC -!- PTM: O-glycosylated.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants are unable to be horizontally
CC transmitted to naive chickens contrary to the wild-type virus while
CC skin tropism remains unaffected. Mutants show also an increase of
CC unspliced glycoprotein/gC transcripts. {ECO:0000269|PubMed:32999032}.
CC -!- MISCELLANEOUS: Expressed in late in the infection. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae HHV-1 UL47 family.
CC {ECO:0000305}.
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DR EMBL; AF243438; AAG14240.1; -; Genomic_DNA.
DR RefSeq; YP_001033976.1; NC_002229.3.
DR PRIDE; Q9E6M8; -.
DR GeneID; 4811521; -.
DR KEGG; vg:4811521; -.
DR Proteomes; UP000008072; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR005029; Herpes_UL47.
DR Pfam; PF03362; Herpes_UL47; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Host cytoplasm; Host nucleus; Late protein;
KW Reference proteome; Transcription; Transcription regulation; Virion;
KW Virion tegument.
FT CHAIN 1..808
FT /note="Tegument protein UL47 homolog"
FT /id="PRO_0000406587"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..155
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..213
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 91917 MW; 02FB71C13ACDC497 CRC64;
MQMPSMHRYG HPGQNQRREN QSIRNYLSTR SGSRNRISRS PHNMASVYTR APAIAYDDDT
YDTLEESEDN GFVKTIPNEE QFDNSRGRDR TRSGRSNGHS FLGYLRDTFT ERQPSGRRGS
DTSRDMINAS LKSRARSRRR SSSRRRHRNA SMHMHFRGGS RRSATGSQNL INHDRHRRIS
QSSLGSSREG EYNHASRSSR VRRRHRRSSR RRGPRAGGHG DSFTSITPSG SAEHPISDID
QKRLRKNSDT SSRGTRESPI DDSFGEDNYR LVSRNRATSI YTTPSALYTR TESLKTYKRT
TGDSKGTSPA LASFLEHKTL SADVINHIPL LRMLESVPRS EAIREDELLY MSAKTFKYVS
HWYSNSRPDY ANGKMYTSPP PENALAWKRT AKQAHALILH LGRDSLRSSV MSLRELNQSN
AVLFLLNSCL KIAICIHKNK MHKYGNVKIL STMPHVRKGD AQIFENSTIH TMRDPMASAA
RASYGSLAYW PELRCALGSE NKRIVRYAIV AMLQAEIYLL TRISSQRVSM NKSELRILSS
CITMECVAAC IAVQFLYTSL WQILYSSKIN REYIWLKTAS ERSKKLPMAS TDLLYAEGAC
LGRLESSLYG TEGTPLGRTL VEAYLATRSA FTELIYEFQS NSDLFLEKQN VKLGEKLTAA
VITATVVLQR LLGHLNIIIA QMVIGSVYHK KDVDVWSETF KMYQYLSYVC KSLYRPVTID
EYINDRDDTM EYLTLEFARG DPPTGMASVI YEDEKSEELE SLKLVPPPIN YDILGNLVPL
RNAIEDASDV IFEKRAVETA RREPQRAN
