ID   TEG5_EHV4               Reviewed;         872 AA.
AC   P25073;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Tegument protein UL47 homolog;
DE   AltName: Full=GP10;
GN   Name=13; Synonyms=B6;
OS   Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10333;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1850013; DOI=10.1128/jvi.65.5.2320-2326.1991;
RA   Whittaker G.R., Riggio M.P., Halliburton I.W., Killington R.A., Allen G.P.,
RA   Meredith D.M.;
RT   "Antigenic and protein sequence homology between VP13/14, a herpes simplex
RT   virus type 1 tegument protein, and gp10, a glycoprotein of equine
RT   herpesvirus 1 and 4.";
RL   J. Virol. 65:2320-2326(1991).
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. {ECO:0000250|UniProtKB:P10231}.
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   -!- 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; X17684; CAA35672.1; -; Genomic_DNA.
DR   PIR; A37992; TNBEEH.
DR   PRIDE; P25073; -.
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; Transcription;
KW   Transcription regulation; Virion; Virion tegument.
FT   CHAIN           1..872
FT                   /note="Tegument protein UL47 homolog"
FT                   /id="PRO_0000116079"
FT   REGION          1..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           13..33
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..128
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..200
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   872 AA;  97377 MW;  1F07FFD6AFD6430D CRC64;
     MDQHHGVRGG APIRRPRRSI ETRSHPFRAA GNTQRTYSTP RLSYRDGLSG RASSLEPGGQ
     AHDQNESSTQ STSNNQPSTS FWGYLRRVFS DDAPAQPQAP RSRADFAPPP EEDSSSEEED
     EEGPSQAPLD EEDQLMYADQ YSVGNSSDDN EEDYLQPEVE YPTSAESGEY HNSGMFAEEE
     PESESESDME NYETYEENDT EVISDDSHRL TRTWLDRSIR LMDDALAQSS EISKAITKST
     RRLYDSQFTP GGRGYKQTET PSQRLVHLSR AGMYDSDEIV MTGDYMEVDD DPNSAYQSWV
     RAIHHPVAMN PSWEETISNH TNTSFSADID YDIDELIEMN LARTPPVFEG LLDSADFFYR
     LPMLYTYATI TQDEAYEERQ AWSNTQALHG HEQSSWPALV SDYSKGGMYV SPTQEPRGIW
     RRALKQAMAL QLKLCVLGLT EFVTKRELTQ HHSAVTFLVD SLLRTAKNCY LASRLLVFAW
     ERRRETGVRR PAEPLIALSG VTLLQPLPPE VSELLEQRTF DIGLRTPQSG VFRAFFGPLV
     YWAELRRALR DPAAINCRYV GFHLQTSEIY LLARAHSASP GYTKEELVAM EATLTLGTLM
     LEVALQWIHV ASAQLLSEND ALKAFRRVSA SIPHALAPLG SIRLHDAEFE VLSNPDVMVA
     RDETALSQAL FLGYFSVRTA LTACMRDYAN EVDGGSKETV TGLFLGVGLI IQRLAGHMNF
     LLNCMAGAAL YGGSKIAIHS LTLPRYSLLA DVMAPMLQQQ SLVDFWRARD DMLEELEITP
     RPGPPTQGKR VVLEMPLPSD DLPAMTPSGQ VNNGAGLGRM VDMAKHLQHY RETIIGDDAS
     SSVGKRGLMK SGVGVRHALE AEKVIRYSPK ST