UL13_HHV11
ID UL13_HHV11 Reviewed; 518 AA.
AC P04290; B9VQE0; Q09IC0;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Serine/threonine-protein kinase UL13;
DE EC=2.7.11.1;
DE AltName: Full=Virion protein VMW57;
GN ORFNames=UL13;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3010237; DOI=10.1093/nar/14.8.3435;
RA McGeoch D.J., Dolan A., Frame M.C.;
RT "DNA sequence of the region in the genome of herpes simplex virus type 1
RT containing the exonuclease gene and neighbouring genes.";
RL Nucleic Acids Res. 14:3435-3448(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nonneuroinvasive mutant HF10;
RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT "Determination and analysis of the DNA sequence of highly attenuated herpes
RT simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL Microbes Infect. 9:142-149(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROBABLE FUNCTION.
RX PubMed=2535748; DOI=10.1128/jvi.63.1.450-455.1989;
RA Smith R.F., Smith T.F.;
RT "Identification of new protein kinase-related genes in three herpesviruses,
RT herpes simplex virus, varicella-zoster virus, and Epstein-Barr virus.";
RL J. Virol. 63:450-455(1989).
RN [6]
RP AUTOPHOSPHORYLATION.
RX PubMed=1311359; DOI=10.1099/0022-1317-73-2-303;
RA Cunningham C., Davison A.J., Dolan A., Frame M.C., McGeoch D.J.,
RA Meredith D.M., Moss H.W., Orr A.C.;
RT "The UL13 virion protein of herpes simplex virus type 1 is phosphorylated
RT by a novel virus-induced protein kinase.";
RL J. Gen. Virol. 73:303-311(1992).
RN [7]
RP FUNCTION IN PHOSPHORYLATION OF GE AND GI.
RX PubMed=9454715; DOI=10.1006/viro.1997.8963;
RA Ng T.I., Ogle W.O., Roizman B.;
RT "UL13 protein kinase of herpes simplex virus 1 complexes with glycoprotein
RT E and mediates the phosphorylation of the viral Fc receptor: glycoproteins
RT E and I.";
RL Virology 241:37-48(1998).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF US3.
RC STRAIN=F;
RX PubMed=16415024; DOI=10.1128/jvi.80.3.1476-1486.2006;
RA Kato A., Yamamoto M., Ohno T., Tanaka M., Sata T., Nishiyama Y.,
RA Kawaguchi Y.;
RT "Herpes simplex virus 1-encoded protein kinase UL13 phosphorylates viral
RT Us3 protein kinase and regulates nuclear localization of viral envelopment
RT factors UL34 and UL31.";
RL J. Virol. 80:1476-1486(2006).
RN [9]
RP FUNCTION, AND IDENTIFICATION OF SUBSTRATE PROTEINS.
RX PubMed=17913541; DOI=10.1016/j.micinf.2007.07.008;
RA Asai R., Ohno T., Kato A., Kawaguchi Y.;
RT "Identification of proteins directly phosphorylated by UL13 protein kinase
RT from herpes simplex virus 1.";
RL Microbes Infect. 9:1434-1438(2007).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=F;
RX PubMed=18596102; DOI=10.1128/jvi.00904-08;
RA Loret S., Guay G., Lippe R.;
RT "Comprehensive characterization of extracellular herpes simplex virus type
RT 1 virions.";
RL J. Virol. 82:8605-8618(2008).
CC -!- FUNCTION: Multifunctional serine/threonine kinase that plays a role in
CC several processes including egress of virus particles from the nucleus,
CC modulation of the actin cytoskeleton and regulation of viral and
CC cellular gene expression. Regulates the nuclear localization of viral
CC envelopment factors UL34 and UL31, by phosphorylating the US3 kinase,
CC indicating a role in nuclear egress. Disrupts host nuclear lamins,
CC including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed
CC of glycoproteins E (gE) and I (gI). Phosphorylation of glycoprotein E
CC (gE) by UL13 alters its subcellular localization, from the host early
CC endosome to the plasma membrane. Participates in the transcriptional
CC regulation of cellular and viral mRNAs mainly by phosphorylating the
CC viral transcriptional regulator ICP22. Additional substrates have been
CC identified, including UL41, UL49 or host EF1D.
CC {ECO:0000269|PubMed:16415024, ECO:0000269|PubMed:17913541,
CC ECO:0000269|PubMed:9454715}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000269|PubMed:18596102}.
CC Host nucleus {ECO:0000250}.
CC -!- PTM: Autophosphorylated.
CC -!- MISCELLANEOUS: Displays a substrate specificity similar to host CDC2.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X03839; CAA27454.1; -; Genomic_DNA.
DR EMBL; X14112; CAA32326.1; -; Genomic_DNA.
DR EMBL; DQ889502; ABI63475.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62235.1; -; Genomic_DNA.
DR PIR; A03738; WMBE71.
DR RefSeq; YP_009137087.1; NC_001806.2.
DR BioGRID; 971421; 1.
DR IntAct; P04290; 1.
DR MINT; P04290; -.
DR PRIDE; P04290; -.
DR DNASU; 2703383; -.
DR GeneID; 2703383; -.
DR KEGG; vg:2703383; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Host nucleus; Host-virus interaction; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Virion; Virion tegument.
FT CHAIN 1..518
FT /note="Serine/threonine-protein kinase UL13"
FT /id="PRO_0000086187"
FT DOMAIN 151..518
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 157..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VARIANT 35
FT /note="V -> I (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 53
FT /note="D -> N (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 63
FT /note="S -> C (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 94
FT /note="T -> A (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 164
FT /note="D -> E (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 198
FT /note="V -> A (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 344
FT /note="T -> I (in strain: 17 syn+)"
FT VARIANT 376
FT /note="D -> E (in strain: Nonneuroinvasive mutant HF10)"
SQ SEQUENCE 518 AA; 57197 MW; EEBBF813B97EF4B8 CRC64;
MDESRRQRPA GHVAANLSPQ GARQRSFKDW LASYVHSNPH GASGRPSGPS LQDAAVSRSS
HGSRHRSGLR ERLRAGLSRW RMSRSSHRRA SPETPGTAAK LNRPPLRRSQ AALTAPPSSP
SHILTLTRIR KLCSPVFAIN PALHYTTLEI PGARSFGGSG GYGDVQLIRE HKLAVKTIKE
KEWFAVELIA TLLVGECVLR AGRTHNIRGF IAPLGFSLQQ RQIVFPAYDM DLGKYIGQLA
SLRTTNPSVS TALHQCFTEL ARAVVFLNTT CGISHLDIKC ANILVMLRSD AVSLRRAVLA
DFSLVTLNSN STIARGQFCL QEPDLKSPRM FGMPTALTTA NFHTLVGHGY NQPPELLVKY
LNNERAEFTN HRLKHDVGLA VDLYALGQTL LELVVSVYVA PSLGVPVTRF PGYQYFNNQL
SPDFALALLA YRCVLHPALF VNSAETNTHG LAYDVPEGIR RHLRNPKIRR AFTDRCINYQ
HTHKAILSSV ALPPELKPLL VLVSRLCHTN PCARHALS
