EP84_HCMVA
ID EP84_HCMVA Reviewed; 684 AA.
AC P17151; O10417; O10418; O12567; P16768; P87888; Q7M6T1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 29-SEP-2021, entry version 65.
DE RecName: Full=Early phosphoprotein p84;
DE Contains:
DE RecName: Full=p20;
DE Contains:
DE RecName: Full=p26;
DE Contains:
DE RecName: Full=p28;
GN Name=UL112/UL113;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM P84).
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P34; P43; P50 AND P84).
RA Wang S.-K., Duh C.-Y.;
RT "Regulation of major immediate early gene promoter by early phosphoproteins
RT of human cytomegalovirus.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=2824853; DOI=10.1128/jvi.62.1.331-340.1988;
RA Wright D.A., Staprans S.I., Spector D.H.;
RT "Four phosphoproteins with common amino termini are encoded by human
RT cytomegalovirus AD169.";
RL J. Virol. 62:331-340(1988).
RN [6]
RP ALTERNATIVE SPLICING.
RX PubMed=2542619; DOI=10.1128/jvi.63.7.3117-3127.1989;
RA Wright D.A., Spector D.H.;
RT "Posttranscriptional regulation of a class of human cytomegalovirus
RT phosphoproteins encoded by an early transcription unit.";
RL J. Virol. 63:3117-3127(1989).
RN [7]
RP IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [8]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(2004).
RN [9]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16501081; DOI=10.1128/jvi.80.6.2718-2727.2006;
RA Park M.-Y., Kim Y.-E., Seo M.-R., Lee J.-R., Lee C.H., Ahn J.-H.;
RT "Interactions among four proteins encoded by the human cytomegalovirus
RT UL112-113 region regulate their intranuclear targeting and the recruitment
RT of UL44 to prereplication foci.";
RL J. Virol. 80:2718-2727(2006).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=19656965; DOI=10.1099/vir.0.013037-0;
RA Wang S.K., Hu C.H., Lu M.C., Duh C.Y., Liao P.C., Tyan Y.C.;
RT "Novel virus-associated proteins encoded by UL112-113 of human
RT cytomegalovirus.";
RL J. Gen. Virol. 90:2840-2848(2009).
RN [11]
RP CLEAVAGE BY HOST CAPN1 AND CAPN2.
RX PubMed=25564485; DOI=10.1099/vir.0.000040;
RA Wang S.K., Jiang M.J., Lin S.R., Chen M.Y., Wang H.H., Duh C.Y.;
RT "Calpains mediate the proteolytic modification of human cytomegalovirus
RT UL112-113 proteins.";
RL J. Gen. Virol. 96:1115-1126(2015).
CC -!- FUNCTION: Promotes efficient viral DNA replication. Recruits the DNA
CC polymerase processivity factor to pre-replication foci.
CC {ECO:0000269|PubMed:16501081}.
CC -!- SUBUNIT: Isoforms p34, p43, p50 and p84 self-interact and interact with
CC each other via a shared N-terminal region; these interactions play an
CC important role in their intranuclear targeting and in the recruitment
CC of UL44 to subnuclear sites for viral replication.
CC {ECO:0000269|PubMed:16501081}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16501081,
CC ECO:0000269|PubMed:2824853}. Virion {ECO:0000269|PubMed:2824853}.
CC Note=Found in subnuclear structures known as promyelocytic leukemia
CC oncogenic domains (PODs) or nuclear domain 10 (ND10) during the early
CC stages of viral infection (PubMed:16501081).
CC -!- SUBCELLULAR LOCATION: [p20]: Virion {ECO:0000269|PubMed:19656965}.
CC -!- SUBCELLULAR LOCATION: [p26]: Virion {ECO:0000269|PubMed:19656965}.
CC -!- SUBCELLULAR LOCATION: [p28]: Virion {ECO:0000269|PubMed:19656965}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Isoforms 1, 2, 3 and 4 share a common N-terminus.;
CC Name=p84; Synonyms=84 kDa phosphoprotein;
CC IsoId=P17151-1; Sequence=Displayed;
CC Name=p50; Synonyms=50 kDa phosphoprotein;
CC IsoId=P17151-2; Sequence=VSP_034769, VSP_034772;
CC Name=p43; Synonyms=43 kDa phosphoprotein;
CC IsoId=P17151-3; Sequence=VSP_034770, VSP_034771;
CC Name=p34; Synonyms=34 kDa phosphoprotein;
CC IsoId=P17151-4; Sequence=VSP_034767, VSP_034768;
CC -!- PTM: The isoforms p34, p43, p50 and p84 are cleaved by host calpain-
CC 1/CAPN1 and calpain-2/CAPN2 to generate p20, p26 and p28.
CC -!- MISCELLANEOUS: [Isoform p43]: Most abundant product which level of
CC expression remains constant throughout infection. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the herpesviridae U79/UL112 family.
CC {ECO:0000305}.
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DR EMBL; X17403; CAA35315.1; -; Genomic_DNA.
DR EMBL; U57431; AAB53250.1; -; mRNA.
DR EMBL; U57432; AAB53251.1; -; mRNA.
DR EMBL; U57433; AAB53252.1; -; mRNA.
DR EMBL; U57434; AAB53253.1; -; mRNA.
DR EMBL; BK000394; DAA00103.1; -; Genomic_DNA.
DR PIR; S09860; S09860.
DR PIR; S09880; S09880.
DR SMR; P17151; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR InterPro; IPR004138; U79_P34.
DR Pfam; PF03064; U79_P34; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Early protein; Host nucleus; Phosphoprotein;
KW Reference proteome; Virion.
FT CHAIN 1..684
FT /note="Early phosphoprotein p84"
FT /id="PRO_0000116328"
FT CHAIN 1..243
FT /note="p28"
FT /evidence="ECO:0000305|PubMed:25564485"
FT /id="PRO_0000438161"
FT CHAIN 1..231
FT /note="p26"
FT /evidence="ECO:0000305|PubMed:25564485"
FT /id="PRO_0000438162"
FT CHAIN 1..200
FT /note="p20"
FT /evidence="ECO:0000305|PubMed:25564485"
FT /id="PRO_0000438163"
FT REGION 166..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 261..264
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 177..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 254..268
FT /note="SPPLREAKRQKTTAQ -> ESRPSSRHGAFRVDS (in isoform p34)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034767"
FT VAR_SEQ 269..684
FT /note="Missing (in isoform p34)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034768"
FT VAR_SEQ 346..423
FT /note="GALLLPIERGAVVSSPSSTSPSSLLSLPRPSSAHSAGETVQESEAAATAAAA
FT GLMMMRRMRRAPAEAAEAPPQSEEEN -> DSCQRRRAGLSSSTTAASRGPPQLSPQPA
FT LAPQQPHVRHSSPPVLYPQVPSPVSRPLPPQSKHQLLLPGPCVKSSPTW (in
FT isoform p50)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034769"
FT VAR_SEQ 347..358
FT /note="ALLLPIERGAVV -> IRGASASSQSAF (in isoform p43)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034770"
FT VAR_SEQ 359..684
FT /note="Missing (in isoform p43)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034771"
FT VAR_SEQ 424..684
FT /note="Missing (in isoform p50)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034772"
SQ SEQUENCE 684 AA; 70272 MW; F3325CE2E29EF449 CRC64;
MDLPTTVVRK YWTFANPNRI LHQSVNQTFD VRQFVFDTAR LVNCVDGDGK VLHLNKGWLC
ATIMQHGEAS AGAKTQQGFM SIDITGDGEL QEHLFVRGGI VFNKSVSSVV GSSGPNESAL
LTMISENGNL QVTYVRHYLK NHGESSSGGG GCGAASTASA VCVSSLGGSG GTRDGPSAEE
QQRRRQEQRH EERRKKSSSS AGGGGGGGAG GGGGGGGSGG QHSSDSANGL LRDPRLMNRQ
KERRPPPSSE NDGSPPLREA KRQKTTAQHE GHGGGGKNET EQQSGGAGGG GGGGSGRMSL
PLDTSEAVAF LNYSSSSSAV SSSSNNHHHH HHHHNAVTDV AAGTDGALLL PIERGAVVSS
PSSTSPSSLL SLPRPSSAHS AGETVQESEA AATAAAAGLM MMRRMRRAPA EAAEAPPQSE
EENDSTTPVS NCRVPPNSQE SAAPQPPRSP RFDDIIQSLT KMLNDCKEKR LCDLPLVSSR
LLPETSGGTV VVNHSSVART AAAVSAAGVG PPAAACPPLV TTGVVPSGSV AGVAPVAAAI
ETPAAPPRPV CEIKPYVVNP VVATAAAASN SSSSSSAPLP PPPPPSGGRR GRARNNTRGG
GGGGGGRNSR RQAASSSSSS SRRSRRRNNR HEDEEDNDPL LRLSQVAGNG RRRGPSFLED
GLEIIDPSEE AAIAAASIAA FFDD
