PP150_HCMVA
ID PP150_HCMVA Reviewed; 1048 AA.
AC P08318; Q7M6Q1;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Large structural phosphoprotein;
DE AltName: Full=150 kDa matrix phosphoprotein;
DE AltName: Full=150 kDa phosphoprotein;
DE Short=pp150;
DE AltName: Full=Basic phosphoprotein;
DE Short=BPP;
DE AltName: Full=Phosphoprotein UL32;
DE AltName: Full=Tegument protein UL32;
GN Name=UL32;
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 [GENOMIC DNA].
RX PubMed=3033266; DOI=10.1128/jvi.61.5.1358-1367.1987;
RA Jahn G., Kouzarides T., Mach M., Scholl B.-C., Plachter B., Traupe B.,
RA Preddie E., Satchwell S.C., Fleckenstein B., Barrell B.G.;
RT "Map position and nucleotide sequence of the gene for the large structural
RT phosphoprotein of human cytomegalovirus.";
RL J. Virol. 61:1358-1367(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3]
RP GLYCOSYLATION AT SER-921 AND SER-952.
RX PubMed=7966627; DOI=10.1128/jvi.68.12.8339-8349.1994;
RA Greis K.D., Gibson W.G., Hart G.W.;
RT "Site-specific glycosylation of the human cytomegalovirus tegument basic
RT phosphoprotein (UL32) at serine 921 and serine 952.";
RL J. Virol. 68:8339-8349(1994).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=9049366; DOI=10.1099/0022-1317-76-7-1591;
RA Hensel G., Meyer H., Gartner S., Brand G., Kern H.F.;
RT "Nuclear localization of the human cytomegalovirus tegument protein pp150
RT (ppUL32).";
RL J. Gen. Virol. 76:1591-1601(1995).
RN [9]
RP FUNCTION.
RX PubMed=16873276; DOI=10.1128/jvi.00457-06;
RA Aucoin D.P., Smith G.B., Meiering C.D., Mocarski E.S.;
RT "Betaherpesvirus-conserved cytomegalovirus tegument protein ppUL32 (pp150)
RT controls cytoplasmic events during virion maturation.";
RL J. Virol. 80:8199-8210(2006).
RN [10]
RP FUNCTION.
RX PubMed=18653449; DOI=10.1128/jvi.00533-08;
RA Tandon R., Mocarski E.S.;
RT "Control of cytoplasmic maturation events by cytomegalovirus tegument
RT protein pp150.";
RL J. Virol. 82:9433-9444(2008).
RN [11]
RP INTERACTION WITH HOST BICD1.
RX PubMed=20089649; DOI=10.1128/jvi.01776-09;
RA Indran S.V., Ballestas M.E., Britt W.J.;
RT "Bicaudal D1-dependent trafficking of human cytomegalovirus tegument
RT protein pp150 in virus-infected cells.";
RL J. Virol. 84:3162-3177(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST RAB6A AND BICD1.
RX PubMed=21411515; DOI=10.1128/jvi.02605-10;
RA Indran S.V., Britt W.J.;
RT "A role for the small GTPase Rab6 in assembly of human cytomegalovirus.";
RL J. Virol. 85:5213-5219(2011).
RN [13]
RP FUNCTION, AND INTERACTION WITH UL48A.
RX PubMed=23966856; DOI=10.1371/journal.ppat.1003525;
RA Dai X., Yu X., Gong H., Jiang X., Abenes G., Liu H., Shivakoti S.,
RA Britt W.J., Zhu H., Liu F., Zhou Z.H.;
RT "The smallest capsid protein mediates binding of the essential tegument
RT protein pp150 to stabilize DNA-containing capsids in human
RT cytomegalovirus.";
RL PLoS Pathog. 9:E1003525-E1003525(2013).
RN [14]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH HOST CCNA2.
RX PubMed=24101496; DOI=10.1073/pnas.1312235110;
RA Bogdanow B., Weisbach H., von Einem J., Straschewski S., Voigt S.,
RA Winkler M., Hagemeier C., Wiebusch L.;
RT "Human cytomegalovirus tegument protein pp150 acts as a cyclin A2-CDK-
RT dependent sensor of the host cell cycle and differentiation state.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:17510-17515(2013).
CC -!- FUNCTION: Participates in the last steps of viral maturation and
CC release. Associates with nuclear capsids prior to DNA encapsidation and
CC later preserves the integrity of nucleocapsids through secondary
CC envelopment at the assembly compartment. Interacts with host CCNA2 and
CC thereby blocks the onset of lytic gene expression to promote
CC establishment of a quiescent state of infection in undifferentiated
CC cells. {ECO:0000269|PubMed:16873276, ECO:0000269|PubMed:18653449,
CC ECO:0000269|PubMed:21411515, ECO:0000269|PubMed:23966856,
CC ECO:0000269|PubMed:24101496}.
CC -!- SUBUNIT: Interacts with host BICD1 and RAB6A. Interacts with small
CC capsid protein UL48A; this interaction links together the capsid and
CC pp150. Interacts with host CCNA2. {ECO:0000269|PubMed:20089649,
CC ECO:0000269|PubMed:21411515, ECO:0000269|PubMed:23966856,
CC ECO:0000269|PubMed:24101496}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000269|PubMed:9049366}.
CC Host cytoplasm {ECO:0000269|PubMed:21411515,
CC ECO:0000269|PubMed:9049366}. Host nucleus {ECO:0000269|PubMed:9049366}.
CC Note=Found initially localized in the host nucleus, associated either
CC with the nuclear membrane or with viral assembly regions, and later in
CC the host cytoplasm.
CC -!- PTM: Phosphorylated by host CCNA2. {ECO:0000269|PubMed:24101496}.
CC -!- SIMILARITY: Belongs to the herpesviridae large structural
CC phosphoprotein family. {ECO:0000305}.
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DR EMBL; M16022; AAA45992.1; -; Genomic_DNA.
DR EMBL; X17403; CAA35431.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00137.1; -; Genomic_DNA.
DR PIR; A29533; XPBEA9.
DR PDB; 5VKU; EM; 3.90 A; 0/1/2/3/4/5/6/7/8/9/v/w/x/y/z=1-285.
DR PDB; 7ET3; EM; 4.20 A; 1=1-1048.
DR PDB; 7LIV; EM; 3.60 A; 4/5/6=1-285.
DR PDB; 7LJ3; EM; 2.90 A; 0/4/5/6/7/8/9/y/z=1-285.
DR PDBsum; 5VKU; -.
DR PDBsum; 7ET3; -.
DR PDBsum; 7LIV; -.
DR PDBsum; 7LJ3; -.
DR SMR; P08318; -.
DR IntAct; P08318; 1.
DR GlyConnect; 323; 1 O-Linked glycan (2 sites).
DR PRIDE; P08318; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0072517; C:host cell viral assembly compartment; IDA:BHF-UCL.
DR GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR010340; Herpes_UL11/UL32.
DR Pfam; PF06070; Herpes_UL32; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Phosphoprotein; Reference proteome; Virion;
KW Virion tegument.
FT CHAIN 1..1048
FT /note="Large structural phosphoprotein"
FT /id="PRO_0000116302"
FT REGION 366..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 921
FT /note="O-linked (GlcNAc) serine; by host"
FT /evidence="ECO:0000269|PubMed:7966627"
FT /id="CAR_000179"
FT CARBOHYD 952
FT /note="O-linked (GlcNAc) serine; by host"
FT /evidence="ECO:0000269|PubMed:7966627"
FT /id="CAR_000195"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:7LJ3"
FT TURN 40..45
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 48..69
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 74..93
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:7LJ3"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 121..140
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 195..240
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:7LJ3"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:7LJ3"
SQ SEQUENCE 1048 AA; 112688 MW; 9C4DD60B4F56FF1D CRC64;
MSLQFIGLQR RDVVALVNFL RHLTQKPDVD LEAHPKILKK CGEKRLHRRT VLFNELMLWL
GYYRELRFHN PDLSSVLEEF EVRCVAVARR GYTYPFGDRG KARDHLAVLD RTEFDTDVRH
DAEIVERALV SAVILAKMSV RETLVTAIGQ TEPIAFVHLK DTEVQRIEEN LEGVRRNMFC
VKPLDLNLDR HANTALVNAV NKLVYTGRLI MNVRRSWEEL ERKCLARIQE RCKLLVKELR
MCLSFDSNYC RNILKHAVEN GDSADTLLEL LIEDFDIYVD SFPQSAHTFL GARSPSLEFD
DDANLLSLGG GSAFSSVPKK HVPTQPLDGW SWIASPWKGH KPFRFEAHGS LAPAAEAHAA
RSAAVGYYDE EEKRRERQKR VDDEVVQREK QQLKAWEERQ QNLQQRQQQP PPPARKPSAS
RRLFGSSADE DDDDDDDEKN IFTPIKKPGT SGKGAASGGG VSSIFSGLLS SGSQKPTSGP
LNIPQQQQRH AAFSLVSPQV TKASPGRVRR DSAWDVRPLT ETRGDLFSGD EDSDSSDGYP
PNRQDPRFTD TLVDITDTET SAKPPVTTAY KFEQPTLTFG AGVNVPAGAG AAILTPTPVN
PSTAPAPAPT PTFAGTQTPV NGNSPWAPTA PLPGDMNPAN WPRERAWALK NPHLAYNPFR
MPTTSTASQN TVSTTPRRPS TPRAAVTQTA SRDAADEVWA LRDQTAESPV EDSEEEDDDS
SDTGSVVSLG HTTPSSDYNN DVISPPSQTP EQSTPSRIRK AKLSSPMTTT STSQKPVLGK
RVATPHASAR AQTVTSTPVQ GRLEKQVSGT PSTVPATLLQ PQPASSKTTS SRNVTSGAGT
SSASSARQPS ASASVLSPTE DDVVSPATSP LSMLSSASPS PAKSAPPSPV KGRGSRVGVP
SLKPTLGGKA VVGRPPSVPV SGSAPGRLSG SSRAASTTPT YPAVTTVYPP SSTAKSSVSN
APPVASPSIL KPGASAALQS RRSTGTAAVG SPVKSTTGMK TVAFDLSSPQ KSGTGPQPGS
AGMGGAKTPS DAVQNILQKI EKIKNTEE
