PP150_HCMVM
ID PP150_HCMVM Reviewed; 1049 AA.
AC Q6SW99; D2K3K0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 54.
DE RecName: Full=Tegument protein pp150;
GN Name=UL32;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
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:0000250|UniProtKB:P08318}.
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:0000250|UniProtKB:P08318}.
CC -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P08318}.
CC Host cytoplasm {ECO:0000250|UniProtKB:P08318}. Host nucleus
CC {ECO:0000250|UniProtKB:P08318}. Note=Found initially localized in the
CC host nucleus, associated either with the nuclear membrane or with viral
CC assembly regions, and later in the host cytoplasm.
CC {ECO:0000250|UniProtKB:P08318}.
CC -!- PTM: Phosphorylated by host CCNA2. {ECO:0000250|UniProtKB:P08318}.
CC -!- SIMILARITY: Belongs to the herpesviridae large structural
CC phosphoprotein family. {ECO:0000305}.
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DR EMBL; AY446894; AAR31597.1; -; Genomic_DNA.
DR RefSeq; YP_081491.1; NC_006273.2.
DR SMR; Q6SW99; -.
DR PRIDE; Q6SW99; -.
DR DNASU; 3077422; -.
DR GeneID; 3077422; -.
DR KEGG; vg:3077422; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; 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:0019028; C:viral capsid; TAS:Reactome.
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 3: Inferred from homology;
KW Glycoprotein; Host cytoplasm; Host nucleus; Host-virus interaction;
KW Phosphoprotein; Reference proteome; Virion; Virion tegument.
FT CHAIN 1..1049
FT /note="Tegument protein pp150"
FT /id="PRO_0000418267"
FT REGION 397..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 922
FT /note="O-linked (GlcNAc) serine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 953
FT /note="O-linked (GlcNAc) serine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1049 AA; 112759 MW; 871A6044F7406D84 CRC64;
MSLQFIGLQR RDVVALVNFL RHLTQKPDVD LEAHPKILKK CGEKRLHRRT VLFNELMLWL
GYYRELRFHN PDLSSVLEEF EVRCAAVARR GYTYPFGDRG KARDHLAVLD RTEFDTDVRH
DAEIVERALV SAVILAKMSV RETLVTAIGQ TEPIAFVHLK DTEVQRIEEN LEGVRRNMFC
AKPLDLNLDR HANTALVNAV NKLVYTGRLI MNVRRSWEEL ERKCLARIQE RCKLLVKELR
MCLSFDSNYC RNILKHAVEN GDSADTLLEL LIEDFDIYVD SFPQSAHTFL GARSPSLEFD
DDANLLSLGG GSAFSSVPKK HVPTQPLDGW SWIASPWKGH KPFRFEAHGS LAPAAEAHAA
RSAAVGYYDE EEKRRERQKR VDDEVVQREK QQLKAWEERQ QNLQQRQQQP PPPTRKPGAS
RRLFGSSADE DDDDDDDDEK NIFTPIKKPG TSGKGAASGG GVSSIFSGLL SSGSQKPTSG
PLNIPQQQQR HAAFSLVSPQ VTKASPGRVR RDSAWDVRPL TETRGDLFSG DEDSDSSDGY
PPNRQDPRFT DTLVDITDTE TSAKPPVTTA YKFEQPTLTF GAGVNVPAGA GAAILTPTPV
NPSTAPAPAP TPTFAGTQTP VNGNSPWAPT APLPGDMNPA NWPRERAWAL KNPHLAYNPF
RMPTTSTASQ NTVSTTPRRP STPRAAVTQT ASRDAADEVW ALRDQTAESP VEDSEEEDDD
SSDTGSVVSL GHTTPSSDYN NDVISPPSQT PEQSTPSRIR KAKLSSPMTT TSTSQKPVLG
KRVATPHASA RAQTVTSTPV QGRLEKQVSG TPSTVPATLL QPQPASSKTT SSRNVTSGAG
TSSASSARQP SASASVLSPT EDDVVSPATS PLSMLSSASP SPAKSAPPSP VKGRGSRVGV
PSLKPTLGGK AVVGRPPSVP VSGSAPGRLS GSSRAASTTP TYPAVTTVYP PSSTAKSSVS
NAPPVASPSI LKPGASAALQ SRRSTGIAAV GSPVKSTTGM KTVAFDLSSP QKSGTGPQPG
SAGMGGAKTP SDAVQNILQK IEKIKNTEE
