GO_HHV6Z
ID GO_HHV6Z Reviewed; 738 AA.
AC P52549;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 23-FEB-2022, entry version 64.
DE RecName: Full=130 kDa Glycoprotein O;
DE Short=gO-130K;
DE AltName: Full=Glycoprotein U47;
DE Contains:
DE RecName: Full=80 kDa Glycoprotein O;
DE Short=gO-80K;
DE Flags: Precursor;
GN Name=U47; Synonyms=KA8L;
OS Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7983761; DOI=10.1128/jvi.69.1.589-596.1995;
RA Stamey F.R., Dominguez G., Black J.B., Dambaugh T.R., Pellett P.E.;
RT "Intragenomic linear amplification of human herpesvirus 6B oriLyt suggests
RT acquisition of oriLyt by transposition.";
RL J. Virol. 69:589-596(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison with
RT human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
RN [3]
RP IDENTIFICATION IN COMPLEX WITH GLYCOPROTEIN L AND GLYCOPROTEIN H (80 KDA
RP GLYCOPROTEIN O), SUBCELLULAR LOCATION (80 KDA GLYCOPROTEIN O),
RP GLYCOSYLATION (80 KDA GLYCOPROTEIN O), AND GLYCOSYLATION (120 KDA
RP GLYCOPROTEIN O).
RC STRAIN=HST;
RX PubMed=15078943; DOI=10.1128/jvi.78.9.4609-4616.2004;
RA Mori Y., Akkapaiboon P., Yonemoto S., Koike M., Takemoto M., Sadaoka T.,
RA Sasamoto Y., Konishi S., Uchiyama Y., Yamanishi K.;
RT "Discovery of a second form of tripartite complex containing gH-gL of human
RT herpesvirus 6 and observations on CD46.";
RL J. Virol. 78:4609-4616(2004).
CC -!- SUBUNIT: [80 kDa Glycoprotein O]: Part of a gH-gL-gO complex.
CC {ECO:0000269|PubMed:15078943}.
CC -!- SUBCELLULAR LOCATION: [80 kDa Glycoprotein O]: Virion
CC {ECO:0000269|PubMed:15078943}. Host cell membrane
CC {ECO:0000250|UniProtKB:P30005}.
CC -!- PTM: 120 kDa Glycoprotein O: A shorter mature protein, gO-80K, is
CC produced probably by proteolytic cleavage.
CC {ECO:0000250|UniProtKB:P30005}.
CC -!- PTM: 120 kDa Glycoprotein O: Modified with high mannose-
CC oligosaccharides. {ECO:0000269|PubMed:15078943}.
CC -!- PTM: [80 kDa Glycoprotein O]: N-glycosylated with complex glycans.
CC {ECO:0000269|PubMed:15078943}.
CC -!- SIMILARITY: Belongs to the herpesviridae U47 family. {ECO:0000305}.
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DR EMBL; AF157706; AAB06345.1; -; Genomic_DNA.
DR PIR; T44194; T44194.
DR RefSeq; NP_050228.1; NC_000898.1.
DR PRIDE; P52549; -.
DR DNASU; 1497049; -.
DR GeneID; 1497049; -.
DR KEGG; vg:1497049; -.
DR Proteomes; UP000006930; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR InterPro; IPR008645; Roseolovirus_U47.
DR Pfam; PF05467; Herpes_U47; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Host cell membrane; Host membrane; Membrane;
KW Reference proteome; Signal; Virion.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..738
FT /note="130 kDa Glycoprotein O"
FT /id="PRO_0000038317"
FT CHAIN 24..?
FT /note="80 kDa Glycoprotein O"
FT /id="PRO_0000445359"
FT REGION 240..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 738 AA; 82991 MW; EA6BCE87D45BE77A CRC64;
MLHISRLGLF LALFAIVMHS VNLIKYTSDP LEAFKTVNRH NWSDEQREHF YDLRNLYTTF
CQRNLSLDCF TQILTNVFSW NIRDLQCKSA VNLSPLQNLP RAETKIVLSS TAANKSIVAS
SFSLFYLLFA TLSTYTADPP CVELLPFKIL GTQLFDIKLT DESLQMAISK FSNSNLTRSL
TPFTPEIFFN YTSFVYFLLY NTTSCIRSND QYFEHSPKPI NVTTSFGRAI VNFHSILTTT
PSSTPSSTSA SITSPHIPST NTPTPEPSPV TKNFTELQTD TIKVTPNTPT ITAQTTESIK
KVVKRSDFPR PMYTPTDIPT LTIRRNATIK TEQNTENPTE NPKSPPKPTN FENTTIRIPE
TFESTTVATN TTQKLESTTF ATTIGIEEIS DNIYSSPKNS IYLKSKSQQS TTKFTDTEHT
TPILKFTTWQ DAARTYMSHN TEVQNMTENF IKISLGETMG ITPKEPTNPT QLLNVKNQTE
YANETHSTEV QTVKTFKEDR FQRTTLKSSS EPPTVQTLSV TPKKKLPSNV TAKTEVQVTN
NALPSSNSSH SITKVTEEPK QNRMSASTHG EINHTEIPRM TPILNAHTWE KSTTPQWPFT
AETSLTTSSK SAILTWSNLL TTPKEPLTNT SLRSTNHITT QLTTSNRTQS AKLTKAHVSS
QTTNIYPQTI TERSTDVKKK SSTESREANK TLPGNDYRVT DKNSHNHPDN LTTKAYSTQN
ATHYTYNERH DLNNTDST
