GH_HHV6Z
ID GH_HHV6Z Reviewed; 694 AA.
AC P52543;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Envelope glycoprotein H {ECO:0000255|HAMAP-Rule:MF_04033};
DE Short=gH {ECO:0000255|HAMAP-Rule:MF_04033};
DE Flags: Precursor;
GN Name=gH {ECO:0000255|HAMAP-Rule:MF_04033}; Synonyms=KA9L, U48;
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).
CC -!- FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for
CC the fusion of viral and plasma membranes leading to virus entry into
CC the host cell. Following initial binding to host receptor, membrane
CC fusion is mediated by the fusion machinery composed of gB and the
CC heterodimer gH/gL. May also be involved in the fusion between the
CC virion envelope and the outer nuclear membrane during virion
CC morphogenesis. {ECO:0000255|HAMAP-Rule:MF_04033}.
CC -!- SUBUNIT: Interacts with glycoprotein L (gL); this interaction is
CC necessary for the correct processing and cell surface expression of gH.
CC The heterodimer gH/gL seems to interact with gB trimers during fusion.
CC {ECO:0000255|HAMAP-Rule:MF_04033}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04033}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04033};
CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}.
CC Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Note=During
CC virion morphogenesis, this protein probably accumulates in the
CC endosomes and trans-Golgi where secondary envelopment occurs. It is
CC probably transported to the cell surface from where it is endocytosed
CC and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-
CC Rule:MF_04033}.
CC -!- PTM: N-glycosylated, O-glycosylated, and sialylated.
CC {ECO:0000255|HAMAP-Rule:MF_04033}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein H family.
CC {ECO:0000255|HAMAP-Rule:MF_04033}.
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DR EMBL; AF157706; AAB06346.1; -; Genomic_DNA.
DR PIR; T44195; T44195.
DR RefSeq; NP_050229.1; NC_000898.1.
DR SMR; P52543; -.
DR PRIDE; P52543; -.
DR ABCD; P52543; 1 sequenced antibody.
DR DNASU; 1497050; -.
DR GeneID; 1497050; -.
DR KEGG; vg:1497050; -.
DR Proteomes; UP000006930; Genome.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.3190; -; 1.
DR HAMAP; MF_04033; HSV_GH; 1.
DR InterPro; IPR003493; Herpes_gH.
DR InterPro; IPR035305; Herpes_glycoH_C.
DR InterPro; IPR038172; Herpes_glycoH_C_sf.
DR Pfam; PF17488; Herpes_glycoH_C; 1.
PE 3: Inferred from homology;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host endosome; Host membrane; Membrane;
KW Reference proteome; Sialic acid; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 17..694
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000436660"
FT TOPO_DOM 17..671
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 693..694
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 174..234
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ SEQUENCE 694 AA; 79574 MW; 030C3C62FBDC39E5 CRC64;
MLFRLWVFVL LTPCYSWRPW TISDESHCKN GNSENPIVRP GFITFNFYTK NDTRIYQVPK
CLLGSDITYH LFDAINTTES LTNYEKRVTR FYEPPMNDIL RLSTVPAVKQ FNLDHSIQPQ
IVYSLNLYPS HGIYYIRVVE VRQMQYDNVS CKLPNSLNEL IFPVQVRCAK ITRYAGENIY
THFFTPDFMI LYIQNPAGDL TMMYGNTTDI NFKAPYRKSS FIFKQTLTDD LLLIVEKDVV
DEEYRFISDA TFVDETLDDV DEVEALLLKF NNLGIQTLLR GDCKKPDYAG IPQMMFLYGI
VHFSYSTKNT GPMPVLRVLK THENLLSIDS FVNRCVNVSE GTIQYPKMKE FLKYEPSDYS
YITKNKSIPV STLLTYLATA YETNVTISRY KWSDIANTLQ KIYEKHMFFT NLTFSDRETL
FMLAEIANFI PADERMQRHM QLLIGNLCNP VEIVSWAHML TADKAPNLEN IYSPCASPVR
RDVTNSFVKT VLTYASLDRY RSDMMEMLSV YRPPDMARVA AIQCLSPSEP AASLPLPNVT
FVISPSYVIK GVSLTITTTI VATSIIITAI PLNSTCVSTN YKYAGQDLLV LRNISSQTCE
FCQSVVMEYD DIDGPLQYIY IKNIDELKTL TDPNNNLLVP NTRTHYLLLA KNGSVFEMSE
VGIDIDQVSI ILVIIYVLIA IIALFGLYRL IRLC
