GH_ALHV1
ID GH_ALHV1 Reviewed; 733 AA.
AC O36372;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=22;
OS Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX NCBI_TaxID=654901;
OH NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA Ensser A., Pflanz R., Fleckenstein B.;
RT "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL J. Virol. 71:6517-6525(1997).
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; AF005370; AAC58069.1; -; Genomic_DNA.
DR PIR; T03117; T03117.
DR RefSeq; NP_065521.1; NC_002531.1.
DR SMR; O36372; -.
DR GeneID; 911757; -.
DR KEGG; vg:911757; -.
DR Proteomes; UP000000941; 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..14
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 15..733
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000436646"
FT TOPO_DOM 15..707
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 729..733
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 185..249
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 561
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 612
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ SEQUENCE 733 AA; 83007 MW; 9FD3E77EC47A237F CRC64;
MLFLILLCVT GAQAITTPAP PRPATTTPRR GVTSAPLIVP ASSSELIVTL DGTFHSVTID
MTEIRQYVRQ EIIEALWNAS HVFESLETTY NRYKDVYRFT DQSIRVNTRG KLSTCKEVNK
STEVSFYKSI TSQTINGKYD GDLGISNHQL GQQLFFYVMN VFPVENAFYP VRKHVVYSSL
SLADGAYQLA GMATTNYVSL VVVRKISSTV THEATIVFGN KKLLPSMRGS ITKYDISLVN
SDAEELLLLT SQKDYEYFSK NLFPQNWTDV FSLITSHTVG ELAQILQTSV VDFARKGRCR
SVHFNSHFLT TYLAVLSLYY KMGTEFVSKN ERQISLQCIL PKLYEANVCF DMVHRCFTSQ
YTRGFDSDGI NRLSAAILGS MPFEPNQGLS VPTNWFLQTL YFVDGNLDPQ NKGLHGITLI
LMDIYGRYVV NFTLTPEDRE TLFYVYNALR GRKHLSTTMK NKYVSLIYCY TTSMCSATEL
AWGIEYWGEE STHSAHHSFS PCFMSLRFDY TLEKLNIEGS QDVKLTQTQL SNGVSAMYSL
LTAKSSTWTI DSLSIKPCIY NASFVKMIVP FTNVSYVISQ GVAAPGTTYD VAETFLKSSM
VITVVSNSEC YNLTASKEIL KIPVVYNMTH PRIKCQLCDS VVISYDEYDG LQTMVYISNY
KVQQDLFSDY SIFFDFNNMH THYLLLMNNG TLFEIRGLYA NRAMNIIIIL LFTIAALAGV
FIVYKIVMYM TFK
