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Envelope glycoprotein H (gH)

 GH_ALHV1                Reviewed;         733 AA.
O36372;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
23-MAY-2018, entry version 54.
RecName: Full=Envelope glycoprotein H {ECO:0000255|HAMAP-Rule:MF_04033};
Short=gH {ECO:0000255|HAMAP-Rule:MF_04033};
Flags: Precursor;
Name=gH {ECO:0000255|HAMAP-Rule:MF_04033}; Synonyms=22;
Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal
fever virus).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Gammaherpesvirinae; Macavirus.
NCBI_TaxID=654901;
NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=9261371;
Ensser A., Pflanz R., Fleckenstein B.;
"Primary structure of the alcelaphine herpesvirus 1 genome.";
J. Virol. 71:6517-6525(1997).
-!- FUNCTION: The heterodimer glycoprotein H-glycoprotein L is
required for the fusion of viral and plasma membranes leading to
virus entry into the host cell. Following initial binding to host
receptor, membrane fusion is mediated by the fusion machinery
composed of gB and the heterodimer gH/gL. May also be involved in
the fusion between the virion envelope and the outer nuclear
membrane during virion morphogenesis. {ECO:0000255|HAMAP-
Rule:MF_04033}.
-!- SUBUNIT: Interacts with glycoprotein L (gL); this interaction is
necessary for the correct processing and cell surface expression
of gH. The heterodimer gH/gL seems to interact with gB trimers
during fusion. {ECO:0000255|HAMAP-Rule:MF_04033}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04033}; Single-pass type I membrane protein
{ECO:0000255|HAMAP-Rule:MF_04033}. Host cell membrane
{ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host endosome membrane
{ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04033}. Note=During virion
morphogenesis, this protein probably accumulates in the endosomes
and trans-Golgi where secondary envelopment occurs. It is probably
transported to the cell surface from where it is endocytosed and
directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-
Rule:MF_04033}.
-!- PTM: N-glycosylated, O-glycosylated, and sialylated.
{ECO:0000255|HAMAP-Rule:MF_04033}.
-!- SIMILARITY: Belongs to the herpesviridae glycoprotein H family.
{ECO:0000255|HAMAP-Rule:MF_04033}.
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EMBL; AF005370; AAC58069.1; -; Genomic_DNA.
PIR; T03117; T03117.
RefSeq; NP_065521.1; NC_002531.1.
PRIDE; O36372; -.
GeneID; 911757; -.
KEGG; vg:911757; -.
OrthoDB; VOG0900004Y; -.
Proteomes; UP000000941; Genome.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
Gene3D; 2.60.40.3190; -; 1.
HAMAP; MF_04033; HSV_GH; 1.
InterPro; IPR003493; Herpes_gH.
InterPro; IPR035305; Herpes_glycoH_C.
InterPro; IPR038172; Herpes_glycoH_C_sf.
Pfam; PF17488; Herpes_glycoH_C; 1.
3: Inferred from homology;
Complete proteome; Fusion of virus membrane with host cell membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host endosome; Host membrane; Membrane;
Reference proteome; Sialic acid; Signal; Transmembrane;
Transmembrane helix; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 14 {ECO:0000255|HAMAP-Rule:MF_04033}.
CHAIN 15 733 Envelope glycoprotein H.
{ECO:0000255|HAMAP-Rule:MF_04033}.
/FTId=PRO_0000436646.
TOPO_DOM 15 707 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04033}.
TRANSMEM 708 728 Helical. {ECO:0000255|HAMAP-
Rule:MF_04033}.
TOPO_DOM 729 733 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04033}.
REGION 185 249 Interaction with gL. {ECO:0000255|HAMAP-
Rule:MF_04033}.
COMPBIAS 246 249 Poly-Leu.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04033}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04033}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04033}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04033}.
CARBOHYD 561 561 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04033}.
CARBOHYD 573 573 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04033}.
CARBOHYD 612 612 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04033}.
CARBOHYD 627 627 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04033}.
CARBOHYD 689 689 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04033}.
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


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