GH_HHV8P
ID GH_HHV8P Reviewed; 730 AA.
AC F5HAK9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 35.
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=ORF22;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP FUNCTION.
RX PubMed=11932406; DOI=10.1128/jvi.76.9.4390-4400.2002;
RA Pertel P.E.;
RT "Human herpesvirus 8 glycoprotein B (gB), gH, and gL can mediate cell
RT fusion.";
RL J. Virol. 76:4390-4400(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH HOST EPHA2.
RX PubMed=22635007; DOI=10.1038/nm.2805;
RA Hahn A.S., Kaufmann J.K., Wies E., Naschberger E., Panteleev-Ivlev J.,
RA Schmidt K., Holzer A., Schmidt M., Chen J., Konig S., Ensser A., Myoung J.,
RA Brockmeyer N.H., Sturzl M., Fleckenstein B., Neipel F.;
RT "The ephrin receptor tyrosine kinase A2 is a cellular receptor for Kaposi's
RT sarcoma-associated herpesvirus.";
RL Nat. Med. 18:961-966(2012).
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 (By similarity). Targets host EPHA2 to promote KSHV
CC entry. {ECO:0000255|HAMAP-Rule:MF_04033, ECO:0000269|PubMed:11932406,
CC ECO:0000269|PubMed:22635007}.
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 (By similarity). When in complex with gL, interacts with host EPHA2;
CC this interaction triggers EPHA2 phosphorylation and endocytosis
CC allowing KSHV entry. {ECO:0000255|HAMAP-Rule:MF_04033,
CC ECO:0000269|PubMed:22635007}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF148805; ABD28873.1; -; Genomic_DNA.
DR RefSeq; YP_001129375.1; NC_009333.1.
DR SMR; F5HAK9; -.
DR PRIDE; F5HAK9; -.
DR ABCD; F5HAK9; 2 sequenced antibodies.
DR DNASU; 4961506; -.
DR GeneID; 4961506; -.
DR KEGG; vg:4961506; -.
DR Proteomes; UP000000942; 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; IDA:CACAO.
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 1: Evidence at protein level;
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..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 22..730
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000436655"
FT TOPO_DOM 22..706
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 728..730
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 190..254
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 274
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 556
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ SEQUENCE 730 AA; 81266 MW; B5DB4B733DDFE451 CRC64;
MQGLAFLAAL ACWRCISLTC GATGALPTTA TTITRSATQL INGRTNLSIE LEFNGTSFFL
NWQNLLNVIT EPALTELWTS AEVAEDLRVT LKKRQSLFFP NKTVVISGDG HRYTCEVPTS
SQTYNITKGF NYSALPGHLG GFGINARLVL GDIFASKWSL FARDTPEYRV FYPMNVMAVK
FSISIGNNES GVALYGVVSE DFVVVTLHNR SKEANETASH LLFGLPDSLP SLKGHATYDE
LTFARNAKYA LVAILPKDSY QTLLTENYTR IFLNMTESTP LEFTRTIQTR IVSIEARRAC
AAQEAAPDIF LVLFQMLVAH FLVARGIAEH RFVEVDCVCR QYAELYFLRR ISRLCMPTFT
TVGYNHTTLG AVAATQIARV SATKLASLPR SSQETVLAMV QLGARDGAVP SSILEGIAMV
VEHMYTAYTY VYTLGDTERK LMLDIHTVLT DSCPPKDSGV SEKLLRTYLM FTSMCTNIEL
GEMIARFSKP DSLNIYRAFS PCFLGLRYDL HPAKLRAEAP QSSALTRTAV ARGTSGFAEL
LHALHLDSLN LIPAINCSKI TADKIIATVP LPHVTYIISS EALSNAVVYE VSEIFLKSAM
FISAIKPDCS GFNFSQIDRH IPIVYNISTP RRGCPLCDSV IMSYDESDGL QSLMYVTNER
VQTNLFLDKS PFFDNNNLHI HYLWLRDNGT VVEIRGMYRR RAASALFLIL SFIGFSGVIY
FLYRLFSILY
