GH_HCMVA
ID GH_HCMVA Reviewed; 743 AA.
AC P12824; Q7M6L7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=UL75;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2831402; DOI=10.1128/jvi.62.4.1416-1422.1988;
RA Cranage M.P., Smith G.L., Bell S.E., Hart H., Brown C., Bankier A.T.,
RA Tomlinson P., Barrell B.G., Minson T.C.;
RT "Identification and expression of a human cytomegalovirus glycoprotein with
RT homology to the Epstein-Barr virus BXLF2 product, varicella-zoster virus
RT gpIII, and herpes simplex virus type 1 glycoprotein H.";
RL J. Virol. 62:1416-1422(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP PROTEIN SEQUENCE OF 32-44, AND IDENTIFICATION IN A COMPLEX WITH GL AND GO.
RX PubMed=9733861; DOI=10.1128/jvi.72.10.8191-8197.1998;
RA Huber M.T., Compton T.;
RT "The human cytomegalovirus UL74 gene encodes the third component of the
RT glycoprotein H-glycoprotein L-containing envelope complex.";
RL J. Virol. 72:8191-8197(1998).
RN [6]
RP IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [7]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(2004).
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). In human cytomegalovirus, forms two
CC distincts complexes to mediate viral entry, a trimer and a pentamer at
CC the surface of the virion envelope. The gH-gL-gO trimer is required for
CC infection in fibroblasts by interacting with host PDGFRA. The gH-gL-
CC UL128-UL130-UL131A pentamer is essential for viral entry in epithelial,
CC endothelial and myeloid cells via interaction with host NRP2 (By
CC similarity). {ECO:0000250|UniProtKB:Q6SW67, ECO:0000255|HAMAP-
CC 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 (By similarity). Forms the envelope pentamer complex (PC) composed of
CC gH, gL, UL128, UL130, and UL131A. The pentamer interacts with host
CC NRP2. Forms the envelope trimer complex composed of gH, gL, and gO
CC (PubMed:9733861). The trimer interacts with host PDGFRA (By
CC similarity). Interacts with UL116 (By similarity).
CC {ECO:0000250|UniProtKB:Q6SW67, ECO:0000255|HAMAP-Rule:MF_04033,
CC ECO:0000269|PubMed:9733861}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:Q6SW67,
CC ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04033}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04033}. Host endosome membrane
CC {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04033}. Note=During virion morphogenesis,
CC this protein probably accumulates in the endosomes and trans-Golgi
CC where secondary envelopment occurs. It is probably transported to the
CC cell surface from where it is endocytosed and directed to the trans-
CC Golgi network (TGN). {ECO:0000250|UniProtKB:Q6SW67}.
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; X17403; CAA35390.1; -; Genomic_DNA.
DR EMBL; M19882; AAA45938.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00171.1; -; Genomic_DNA.
DR PIR; A29888; VGBEHC.
DR SMR; P12824; -.
DR ChEMBL; CHEMBL3988504; -.
DR ABCD; P12824; 2 sequenced antibodies.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
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 Direct protein sequencing;
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; Host-virus interaction;
KW Membrane; Reference proteome; Sialic acid; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..743
FT /note="Envelope glycoprotein H"
FT /id="PRO_0000038255"
FT TOPO_DOM 24..720
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 742..743
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 218..281
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ SEQUENCE 743 AA; 84452 MW; 6D24BC7FEF6821A3 CRC64;
MRPGLPPYLT VFTVYLLSHL PSQRYGADAA SEALDPHAFH LLLNTYGRPI RFLRENTTQC
TYNSSLRNST VVRENAISFN FFQSYNQYYV FHMPRCLFAG PLAEQFLNQV DLTETLERYQ
QRLNTYALVS KDLASYRSFS QQLKAQDSLG QQPTTVPPPI DLSIPHVWMP PQTTPHDWKG
SHTTSGLHRP HFNQTCILFD GHDLLFSTVT PCLHQGFYLM DELRYVKITL TEDFFVVTVS
IDDDTPMLLI FGHLPRVLFK APYQRDNFIL RQTEKHELLV LVKKAQLNRH SYLKDSDFLD
AALDFNYLDL SALLRNSFHR YAVDVLKSGR CQMLDRRTVE MAFAYALALF AAARQEEAGT
EISIPRALDR QAALLQIQEF MITCLSQTPP RTTLLLYPTA VDLAKRALWT PDQITDITSL
VRLVYILSKQ NQQHLIPQWA LRQIADFALQ LHKTHLASFL SAFARQELYL MGSLVHSMLV
HTTERREIFI VETGLCSLAE LSHFTQLLAH PHHEYLSDLY TPCSSSGRRD HSLERLTRLF
PDATVPATVP AALSILSTMQ PSTLETFPDL FCLPLGESFS ALTVSEHVSY VVTNQYLIKG
ISYPVSTTVV GQSLIITQTD SQTKCELTRN MHTTHSITAA LNISLENCAF CQSALLEYDD
TQGVINIMYM HDSDDVLFAL DPYNEVVVSS PRTHYLMLLK NGTVLEVTDV VVDATDSRLL
MMSVYALSAI IGIYLLYRML KTC
