GH_HCMVT
ID GH_HCMVT Reviewed; 742 AA.
AC P17176;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Towne) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10363;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2539698; DOI=10.1016/0042-6822(89)90167-0;
RA Pachl C., Probert W.S., Hermsen K.M., Masiarz F.R., Rasmussen L.,
RA Merigan T.C., Spaete R.R.;
RT "The human cytomegalovirus strain Towne glycoprotein H gene encodes
RT glycoprotein p86.";
RL Virology 169:418-426(1989).
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. The
CC trimer interacts with host PDGFRA (By similarity).
CC {ECO:0000250|UniProtKB:Q6SW67, ECO:0000255|HAMAP-Rule:MF_04033}.
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; M25271; AAA45946.1; -; Genomic_DNA.
DR PIR; A30182; VGBEHT.
DR SMR; P17176; -.
DR PRIDE; P17176; -.
DR ABCD; P17176; 4 sequenced antibodies.
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 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; Host-virus interaction;
KW Membrane; Sialic acid; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral attachment to host entry receptor;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..29
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 30..742
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000038256"
FT TOPO_DOM 30..719
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 741..742
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 217..280
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
SQ SEQUENCE 742 AA; 84275 MW; B5B8011243EE9EA3 CRC64;
MRPGLPSYLI VLAVCLLSHL LSSRYGAEAI SEPLDKAFHL LLNTYGRPIR FLRENTTQCT
YNSSLRNSTV VRENAISFNF FQSYNQYYVF HMPRCLFAGP LAEQFLNQVD LTETLERYQQ
RLNTYALVSK DLASYRSFSQ QLKAQDSLGE QPTTVPPPID LSIPHVWMPP QTTPHGWTES
HTTSGLHRPH FNQTCILFDG HDLLFSTVTP CLHQGFYLID ELRYVKITLT EDFFVVTVSI
DDDTPMLLIF GHLPRVLFKA PYQRDNFILR QTEKHELLVL VKKDQLNRHS YLKDPDFLDA
ALDFNYLDLS ALLRNSFHRY AVDVLKSGRC QMLDRRTVEM AFAYALALFA AARQEEAGAQ
VSVPRALDRQ AALLQIQEFM ITCLSQTPPR TTLLLYPTAV DLAKRALWTP NQITDITSLV
RLVYILSKQN QQHLIPQWAL RQIADFALKL HKTHLASFLS AFARQELYLM GSLVHSMLVH
TTERREIFIV ETGLCSLAEL SHFTQLLAHP HHEYLSDLYT PCSSSGRRDH SLERLTRLFP
DATVPTTVPA ALSILSTMQP STLETFPDLF CLPLGESFSA LTVSEHVSYV VTNQYLIKGI
SYPVSTTVVG QSLIITQTDS QTKCELTRNM HTTHSITAAL NISLENCAFC QSALLEYDDT
QGVINIMYMH DSDDVLFALD PYNEVVVSSP RTHYLMLLKN GTVLEVTDVV VDATDSRLLM
MSVYALSAII GIYLLYRMLK TC
