GH_HHV2H
ID GH_HHV2H Reviewed; 838 AA.
AC P89445;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 76.
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}; ORFNames=UL22;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
RN [2]
RP DISULFIDE BOND.
RX PubMed=15680420; DOI=10.1016/j.virol.2004.12.006;
RA Cairns T.M., Landsburg D.J., Whitbeck J.C., Eisenberg R.J., Cohen G.H.;
RT "Contribution of cysteine residues to the structure and function of herpes
RT simplex virus gH/gL.";
RL Virology 332:550-562(2005).
RN [3]
RP FUNCTION, AND INTERACTION WITH HOST ITGAV AND ITGB3.
RX PubMed=24942591; DOI=10.1128/jvi.00725-14;
RA Cheshenko N., Trepanier J.B., Gonzalez P.A., Eugenin E.A., Jacobs W.R. Jr.,
RA Herold B.C.;
RT "Herpes simplex virus type 2 glycoprotein H interacts with integrin
RT alphavbeta3 to facilitate viral entry and calcium signaling in human
RT genital tract epithelial cells.";
RL J. Virol. 88:10026-10038(2014).
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). Interaction with host integrins
CC ITGAV/ITGB3 triggers release of cytosolic Ca(2+) and FAK
CC phosphorylation leading to efficient viral entry into host genital
CC tract epithelial cells (PubMed:24942591). {ECO:0000255|HAMAP-
CC Rule:MF_04033, ECO:0000269|PubMed:24942591}.
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 Interacts with host integrins ITGAV/ITGB3 to mediate viral entry into
CC epithelial cells. {ECO:0000255|HAMAP-Rule:MF_04033,
CC ECO:0000269|PubMed:24942591}.
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; Z86099; CAB06746.1; -; Genomic_DNA.
DR PDB; 3M1C; X-ray; 3.00 A; A=48-803.
DR PDBsum; 3M1C; -.
DR SMR; P89445; -.
DR PRIDE; P89445; -.
DR EvolutionaryTrace; P89445; -.
DR Proteomes; UP000001874; 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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond;
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 envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 19..838
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000436657"
FT TOPO_DOM 21..803
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 825..838
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 171..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..323
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT COMPBIAS 172..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT DISULFID 258..429
FT /evidence="ECO:0000305|PubMed:15680420"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3M1C"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:3M1C"
FT TURN 97..101
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:3M1C"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 246..258
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 281..290
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 352..364
FT /evidence="ECO:0007829|PDB:3M1C"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 376..400
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 405..425
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 443..463
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 467..480
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 483..506
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 513..531
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 537..553
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 556..572
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 582..585
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 588..591
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 600..608
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 617..635
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 638..644
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 662..665
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 672..678
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 681..687
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 698..702
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 733..737
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 743..748
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 752..759
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 776..781
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 787..789
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 791..793
FT /evidence="ECO:0007829|PDB:3M1C"
SQ SEQUENCE 838 AA; 89705 MW; AC92B7975779C4A6 CRC64;
MGPGLWVVMG VLVGVAGGHD TYWTEQIDPW FLHGLGLART YWRDTNTGRL WLPNTPDASD
PQRGRLAPPG ELNLTTASVP MLRWYAERFC FVLVTTAEFP RDPGQLLYIP KTYLLGRPRN
ASLPELPEAG PTSRPPAEVT QLKGLSHNPG ASALLRSRAW VTFAAAPDRE GLTFPRGDDG
ATERHPDGRR NAPPPGPPAG TPRHPTTNLS IAHLHNASVT WLAARGLLRT PGRYVYLSPS
ASTWPVGVWT TGGLAFGCDA ALVRARYGKG FMGLVISMRD SPPAEIIVVP ADKTLARVGN
PTDENAPAVL PGPPAGPRYR VFVLGAPTPA DNGSALDALR RVAGYPEEST NYAQYMSRAY
AEFLGEDPGS GTDARPSLFW RLAGLLASSG FAFVNAAHAH DAIRLSDLLG FLAHSRVLAG
LAARGAAGCA ADSVFLNVSV LDPAARLRLE ARLGHLVAAI LEREQSLVAH ALGYQLAFVL
DSPAAYGAVA PSAARLIDAL YAEFLGGRAL TAPMVRRALF YATAVLRAPF LAGAPSAEQR
ERARRGLLIT TALCTSDVAA ATHADLRAAL ARTDHQKNLF WLPDHFSPCA ASLRFDLAEG
GFILDALAMA TRSDIPADVM AQQTRGVASV LTRWAHYNAL IRAFVPEATH QCSGPSHNAE
PRILVPITHN ASYVVTHTPL PRGIGYKLTG VDVRRPLFIT YLTATCEGHA REIEPKRLVR
TENRRDLGLV GAVFLRYTPA GEVMSVLLVD TDATQQQLAQ GPVAGTPNVF SSDVPSVALL
LFPNGTVIHL LAFDTLPIAT IAPGFLAASA LGVVMITAAL AGILRVVRTC VPFLWRRE
