GH_SUHVK
ID GH_SUHVK Reviewed; 686 AA.
AC P27416;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 84.
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};
OS Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS Kaplan)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=33703;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1850925; DOI=10.1016/0042-6822(91)90614-h;
RA Klupp B.G., Mettenleiter T.C.;
RT "Sequence and expression of the glycoprotein gH gene of pseudorabies
RT virus.";
RL Virology 182:732-741(1991).
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. {ECO:0000255|HAMAP-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 {ECO:0000255|HAMAP-Rule:MF_04033}.
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; M61196; AAA47466.1; -; Genomic_DNA.
DR PIR; A39990; VGBEPK.
DR RefSeq; YP_068353.1; NC_006151.1.
DR PDB; 2XQY; X-ray; 2.05 A; A/E=107-639.
DR PDBsum; 2XQY; -.
DR SMR; P27416; -.
DR ABCD; P27416; 1 sequenced antibody.
DR GeneID; 2952560; -.
DR KEGG; vg:2952560; -.
DR EvolutionaryTrace; P27416; -.
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; 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; Sialic acid;
KW Signal; Transmembrane; Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 25..686
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000038249"
FT TOPO_DOM 25..646
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 668..686
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 157..217
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 223..238
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 243..259
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 263..286
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 295..312
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 352..367
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 374..387
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 392..403
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 406..420
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 455..463
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 487..491
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 500..504
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 506..516
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 574..579
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 584..589
FT /evidence="ECO:0007829|PDB:2XQY"
FT HELIX 593..600
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 619..624
FT /evidence="ECO:0007829|PDB:2XQY"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:2XQY"
SQ SEQUENCE 686 AA; 71952 MW; 08A149FF77BA4AAF CRC64;
MPASSVRLPL RLLTLAGLLA LAGAAALARG APQGGPPSPQ GGPAPTAAPA RGPTLFVLVG
DGSAWFVFQL GGLGALNDTR IRGHLLGRYL VSYQVVPPPV SAWYFVQRPR ERPRLSGPPS
GAELVAFDAP GVRRTYTTAA VWPAEVAVLA DAEARCPAAV FNVTLGEAFL GLRVALRSFL
PLEVIISAER MRMIAPPALG SDLEPPGPPA GRFHVYTLGF LSDGAMHQTM RDVAAYVHES
DDYLAQLSAA HAAALAAVVQ PGPYYFYRAA VRLGVAAFVF SEAARRDRRA SAPALLRVES
DARLLSRLLM RAAGCPAGFA GLFDGRAERV PVAPADQLRA AWTFGEDPAP RLDLARATVA
EAYRRSVRGK PFDQQALFFA VALLLRAGGP GDARETLLRT TAMCTAERAA AAAELTRAAL
SPTAAWNEPF SLLDVLSPCA VSLRRDLGGD ATLANLGAAA RLALAPAGAP GAAAATDEGA
EEEEEDPVAR AAPEIPAEAL LALPLRGGAS FVFTRRRPDC GPAYTLGGVD IANPLVLAIV
SNDSAACDYT DRMPESQHLP ATDNPSVCVY CDCVFVRYSS AGTILETVLI ESKDMEEQLM
AGANSTIPSF NPTLHGGDVK ALMLFPNGTV VDLLSFTSTR LAPVSPAYVV ASVVGAAITV
GILYALFKML CSFSSEGYSR LINARS
