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Protein

Envelope glycoprotein D

Gene

gD

Organism
Human herpesvirus 1 (strain Patton) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Envelope glycoprotein that binds to the potential host cell entry receptors TNFRSF14/HVEM, NECTIN1 and 3-O-sulfated heparan sulfate. May trigger fusion with host membrane, by recruiting the fusion machinery composed of gB and gH/gL (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Zinc; shared with dimeric partnerCombined sources1 Publication
Metal bindingi240 – 2401Zinc; shared with dimeric partnerCombined sources1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Viral attachment to host entry receptor, Virus entry into host cell

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein D
Short name:
gD
Gene namesi
Name:gD
Synonyms:US6
OrganismiHuman herpesvirus 1 (strain Patton) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10308 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 339314Virion surfaceSequence analysisAdd
BLAST
Transmembranei340 – 36425HelicalSequence analysisAdd
BLAST
Topological domaini365 – 39430IntravirionSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 621V → C: Impaired virus entry into host cell; when associated with C-327. Inability of the corresponding soluble gD to bind TNFRSF14 and NECTIN1. 1 Publication
Mutagenesisi319 – 3191W → A: Impaired virus entry into host cell. 1 Publication
Mutagenesisi327 – 3271A → C: Impaired virus entry into host cell; when associated with C-62. Inability of the corresponding soluble gD to bind TNFRSF14 and NECTIN1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 394369Envelope glycoprotein DPRO_0000038214Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 214Combined sources2 Publications
Glycosylationi119 – 1191N-linked (GlcNAc...); by hostCombined sources2 Publications
Disulfide bondi131 ↔ 227Combined sources2 Publications
Disulfide bondi143 ↔ 152Combined sources2 Publications
Glycosylationi146 – 1461N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi287 – 2871N-linked (GlcNAc...); by hostSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with host receptor TNFRSF14. Interacts with host receptor NECTIN1. Interacts (via profusion domain) with gB; this interaction occurs in the absence of gH/gL. Interacts (via profusion domain) with gH/gL heterodimer; this interaction occurs in the absence of gB. Associates with the gB-gH/gL-gD complex. Interacts (via C-terminus) with UL11 tegument protein (By similarity).By similarity

Protein-protein interaction databases

IntActiP57083. 1 interaction.
MINTiMINT-207993.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 354Combined sources
Turni39 – 413Combined sources
Beta strandi45 – 473Combined sources
Beta strandi60 – 634Combined sources
Beta strandi65 – 684Combined sources
Beta strandi82 – 876Combined sources
Beta strandi92 – 965Combined sources
Helixi102 – 1076Combined sources
Helixi111 – 1144Combined sources
Beta strandi118 – 12811Combined sources
Beta strandi131 – 14313Combined sources
Beta strandi153 – 1564Combined sources
Beta strandi159 – 1624Combined sources
Turni164 – 1663Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi176 – 1805Combined sources
Helixi183 – 1853Combined sources
Beta strandi187 – 1959Combined sources
Beta strandi198 – 21215Combined sources
Helixi224 – 2263Combined sources
Helixi230 – 2356Combined sources
Turni239 – 2435Combined sources
Helixi250 – 26415Combined sources
Beta strandi276 – 2783Combined sources
Helixi280 – 2834Combined sources
Helixi298 – 3014Combined sources
Beta strandi306 – 3083Combined sources
Beta strandi326 – 3305Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JMAX-ray2.65A26-310[»]
1L2GX-ray2.85A/B/C/D26-310[»]
2C36X-ray2.11A/B48-332[»]
2C3AX-ray2.50A/B47-332[»]
ProteinModelPortaliP57083.
SMRiP57083. Positions 26-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP57083.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 5733Interaction with TNFRSF14Add
BLAST
Regioni261 – 30545ProfusionBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi365 – 38117Arg/Lys-rich (highly basic; probably serves to anchor the glycoprotein in the membrane)Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR002896. Herpes_glycop_dom.
IPR007110. Ig-like_dom.
[Graphical view]
PfamiPF01537. Herpes_glycop_D. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P57083-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGTAARLGA VILFVVIVGL HGVRGKYALA DASLKMADPN RFRGKDLPVL
60 70 80 90 100
DQLTDPPGVR RVYHIQAGLP DPFQPPSLPI TVYYAVLERA CRSVLLNAPS
110 120 130 140 150
EAPQIVRGAS EDVRKQPYNL TIAWFRMGGN CAIPITVMEY TECSYNKSLG
160 170 180 190 200
ACPIRTQPRW NYYDSFSAVS EDNLGFLMHA PAFETAGTYL RLVKINDWTE
210 220 230 240 250
ITQFILEHRA KGSCKYALPL RIPPSACLSP QAYQQGVTVD SIGMLPRFIP
260 270 280 290 300
ENQRTVAVYS LKIAGWHGPK APYTSTLLPP ELSETPNATQ PELAPEDPED
310 320 330 340 350
SALLEDPVGT VAPQIPPNWH IPSIQDAATP YHPPATPNNM GLIAGAVGGS
360 370 380 390
LLAALVICGI VYWMHRRTRK APKRIRLPHI REDDQPSSHQ PLFY
Length:394
Mass (Da):43,347
Last modified:July 21, 1986 - v1
Checksum:i052ABB5F53033D5E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02138 Genomic DNA. Translation: CAA26060.1.
J02217 Genomic DNA. Translation: AAA45785.1.
PIRiA94268. VGBED1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02138 Genomic DNA. Translation: CAA26060.1.
J02217 Genomic DNA. Translation: AAA45785.1.
PIRiA94268. VGBED1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JMAX-ray2.65A26-310[»]
1L2GX-ray2.85A/B/C/D26-310[»]
2C36X-ray2.11A/B48-332[»]
2C3AX-ray2.50A/B47-332[»]
ProteinModelPortaliP57083.
SMRiP57083. Positions 26-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP57083. 1 interaction.
MINTiMINT-207993.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP57083.

Family and domain databases

InterProiIPR002896. Herpes_glycop_dom.
IPR007110. Ig-like_dom.
[Graphical view]
PfamiPF01537. Herpes_glycop_D. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGD_HHV1P
AccessioniPrimary (citable) accession number: P57083
Secondary accession number(s): P03171
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 11, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.