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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)DescriptionActionsGraphical viewLength
Metal bindingi64Zinc; shared with dimeric partnerCombined sources1 Publication1
Metal bindingi240Zinc; shared with dimeric partnerCombined sources1 Publication1

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)DescriptionActionsGraphical viewLength
Topological domaini26 – 339Virion surfaceSequence analysisAdd BLAST314
Transmembranei340 – 364HelicalSequence analysisAdd BLAST25
Topological domaini365 – 394IntravirionSequence analysisAdd BLAST30

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi62V → C: Impaired virus entry into host cell; when associated with C-327. Inability of the corresponding soluble gD to bind TNFRSF14 and NECTIN1. 1 Publication1
Mutagenesisi319W → A: Impaired virus entry into host cell. 1 Publication1
Mutagenesisi327A → C: Impaired virus entry into host cell; when associated with C-62. Inability of the corresponding soluble gD to bind TNFRSF14 and NECTIN1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000003821426 – 394Envelope glycoprotein DAdd BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi91 ↔ 214Combined sources2 Publications
Glycosylationi119N-linked (GlcNAc...); by hostCombined sources2 Publications1
Disulfide bondi131 ↔ 227Combined sources2 Publications
Disulfide bondi143 ↔ 152Combined sources2 Publications
Glycosylationi146N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi287N-linked (GlcNAc...); by hostSequence analysis1

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 interactor.
MINTiMINT-207993.

Structurei

Secondary structure

1394
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 35Combined sources4
Turni39 – 41Combined sources3
Beta strandi45 – 47Combined sources3
Beta strandi60 – 63Combined sources4
Beta strandi65 – 68Combined sources4
Beta strandi82 – 87Combined sources6
Beta strandi92 – 96Combined sources5
Helixi102 – 107Combined sources6
Helixi111 – 114Combined sources4
Beta strandi118 – 128Combined sources11
Beta strandi131 – 143Combined sources13
Beta strandi153 – 156Combined sources4
Beta strandi159 – 162Combined sources4
Turni164 – 166Combined sources3
Beta strandi167 – 169Combined sources3
Beta strandi176 – 180Combined sources5
Helixi183 – 185Combined sources3
Beta strandi187 – 195Combined sources9
Beta strandi198 – 212Combined sources15
Helixi224 – 226Combined sources3
Helixi230 – 235Combined sources6
Turni239 – 243Combined sources5
Helixi250 – 264Combined sources15
Beta strandi276 – 278Combined sources3
Helixi280 – 283Combined sources4
Helixi298 – 301Combined sources4
Beta strandi306 – 308Combined sources3
Beta strandi326 – 330Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP57083.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni25 – 57Interaction with TNFRSF14Add BLAST33
Regioni261 – 305ProfusionBy similarityAdd BLAST45

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi365 – 381Arg/Lys-rich (highly basic; probably serves to anchor the glycoprotein in the membrane)Add BLAST17

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP57083. 1 interactor.
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: November 2, 2016
This is version 90 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.