P10228 (GC_HHV11) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 75.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glycoprotein C Short name=gC | ||||
| Gene names |
| ||||
| Organism | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome] | ||||
| Taxonomic identifier | 10299 [NCBI] | ||||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus › ![]() | ||||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 511 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Major attachment protein that mediates binding of the virus to cell surface heparan sulfate or chondroitin sulfate. Plays also several roles in host immune evasion by inhibiting the host complement cascade activation, and by providing a shield against neutralizing antibodies that interfere with gB-gD, gB-gH/gL or gD-gH/gL interactions By similarity. |
| Subunit structure | Interacts with host complement component C3b; this interaction inhibits host immune response by disregulating complement cascade. Ref.2 |
| Subcellular location | Virion membrane; Single-pass membrane protein Potential. |
| Miscellaneous | There are seven external glycoproteins in HSV-1 and 2: gH, gB, gC, gG, gD, gI, and gE. |
| Sequence similarities | Belongs to the herpesviridae glycoprotein C family. Contains 1 Ig-like (immunoglobulin-like) domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Host-virus interaction Inhibition of host complement factors by virus Viral attachment to host cell Viral immunoevasion Virus entry into host cell |
| Cellular component | Membrane Virion |
| Coding sequence diversity | Alternative initiation Alternative splicing |
| Domain | Immunoglobulin domain Signal Transmembrane Transmembrane helix |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | suppression by virus of host complement activation Inferred from electronic annotation. Source: UniProtKB-KW viral attachment to host cellInferred from electronic annotation. Source: UniProtKB-KW viral entry into host cellInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW virion membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing and alternative initiation. [Align] [Select] | ||||||
| Isoform gC (identifier: P10228-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Note: Membrane-bound gC. | ||||||
| Isoform gCsec (identifier: P10228-2) The sequence of this isoform differs from the canonical sequence as follows: 472-511: VIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR → VILGRSRTTHGVEQNASP | ||||||
| Note: Secreted. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | Potential | ||||||||
| Chain | 25 – 511 | 487 | Glycoprotein C | PRO_0000038197 | |||||||
Regions | |||||||||||
| Topological domain | 25 – 480 | 456 | Virion surface Potential | ||||||||
| Transmembrane | 481 – 497 | 17 | Helical; Potential | ||||||||
| Topological domain | 498 – 511 | 14 | Cytoplasmic Potential | ||||||||
| Domain | 267 – 359 | 93 | Ig-like | ||||||||
| Region | 137 – 151 | 15 | Heparin-binding domain By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 42 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||
| Glycosylation | 70 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||
| Glycosylation | 74 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||
| Glycosylation | 108 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||
| Glycosylation | 148 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||
| Glycosylation | 181 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||
| Glycosylation | 197 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||
| Glycosylation | 362 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||
| Disulfide bond | 127 ↔ 144 | Ref.3 | |||||||||
| Disulfide bond | 286 ↔ 347 | Ref.3 | |||||||||
| Disulfide bond | 386 ↔ 442 | Ref.3 | |||||||||
| Disulfide bond | 390 ↔ 419 | Ref.3 | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 472 – 511 | 40 | VIEAI…QRHRR → VILGRSRTTHGVEQNASP in isoform gCsec. | VSP_040892 | |||||||
Sequences
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References
| [1] | "The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1." McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P. J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complement component C3b binds directly to purified glycoprotein C of herpes simplex virus types 1 and 2." Eisenberg R.J., Ponce de Leon M., Friedman H.M., Fries L.F., Frank M.M., Hastings J.C., Cohen G.H. Microb. Pathog. 3:423-435(1987) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HOST C3. |
| [3] | "Disulfide bond structure determination and biochemical analysis of glycoprotein C from herpes simplex virus." Rux A.H., Moore W.T., Lambris J.D., Abrams W.R., Peng C., Friedman H.M., Cohen G.H., Eisenberg R.J. J. Virol. 70:5455-5465(1996) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X14112 Genomic DNA. Translation: CAA32294.1. |
| PIR | VGBEF4. H30088. |
| RefSeq | NP_044646.1. NC_001806.1. |
3D structure databases | |
| ProteinModelPortal | P10228. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2703410. |
Phylogenomic databases | |
| ProtClustDB | PHA3270. |
Family and domain databases | |
| Gene3D | 2.60.40.10. 1 hit. |
| InterPro | IPR001038. GA_GC. IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. [Graphical view] |
| Pfam | PF02124. Marek_A. 1 hit. [Graphical view] |
| PRINTS | PR00668. GLYCPROTEINC. |
| PROSITE | PS50835. IG_LIKE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GC_HHV11 | ||||||||
| Accession | Primary (citable) accession number: P10228 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
